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(3Z)-phycocyanobilin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
biliverdin IXa + reduced ferredoxin
(3Z)-phycocyanobilin + oxidized ferredoxin
biliverdin IXa diamide + reduced ferredoxin
? + oxidized ferredoxin
biliverdin IXalpha + 4 reduced ferredoxin
(3Z)-phycocyanobilin + 4 oxidized ferredoxin
biliverdin IXalpha + reduced ferredoxin
(3E)-phycocyanobilin + oxidized ferredoxin
-
Synechococcus ferredoxin
-
-
?
biliverdin Ixalpha + reduced ferredoxin
(3Z)-phycocyanobilin + oxidized ferredoxin
biliverdin IXalpha + reduced ferredoxin
phycocyanobilin + oxidized ferredoxin
biliverdin IXalpha 12-monoamide + reduced ferredoxin
phycocyanobilin 12-monoamide + oxidized ferredoxin
biliverdin IXalpha 8-monoamide + reduced ferredoxin
phycocyanobilin 8-monoamide + oxidized ferredoxin
-
-
products are corresponding phycocyanobilin monoamides with a mix of the 3E and 3Z forms
-
?
biliverdin XIII + reduced ferredoxin
phycocyanobilin + oxidized ferredoxin
-
-
biliverdin XIII contains two endovinyl groups, so PcyA can convert either (or both) to an ethylidene
-
?
biliverdin XIIIalpha + reduced ferredoxin
(3E)-isophytochromobilin + oxidized ferredoxin
biliverdin XIIIalpha + reduced ferredoxin
(3Z)-isophytochromobilin + oxidized ferredoxin
biliverdin XIIIalpha + reduced ferredoxin
? + oxidized ferredoxin
biliverdin XIIIalpha monoamide + reduced ferredoxin
? + oxidized ferredoxin
-
-
mixture of products
-
?
additional information
?
-
(3Z)-phycocyanobilin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
-
-
-
?
(3Z)-phycocyanobilin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
-
-
-
-
?
(3Z)-phycocyanobilin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
-
(3Z)-phytochromobilin is involved as intermediate
-
?
(3Z)-phycocyanobilin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
-
-
?
(3Z)-phycocyanobilin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
-
-
-
?
(3Z)-phycocyanobilin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
-
-
-
?
(3Z)-phycocyanobilin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
-
-
-
?
(3Z)-phycocyanobilin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
-
-
-
?
(3Z)-phycocyanobilin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
-
-
-
-
?
(3Z)-phycocyanobilin + oxidized ferredoxin
biliverdin IXa + reduced ferredoxin
-
-
?
biliverdin IXa + reduced ferredoxin
(3Z)-phycocyanobilin + oxidized ferredoxin
-
-
-
-
?
biliverdin IXa + reduced ferredoxin
(3Z)-phycocyanobilin + oxidized ferredoxin
-
-
-
-
?
biliverdin IXa + reduced ferredoxin
(3Z)-phycocyanobilin + oxidized ferredoxin
-
-
-
-
?
biliverdin IXa + reduced ferredoxin
(3Z)-phycocyanobilin + oxidized ferredoxin
-
-
-
-
?
biliverdin IXa + reduced ferredoxin
(3Z)-phycocyanobilin + oxidized ferredoxin
-
-
-
-
?
biliverdin IXa + reduced ferredoxin
(3Z)-phycocyanobilin + oxidized ferredoxin
-
-
-
-
?
biliverdin IXa diamide + reduced ferredoxin
? + oxidized ferredoxin
-
activity only at pH 6.0
-
-
?
biliverdin IXa diamide + reduced ferredoxin
? + oxidized ferredoxin
-
activity only at pH 6.0
-
-
?
biliverdin IXalpha + 4 reduced ferredoxin
(3Z)-phycocyanobilin + 4 oxidized ferredoxin
-
-
-
?
biliverdin IXalpha + 4 reduced ferredoxin
(3Z)-phycocyanobilin + 4 oxidized ferredoxin
via the intermediate 181,182-dihydrobiliverdin (181/182-DHBV)
-
-
?
biliverdin IXalpha + 4 reduced ferredoxin
(3Z)-phycocyanobilin + 4 oxidized ferredoxin
via the intermediate 181/182-dihydrobiliverdin (181/182-DHBV)
-
-
?
biliverdin IXalpha + 4 reduced ferredoxin
(3Z)-phycocyanobilin + 4 oxidized ferredoxin
-
-
-
?
biliverdin IXalpha + 4 reduced ferredoxin
(3Z)-phycocyanobilin + 4 oxidized ferredoxin
via the intermediate 181,182-dihydrobiliverdin (181/182-DHBV)
-
-
?
biliverdin IXalpha + 4 reduced ferredoxin
(3Z)-phycocyanobilin + 4 oxidized ferredoxin
via the intermediate 181/182-dihydrobiliverdin (181/182-DHBV)
-
-
?
biliverdin IXalpha + 4 reduced ferredoxin
(3Z)-phycocyanobilin + 4 oxidized ferredoxin
-
-
-
?
biliverdin IXalpha + 4 reduced ferredoxin
(3Z)-phycocyanobilin + 4 oxidized ferredoxin
-
-
-
?
biliverdin IXalpha + 4 reduced ferredoxin
(3Z)-phycocyanobilin + 4 oxidized ferredoxin
-
-
-
?
biliverdin IXalpha + 4 reduced ferredoxin
(3Z)-phycocyanobilin + 4 oxidized ferredoxin
via reaction intermediate 181,182-difydrobiliverdin (18EtBV)
-
-
?
biliverdin Ixalpha + reduced ferredoxin
(3Z)-phycocyanobilin + oxidized ferredoxin
-
-
-
-
?
biliverdin Ixalpha + reduced ferredoxin
(3Z)-phycocyanobilin + oxidized ferredoxin
-
spinach or Synechococcus ferredoxin
pigment I is a bona fide intermediate
-
?
biliverdin Ixalpha + reduced ferredoxin
(3Z)-phycocyanobilin + oxidized ferredoxin
-
Synechococcus ferredoxin
-
-
?
biliverdin Ixalpha + reduced ferredoxin
(3Z)-phycocyanobilin + oxidized ferredoxin
-
-
-
-
?
biliverdin Ixalpha + reduced ferredoxin
(3Z)-phycocyanobilin + oxidized ferredoxin
-
phycocyanobilin:ferredoxin oxidoreductase uses four electrons from reduced ferredoxin to synthesize phycocyanobilin by regiospecific reduction of the exo vinyl group of ring D and the endo vinyl group of ring A of biliverdin IXalpha
-
-
?
biliverdin Ixalpha + reduced ferredoxin
(3Z)-phycocyanobilin + oxidized ferredoxin
-
-
-
-
?
biliverdin Ixalpha + reduced ferredoxin
(3Z)-phycocyanobilin + oxidized ferredoxin
-
-
-
-
?
biliverdin Ixalpha + reduced ferredoxin
(3Z)-phycocyanobilin + oxidized ferredoxin
-
phycocyanobilin:ferredoxin oxidoreductase uses four electrons from reduced ferredoxin to synthesize phycocyanobilin by regiospecific reduction of the exo vinyl group of ring D and the endo vinyl group of ring A of biliverdin IXalpha
-
-
?
biliverdin Ixalpha + reduced ferredoxin
(3Z)-phycocyanobilin + oxidized ferredoxin
-
-
-
-
?
biliverdin Ixalpha + reduced ferredoxin
(3Z)-phycocyanobilin + oxidized ferredoxin
-
-
-
?
biliverdin Ixalpha + reduced ferredoxin
(3Z)-phycocyanobilin + oxidized ferredoxin
-
-
-
-
?
biliverdin Ixalpha + reduced ferredoxin
(3Z)-phycocyanobilin + oxidized ferredoxin
proton-donating role of the carboxylic acid side chain of residue Glu76 for exo-vinyl reduction, structural basis for the reduction regiospecificity of PcyA, overview
-
-
?
biliverdin Ixalpha + reduced ferredoxin
(3Z)-phycocyanobilin + oxidized ferredoxin
-
PcyA catalyzes the multi-step reduction of biliverdin IXalpha to produce 3Z/3E-phycocyanobilin
-
-
?
biliverdin Ixalpha + reduced ferredoxin
(3Z)-phycocyanobilin + oxidized ferredoxin
-
recombinant Synechocystis sp. PCC7002 ferredoxin
-
-
?
biliverdin Ixalpha + reduced ferredoxin
(3Z)-phycocyanobilin + oxidized ferredoxin
Thermosynechococcus vestitus
-
-
-
-
?
biliverdin IXalpha + reduced ferredoxin
phycocyanobilin + oxidized ferredoxin
-
-
with biliverdins containing a single endovinyl group, such as BV IXalpha, PcyA can generate a mixture of 3E and 3Z products
-
?
biliverdin IXalpha + reduced ferredoxin
phycocyanobilin + oxidized ferredoxin
-
recombinant ferredoxin from Synechococcus sp. PCC7002
with biliverdins containing a single endovinyl group, such as BV IXalpha, PcyA can generate a mixture of 3E and 3Z products
-
?
biliverdin IXalpha + reduced ferredoxin
phycocyanobilin + oxidized ferredoxin
-
-
with biliverdins containing a single endovinyl group, such as BV IXalpha, PcyA can generate a mixture of 3E and 3Z products
-
?
biliverdin IXalpha + reduced ferredoxin
phycocyanobilin + oxidized ferredoxin
-
recombinant ferredoxin from Synechococcus sp. PCC7002
with biliverdins containing a single endovinyl group, such as BV IXalpha, PcyA can generate a mixture of 3E and 3Z products
-
?
biliverdin IXalpha + reduced ferredoxin
phycocyanobilin + oxidized ferredoxin
-
-
-
?
biliverdin IXalpha 12-monoamide + reduced ferredoxin
phycocyanobilin 12-monoamide + oxidized ferredoxin
-
-
products are corresponding phycocyanobilin monoamides with a mix of the 3E and 3Z forms
-
?
biliverdin IXalpha 12-monoamide + reduced ferredoxin
phycocyanobilin 12-monoamide + oxidized ferredoxin
-
-
products are corresponding phycocyanobilin monoamides with a mix of the 3E and 3Z forms
-
?
biliverdin XIIIalpha + reduced ferredoxin
(3E)-isophytochromobilin + oxidized ferredoxin
-
-
-
-
?
biliverdin XIIIalpha + reduced ferredoxin
(3E)-isophytochromobilin + oxidized ferredoxin
-
Synechococcus ferredoxin
-
-
?
biliverdin XIIIalpha + reduced ferredoxin
(3Z)-isophytochromobilin + oxidized ferredoxin
-
-
-
-
?
biliverdin XIIIalpha + reduced ferredoxin
(3Z)-isophytochromobilin + oxidized ferredoxin
-
Synechococcus ferredoxin
-
-
?
biliverdin XIIIalpha + reduced ferredoxin
? + oxidized ferredoxin
-
-
-
?
biliverdin XIIIalpha + reduced ferredoxin
? + oxidized ferredoxin
a synthetic substrate that lacks an exo-vinyl group
-
-
?
additional information
?
-
-
semisynthesis of mono- and diamides of biliverdin IXalpha, that function as substrates. The enzyme is accommodating to amidation of the propionic acid side chains of biliverdin IXalpha, which does not require free carboxylic acid side chains to yield its phytobilin product, phycocyanobilin. Bilin amides are assembled with BV-type apophytochromes, demonstrating a role for the 8-propionate in the formation of the spectroscopically native Pr dark states of the biliprotein photosensors. Neither ionizable propionate side chain proves to be essential to primary photoisomerization for BV-type phytochrome. No activity with biliverdin XIIIalpha diamide , but biliverdinXIII diacid is converted into the iso-PthetaB product with moderate yield
-
-
?
additional information
?
-
-
semisynthesis of mono- and diamides of biliverdin IXalpha, that function as substrates. The enzyme is accommodating to amidation of the propionic acid side chains of biliverdin IXalpha, which does not require free carboxylic acid side chains to yield its phytobilin product, phycocyanobilin. Bilin amides are assembled with BV-type apophytochromes, demonstrating a role for the 8-propionate in the formation of the spectroscopically native Pr dark states of the biliprotein photosensors. Neither ionizable propionate side chain proves to be essential to primary photoisomerization for BV-type phytochrome. No activity with biliverdin XIIIalpha diamide , but biliverdinXIII diacid is converted into the iso-PthetaB product with moderate yield
-
-
?
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biliverdin IXalpha + 4 reduced ferredoxin
(3Z)-phycocyanobilin + 4 oxidized ferredoxin
biliverdin Ixalpha + reduced ferredoxin
(3Z)-phycocyanobilin + oxidized ferredoxin
biliverdin IXalpha + reduced ferredoxin
phycocyanobilin + oxidized ferredoxin
biliverdin IXalpha + 4 reduced ferredoxin
(3Z)-phycocyanobilin + 4 oxidized ferredoxin
-
-
-
?
biliverdin IXalpha + 4 reduced ferredoxin
(3Z)-phycocyanobilin + 4 oxidized ferredoxin
-
-
-
?
biliverdin IXalpha + 4 reduced ferredoxin
(3Z)-phycocyanobilin + 4 oxidized ferredoxin
-
-
-
?
biliverdin IXalpha + 4 reduced ferredoxin
(3Z)-phycocyanobilin + 4 oxidized ferredoxin
-
-
-
?
biliverdin IXalpha + 4 reduced ferredoxin
(3Z)-phycocyanobilin + 4 oxidized ferredoxin
-
-
-
?
biliverdin Ixalpha + reduced ferredoxin
(3Z)-phycocyanobilin + oxidized ferredoxin
-
-
-
-
?
biliverdin Ixalpha + reduced ferredoxin
(3Z)-phycocyanobilin + oxidized ferredoxin
-
-
-
-
?
biliverdin Ixalpha + reduced ferredoxin
(3Z)-phycocyanobilin + oxidized ferredoxin
-
-
-
-
?
biliverdin Ixalpha + reduced ferredoxin
(3Z)-phycocyanobilin + oxidized ferredoxin
-
-
-
-
?
biliverdin Ixalpha + reduced ferredoxin
(3Z)-phycocyanobilin + oxidized ferredoxin
-
-
-
-
?
biliverdin Ixalpha + reduced ferredoxin
(3Z)-phycocyanobilin + oxidized ferredoxin
-
-
-
?
biliverdin Ixalpha + reduced ferredoxin
(3Z)-phycocyanobilin + oxidized ferredoxin
-
-
-
-
?
biliverdin Ixalpha + reduced ferredoxin
(3Z)-phycocyanobilin + oxidized ferredoxin
-
PcyA catalyzes the multi-step reduction of biliverdin IXalpha to produce 3Z/3E-phycocyanobilin
-
-
?
biliverdin Ixalpha + reduced ferredoxin
(3Z)-phycocyanobilin + oxidized ferredoxin
Thermosynechococcus vestitus
-
-
-
-
?
biliverdin IXalpha + reduced ferredoxin
phycocyanobilin + oxidized ferredoxin
-
-
with biliverdins containing a single endovinyl group, such as BV IXalpha, PcyA can generate a mixture of 3E and 3Z products
-
?
biliverdin IXalpha + reduced ferredoxin
phycocyanobilin + oxidized ferredoxin
-
-
with biliverdins containing a single endovinyl group, such as BV IXalpha, PcyA can generate a mixture of 3E and 3Z products
-
?
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evolution
-
comparison and discrimination of two bilin reductase families in bilin amide usage for photoconversions of BV-type and phytobilin-type phytochromes, mechanistic differences, overview
evolution
-
synthesis of linear tetrapyrrole chromophores in cyanobacteria, algae, and plants, ooverview
evolution
-
the enzyme is a member of the ferredoxin-dependent biliverdin reductase (FDBR) family
evolution
Acaryochloris marina strain 11017 evolved to utilize specific PcyA enzymes for sensing wide range of spectrum upon both PCB and 181/182-DHBV binding and harvesting short-wavelength orange light upon only PCB binding. Phycocyanin a from Acaryochloris marina strain 11017 binds only phycocyanobilin (PCB) but not 181/182-DHBV
evolution
Acaryochloris marina strain 11017 evolved to utilize specific PcyA enzymes for sensing wide range of spectrum upon both PCB and 181/182-DHBV binding and harvesting shortwavelength orange light upon only PCB binding. Phycocyanin a from Acaryochloris marina strain 11017 binds only phycocyanobilin (PCB) but not 181/182-DHBV
evolution
phycocyanobilin:ferredoxin oxidoreductase (PcyA) is a member of the ferredoxin-dependent bilin reductase (FDBR) family
evolution
-
comparison and discrimination of two bilin reductase families in bilin amide usage for photoconversions of BV-type and phytobilin-type phytochromes, mechanistic differences, overview
-
evolution
-
synthesis of linear tetrapyrrole chromophores in cyanobacteria, algae, and plants, ooverview
-
evolution
-
Acaryochloris marina strain 11017 evolved to utilize specific PcyA enzymes for sensing wide range of spectrum upon both PCB and 181/182-DHBV binding and harvesting short-wavelength orange light upon only PCB binding. Phycocyanin a from Acaryochloris marina strain 11017 binds only phycocyanobilin (PCB) but not 181/182-DHBV
-
evolution
-
Acaryochloris marina strain 11017 evolved to utilize specific PcyA enzymes for sensing wide range of spectrum upon both PCB and 181/182-DHBV binding and harvesting shortwavelength orange light upon only PCB binding. Phycocyanin a from Acaryochloris marina strain 11017 binds only phycocyanobilin (PCB) but not 181/182-DHBV
-
malfunction
-
because PcyA and PebA, EC 1.3.7.6/1.3.7.3, utilize the same substrate, biliverdin IXalpha, severe overexpression of pebA can limit the availability of phycocyanobilin, which appears to be required for viability when cells are grown in continuous light
malfunction
both the pcya1-1 mutant with the C-terminal extension of PCYA1 eliminated and efficient knockdown of PCYA1 expression by artificial microRNA exhibit no significant impact on algal phototrophic growth and photosynthetic proteins accumulation, indicating that the conserved FDBR domain is sufficient and minimally required for bilin biosynthesis and functioning. Chlamydomonas PCYA1 uniquely interacts with light-dependent protochlorophyllide oxidoreductase LPOR (protochlorophyllide reductase, EC 1.3.1.33) but not with ferredoxin:protochlorophyllide reductase DPOR (EC 1.3.7.7). The CTE domain of PCYA1 is dispensable for phototrophic growth and photosynthetic proteins accumulation
malfunction
-
both the pcya1-1 mutant with the C-terminal extension of PCYA1 eliminated and efficient knockdown of PCYA1 expression by artificial microRNA exhibit no significant impact on algal phototrophic growth and photosynthetic proteins accumulation, indicating that the conserved FDBR domain is sufficient and minimally required for bilin biosynthesis and functioning. Chlamydomonas PCYA1 uniquely interacts with light-dependent protochlorophyllide oxidoreductase LPOR (protochlorophyllide reductase, EC 1.3.1.33) but not with ferredoxin:protochlorophyllide reductase DPOR (EC 1.3.7.7). The CTE domain of PCYA1 is dispensable for phototrophic growth and photosynthetic proteins accumulation
-
malfunction
-
because PcyA and PebA, EC 1.3.7.6/1.3.7.3, utilize the same substrate, biliverdin IXalpha, severe overexpression of pebA can limit the availability of phycocyanobilin, which appears to be required for viability when cells are grown in continuous light
-
metabolism
Thermosynechococcus vestitus
-
PcyA is involved in the phycocyanobilin biosynthetic pathway, in which PcyA first forms a stable complexes with the biliverdin IXa molecule
metabolism
-
phycocyanobilin:ferredoxin oxidoreductase, PcyA, is a key enzyme in the biogenesis of heme-derived linear tetrapyrroles, phytobilins, it catalyzes the overall four-electron reduction of biliverdin IXalpha to phycocyanobilin, the common chromophore precursor for both classes of biliproteins
metabolism
Acaryochloris marina strain 11017 exceptionally encodes two PcyA homologues, AmPcyAc and AmPcyAp. The enzymes AmPcyAc and AmPcyAp show completely different kinetics especially for 181/182-DHBV accumulation. High accumulation of 181/182-DHBV for extended periods is observed during the reaction catalyzed by AmPcyAc, whereas 181/182-DHBV is transiently accumulated for a short period during the reaction catalyzed by AmPcyAp. Phycocyanin a from Acaryochloris marina strain 11017 binds only phycocyanobilin (PCB) but not 181/182-DHBV
metabolism
ferredoxin-dependent biliverdin reductase, PCYA1, is a key enzyme involved in the biosynthesis of bilins, mechanism of bilin-mediated regulation of chlorophyll biosynthesis, and regulatory mechanisms of tetrapyrrole biosynthesis in Chlamydomonas reinhardtii, overview
metabolism
-
ferredoxin-dependent biliverdin reductase, PCYA1, is a key enzyme involved in the biosynthesis of bilins, mechanism of bilin-mediated regulation of chlorophyll biosynthesis, and regulatory mechanisms of tetrapyrrole biosynthesis in Chlamydomonas reinhardtii, overview
-
metabolism
-
Acaryochloris marina strain 11017 exceptionally encodes two PcyA homologues, AmPcyAc and AmPcyAp. The enzymes AmPcyAc and AmPcyAp show completely different kinetics especially for 181/182-DHBV accumulation. High accumulation of 181/182-DHBV for extended periods is observed during the reaction catalyzed by AmPcyAc, whereas 181/182-DHBV is transiently accumulated for a short period during the reaction catalyzed by AmPcyAp. Phycocyanin a from Acaryochloris marina strain 11017 binds only phycocyanobilin (PCB) but not 181/182-DHBV
-
physiological function
unlike other ferredoxin-dependent bilin reductases that catalyze a two-electron reduction, PcyA sequentially reduces D-ring (exo) and A-ring (endo) vinyl groups of biliverdin IXalpha to yield phycocyanobilin, a key pigment precursor of the light-harvesting antennae complexes of red algae, cyanobacteria, and cryptophytes
physiological function
-
bilin reductase PcyA catalyzes the proton-coupled four-electron reduction of biliverdin IXa's two vinyl groups to produce phycocyanobilin, an essential chromophore for phytochromes, cyanobacteriochromes and phycobiliproteins
physiological function
-
the pcyA gene of Synechococcus sp. strain PCC 7002 is essential
physiological function
in Chlamydomonas reinhardtii, bilins are not only essential retrograde signals to mitigate oxidative stress during diurnal dark-to-light transitions, they are also required for chlorophyll accumulation and maintenance of a functional photosynthetic apparatus in the light. The ferredoxin-dependent biliverdin reductase, FDBR, is involved in the biosynthesis of bilins. Chlamydomonas phycocyanobilin:ferredoxin oxidoreductase PCYA1 FDBR domain specifically interacts with the rate-limiting chlorophyll biosynthetic enzyme LPOR (light-dependent protochlorophyllide oxidoreductase). CrPCYA1 is a key enzyme involved in bilin biosynthesis in Chlamydomonas. Regulatory role of PCYA1 in chlorophyll biosynthesis via interaction with key Chl biosynthetic enzyme. Chlamydomonas PCYA1 contains unique N- and C-terminal extensions which exhibit autoactivation activity in yeast two-hybrid system
physiological function
phycocyanobilin (PCB) is synthesized by phycocyanobilin:ferredoxin oxidoreductase (PcyA). The reaction of PcyA starts from biliverdin IXalpha (BV), which is a product of the heme oxygenase-mediated cleavage of the heme macrocycle, to PCB through four-electron reduction
physiological function
phycocyanobilin:ferredoxin oxidoreductase (PcyA) catalyzes PCB synthesis from biliverdin via the intermediate 181/182-dihydrobiliverdin (181/182-DHBV), resulting in the stepwise shortening of the absorbing wavelengths. Cyanobacteriochromes (CBCRs) sense longer wavelength far-red light through 181/182-DHBV incorporation, whereas phycocyanobilin (PCB) only harvests orange light through PCB incorporation, suggesting functional diversification of PcyA as AmPcyAc and AmPcyAp to provide 181/182-DHBV and PCB to the light perception and harvesting systems, respectively. While most cyanobacteria utilize chlorophyll a as the photosynthetic reaction center pigment, Acaryochloris marina 11017 exceptionally utilizes chlorophyll d that absorbs longer wavelength far-red light than chlorophyll a
physiological function
phycocyanobilin:ferredoxin oxidoreductase (PcyA) catalyzes PCB synthesis from biliverdin via the intermediate 181/182-dihydrobiliverdin (181/182-DHBV), resulting in the stepwise shortening of the absorbing wavelengths. Cyanobacteriochromes (CBCRs) sense longer wavelength far-red light through 181/182-DHBV incorporation, whereas phycocyanobilin (PCB) only harvests orange light through PCB incorporation, suggesting functional diversification of PcyA as AmPcyAc and AmPcyAp to provide 181/182-DHBV and PCB to the light perception and harvesting systems, respectively. While most cyanobacteria utilize chlorophyll a as the photosynthetic reaction center pigment, Acaryochloris marina strain 11017 exceptionally utilizes chlorophyll d that absorbs longer wavelength far-red light than chlorophyll a
physiological function
-
in Chlamydomonas reinhardtii, bilins are not only essential retrograde signals to mitigate oxidative stress during diurnal dark-to-light transitions, they are also required for chlorophyll accumulation and maintenance of a functional photosynthetic apparatus in the light. The ferredoxin-dependent biliverdin reductase, FDBR, is involved in the biosynthesis of bilins. Chlamydomonas phycocyanobilin:ferredoxin oxidoreductase PCYA1 FDBR domain specifically interacts with the rate-limiting chlorophyll biosynthetic enzyme LPOR (light-dependent protochlorophyllide oxidoreductase). CrPCYA1 is a key enzyme involved in bilin biosynthesis in Chlamydomonas. Regulatory role of PCYA1 in chlorophyll biosynthesis via interaction with key Chl biosynthetic enzyme. Chlamydomonas PCYA1 contains unique N- and C-terminal extensions which exhibit autoactivation activity in yeast two-hybrid system
-
physiological function
-
the pcyA gene of Synechococcus sp. strain PCC 7002 is essential
-
physiological function
-
phycocyanobilin:ferredoxin oxidoreductase (PcyA) catalyzes PCB synthesis from biliverdin via the intermediate 181/182-dihydrobiliverdin (181/182-DHBV), resulting in the stepwise shortening of the absorbing wavelengths. Cyanobacteriochromes (CBCRs) sense longer wavelength far-red light through 181/182-DHBV incorporation, whereas phycocyanobilin (PCB) only harvests orange light through PCB incorporation, suggesting functional diversification of PcyA as AmPcyAc and AmPcyAp to provide 181/182-DHBV and PCB to the light perception and harvesting systems, respectively. While most cyanobacteria utilize chlorophyll a as the photosynthetic reaction center pigment, Acaryochloris marina 11017 exceptionally utilizes chlorophyll d that absorbs longer wavelength far-red light than chlorophyll a
-
physiological function
-
phycocyanobilin:ferredoxin oxidoreductase (PcyA) catalyzes PCB synthesis from biliverdin via the intermediate 181/182-dihydrobiliverdin (181/182-DHBV), resulting in the stepwise shortening of the absorbing wavelengths. Cyanobacteriochromes (CBCRs) sense longer wavelength far-red light through 181/182-DHBV incorporation, whereas phycocyanobilin (PCB) only harvests orange light through PCB incorporation, suggesting functional diversification of PcyA as AmPcyAc and AmPcyAp to provide 181/182-DHBV and PCB to the light perception and harvesting systems, respectively. While most cyanobacteria utilize chlorophyll a as the photosynthetic reaction center pigment, Acaryochloris marina strain 11017 exceptionally utilizes chlorophyll d that absorbs longer wavelength far-red light than chlorophyll a
-
additional information
-
cyanobacteria utilize phycocyanobilin:ferredoxin oxidoreductase (PcyA) to perform a two-step reaction, the enzyme first reduces the 18-vinyl side chain of the D-ring and subsequently reduces the vinyl side chain of the pyrrole A ring to yield phycocyanobilin
additional information
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the fully conserved residue His74 plays a critical role in the H-bonding network that permits proton transfer, molecular dynamics simulations, overview. A conserved buried water molecule that bridges His74 and catalytically essential His88 is not required for activity. The crucial active site residue Asp105 is more dynamic in H74A compared to wild-type PcyA and the two other His74 variants, supporting the conclusion that the Ala74 mutation has increased the flexibility of the active site. Structure analysis of recombinant wild-type and mutant enzymes, overview
additional information
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the interconversion occurs via semireduced bilin radical intermediates that are profoundly stabilized by selected mutations of two critical catalytic residues, Asp105 and His88. Mechanistic scheme for PcyA-mediated reduction of both vinyl groups of biliverdin wherein an axial water molecule, which prematurely binds and ejects from both mutants upon one electron reduction, is required for catalytic turnover of the semireduced state, structure-function relationship, overview
additional information
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the NADPH-dependent biliverdin reductases, BVR and BvdR, are less accommodating to amidation of the propionic acid side chains of biliverdin IXR than PcyA, which does not require free carboxylic acid side chains to yield its phytobilin product, phycocyanobilin
additional information
besides the putative chloroplast transit peptide (TP) and the conserved ferredoxin-dependent biliverdin reductase (FDBR) domain, Chlamydomonas CrPCYA1 contains additional N-terminal extension (NTE) and C-terminal extension (CTE), approximately 120 and 108 amino acids, respectively
additional information
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besides the putative chloroplast transit peptide (TP) and the conserved ferredoxin-dependent biliverdin reductase (FDBR) domain, Chlamydomonas CrPCYA1 contains additional N-terminal extension (NTE) and C-terminal extension (CTE), approximately 120 and 108 amino acids, respectively
additional information
quantum mechanical/molecular mechanical (QM/MM) studies investigating the most probable protonation states of active site amino acids and bound substrate based on a recently reported neutron diffraction structure of phycocyanobilin: ferredoxin oxidoreductase (PcyA), overview. The hydronium ion (H3O+) is energetically unfavorable, preferentially protonating the neighboring His88 residue and that the C-ring of BV is not protonated. The hydronium ion forms hydrogen bonds with His88 (Nepsilon), His74 (Ndelta) and Leu243 (Carbonyl O) residues
additional information
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the NADPH-dependent biliverdin reductases, BVR and BvdR, are less accommodating to amidation of the propionic acid side chains of biliverdin IXR than PcyA, which does not require free carboxylic acid side chains to yield its phytobilin product, phycocyanobilin
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additional information
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besides the putative chloroplast transit peptide (TP) and the conserved ferredoxin-dependent biliverdin reductase (FDBR) domain, Chlamydomonas CrPCYA1 contains additional N-terminal extension (NTE) and C-terminal extension (CTE), approximately 120 and 108 amino acids, respectively
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additional information
-
cyanobacteria utilize phycocyanobilin:ferredoxin oxidoreductase (PcyA) to perform a two-step reaction, the enzyme first reduces the 18-vinyl side chain of the D-ring and subsequently reduces the vinyl side chain of the pyrrole A ring to yield phycocyanobilin
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hanging drop vapour diffusion method with 18% PEG-8000, 0.025 M MES-NaOH at pH 6.5, 0.05 M Ca(OAc)2 at pH 6.5, and 5% dioxane (or 5% ethanol)
high-field electron paramagnetic resonance spectroscopy of frozen solutions and single crystals of the one-electron reduced protein-substrate complex of mutant D102N. Spectra reveal a biliverdin radical with a very narrow g tensor. This g tensor is consistent with a biliverdin radical where the carbonyl oxygen atoms on both the A and the D pyrrole rings are protonated
high-field electron paramagnetic resonance spectroscopy of frozen solutions and single crystals of the one-electron reduced protein-substrate complex of mutant D105N. Spectra reveal a biliverdin radical with a very narrow g tensor with principal values 2.00359(5), 2.00341(5), and 2.00218(5). This g tensor is consistent with a biliverdin radical where the carbonyl oxygen atoms on both the A and the D pyrrole rings are protonated
PcyAbiliverdin IXalpha complex by the hanging-drop vapor-diffusion method, PcyA is folded in a three-layer alpha/beta/alpha sandwich structure, in which biliverdin IXalpha in a cyclic conformation is positioned between the beta-sheet and C-terminal alpha-helices
purified recombinant enzyme mutant V225D in complex with substrates biliverdin IXalpha or biliverdin XIIIalpha, mixing of 0.0009 ml of protein solution, containing 11.5 mg/ml protein and biliverdin, with 0.0009 ml of reservoir solution containing 0.8-1.0 M NaH2PO4, 1.0-1.2 M K2HPO4, and 100 mM sodium acetate, pH 4.0, 20°C, a few days, X-ray diffraction structure determination and analysis at 1.9 A resolution
purified recombinant mutant enzymes, hanging drop vapour diffusion method, dithionite-treated reduced D105N PcyA crystals from 1.45-1.8 M ammonium sulfate, 0.15-0.4 M NaCl, and 0.1 M HEPES, pH 7.0, dithionite-treated reduced H88Q PcyA crystals from 1.7-2.2 M ammonium sulfate, 0.26-0.32 M NaCl, and 0.1 M sodium cacodylate, pH 7.0, 20°C in the dark, cryoprotectant solution is consisting of 30% v/v ethylene glycol in mother liquor, X-ray diffraction structure determination and analysis at 1.5 A resolution
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purified recombinant wild-type and mutant enzymes, hanging drop vapor diffusion method, mixing of 0.002 ml of protein solution containing 15 mg/mL protein and 0.67 mM biliverdin IXalpha, with 0.002 ml of reservoir solution containing 1-1.25 M sodium citrate, 0.1-0.4 M NaCl, and 0.1 M Tris HCl, pH 7.0, 21°C, 1-2 weeks. Crystal trials are set up under green safelight and stored in the dark, X-ray diffraction structure determination and analysis at 1.18-1.49 A resolution
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purified recombinant wild-type PcyA and PcyA-E76Q mutant in complex with 18EtBV or biloverdin IXalpha and biliverdin XIIIalpha, hanging drop vapor diffusion method, 20°C, method optimization, protein solution containing wild-type PcyA or mutant E76Q and bilin is mixed with reservoir solutions containing 0.85 M sodium citrate, 0.1 M sodium cacodylate, pH 7.0, for the PcyA-18EtBV complex and 2.0 M ammonium sulfate, 0.2 M NaCl, and 0.1M sodium cacodylate, pH7.0, for the PcyA-BV13 complex, for the mutant a reservoir solution containing 1.7 M ammonium sulfate, 2% PEG 400, and 0.1 M HEPES, pH 7.0, is used, X-ray diffraction structure determination and analysis at 1.04-1.48 A resolution
substrate-free form of PcyA by the hanging-drop vapor-diffusion method, at 2.5 A resolution, the side-chain of Asp105 is located at a site that would be underneath the biliverdin IXa A-ring in the PcyA-biliverdin IXa complex and hydrogen-bonded with His88, biliverdin IXa may be protonated by a mechanism involving conformational changes of these two residues before reduction
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quantum mechanical approaches show that the propensity of biliverdin to bind PcyA is dominated by electrostatic interactions, especially related to residues Arg149 and Lys221, while H-bonds are formed with His88 and Ser114. The antioxidant activity is dependent on the intramolecular noncovalent bond interactions. The surrounding residues increase the antioxidant character of biliverdin by 2 eV
structure of the I86D-BVH+ complex and the protonation states of residues Asp105 and Glu76 in PcyA. Asp105 adopts a fixed conformation in the I86D mutant, but has dual conformations in wild-type PcyA which reflects the protonation states of biliverdin
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C210A
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retains 90% relative to wild type
C86A
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retains 90% activity relative to wild type
D102N
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retains 11% activity relative to wild type
D116N
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retains 11% activity relative to wild type
D217N
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retains 87% relative to wild type
H71A
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retains less than 1% activity relative to wild type
H71D
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retains 28% activity relative to wild type
H71E
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retains 50% activity relative to wild type
H71N
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retains 46% activity relative to wild type
H71Q
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retains 65% activity relative to wild type
H85A
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retains less than 1% activity relative to wild type
H85D
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retains less than 1% activity relative to wild type
H85E
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retains 5% activity relative to wild type
H85N
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retains less than 1% activity relative to wild type
H85Q
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retains 5% activity relative to wild type
K218E
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retains 20% activity relative to wild type
C86A
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retains 90% activity relative to wild type
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D217N
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retains 87% relative to wild type
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H71A
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retains less than 1% activity relative to wild type
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H71N
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retains 46% activity relative to wild type
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H71Q
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retains 65% activity relative to wild type
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E73Q
exhibits 20% of wild type activity
H71Q
exhibits 65% of wild type activity
H85Q
exhibits 5% of wild type activity
K218E
exhibits 20% of wild type activity
E76Q
site-directed mutagenesis, substrate-binding structure compared to the wild-type enzyme. Overall folds and the binding sites of the U-shaped substrates of all three complexes are similar with wild-type PcyABV, the orientation of the Glu76 side chain, which is in close contact with the exo-vinyl group in PcyA-biliverdin IXalpha, is rotated away from the bilin D-ring. The local structures around the A-rings in the three complexes, which all retain the ability to reduce the A-ring of their bound pigments, are nearly identical with that of wild-type PcyA-biliverdin IXalpha
H74A
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site-directed mutagenesis, inactive mutant
H74E
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site-directed mutagenesis, the mutant retains reasonable activity
H74Q
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site-directed mutagenesis, the mutant retains reasonable activity
V225D
site-directed mutagenesis,substrate binding structure, overview
I86D
biliverdin bound to the I86D mutant is fully protonated (BVH+) and can accept an electron, but I86D is unable to donate protons for the reduction. Compared to the wild-type PcyA, the I86D mutant stabilizes BVH+
D102N
exhibits 11% of wild type activity
D102N
high-field electron paramagnetic resonance spectroscopy of frozen solutions and single crystals of the one-electron reduced protein-substrate complex of mutant D102N. Spectra reveal a biliverdin radical with a very narrow g tensor. This g tensor is consistent with a biliverdin radical where the carbonyl oxygen atoms on both the A and the D pyrrole rings are protonated
D105N
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site-directed mutagenesis
D105N
high-field electron paramagnetic resonance spectroscopy of frozen solutions and single crystals of the one-electron reduced protein-substrate complex of mutant D105N. Spectra reveal a biliverdin radical with a very narrow g tensor with principal values 2.00359(5), 2.00341(5), and 2.00218(5). This g tensor is consistent with a biliverdin radical where the carbonyl oxygen atoms on both the A and the D pyrrole rings are protonated
H88Q
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site-directed mutagenesis
H88Q
the g anisotropy of the biliverdin radical in H88Q is measurably smaller than those of mutant D105N
additional information
identification of mutant pcya1-1, cloning and photosynthetic phenotype analysis, overview. Efficient PCYA1 knockdown by artificial microRNA does not impact algal phototrophic growth. Yeast two-hybrid analyses of protein-protein interaction with bilin biosynthesis metabolism proteins using the coding regions of CrPCYA11TP (amino acids 56-556), CrPCYA1-NTE (amino acids 56-174), CrPCYA1-FDBR (amino acids 175-451), CrPCYA1-CTE (amino acids 449-556), and pull-down assay
additional information
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identification of mutant pcya1-1, cloning and photosynthetic phenotype analysis, overview. Efficient PCYA1 knockdown by artificial microRNA does not impact algal phototrophic growth. Yeast two-hybrid analyses of protein-protein interaction with bilin biosynthesis metabolism proteins using the coding regions of CrPCYA11TP (amino acids 56-556), CrPCYA1-NTE (amino acids 56-174), CrPCYA1-FDBR (amino acids 175-451), CrPCYA1-CTE (amino acids 449-556), and pull-down assay
additional information
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identification of mutant pcya1-1, cloning and photosynthetic phenotype analysis, overview. Efficient PCYA1 knockdown by artificial microRNA does not impact algal phototrophic growth. Yeast two-hybrid analyses of protein-protein interaction with bilin biosynthesis metabolism proteins using the coding regions of CrPCYA11TP (amino acids 56-556), CrPCYA1-NTE (amino acids 56-174), CrPCYA1-FDBR (amino acids 175-451), CrPCYA1-CTE (amino acids 449-556), and pull-down assay
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additional information
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insertional inactivation of pcyA is not possible in wild-type Synechococcus sp. strain PCC 7002 due to lethality of the mutant, but in a variant heterologously expressing HY2 from Arabidopsis thaliana encoding a phytochromobilin:ferredoxin oxidoreductase
additional information
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insertional inactivation of pcyA is not possible in wild-type Synechococcus sp. strain PCC 7002 due to lethality of the mutant, but in a variant heterologously expressing HY2 from Arabidopsis thaliana encoding a phytochromobilin:ferredoxin oxidoreductase
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additional information
construction of a plasmid containing genes of apo-allophycocyanin alpha-subunit without chromophore and chromophore synthetases HO1, i.e. ferredoxin-dependent heme oxygenase, and PcyA, i.e. phycocyanobilin:ferredoxin oxidoreductase, and expression in Escherichia coli. Holo-allophycocyanin, i.e. allophycocyanin alpha-subunit with chromophore, can be synthesized by autocatalysis in Escherichia coli. Recombinant holo-allophycocyanin alpha-subunit shows the same spectral and fluorescent properties as phycocyanin and serves as a good substitute for native phycocyanin for fluorescent tagging. Recombinant allophycocyanin alpha-subunit can inhibit hydroxyl and peroxyl radicals more strongly than holo-allophycocyanin alpha-subunit and native allophycocyanin
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Frankenberg, N.; Mukougawa, K.; Kohchi, T.; Lagarias, J.C.
Functional genomic analysis of the HY2 family of ferredoxin-dependent bilin reductases from oxygenic photosynthetic organisms
Plant Cell
13
965-978
2001
Anabaena sp., Prochlorococcus sp., Synechococcus sp., Synechocystis sp. (Q55891), Nostoc punctiforme (Q93TM9), Prochlorococcus sp. CCMP1378 / MED4, Synechococcus sp. WH8102
brenda
Tooley, A.J.; Glazer, A.N.
Biosynthesis of the cyanobacterial light-harvesting polypeptide phycoerythrocyanin holo-a subunit in a heterologous host
J. Bacteriol.
184
4666-4671
2002
Anabaena sp.
brenda
Tooley, A.J.; Cai, Y.A.; Glazer, A.N.
Biosynthesis of a fluorescent cyanobacterial C-phycocyanin holo-a subunit in a heterologous host
Proc. Natl. Acad. Sci. USA
98
10560-10565
2001
Synechocystis sp.
brenda
Wu, S.H; McDowell, M.T.; Lagaris, J.C.
Phycocyanobilin is the natural precursor of the phytochrome chromophore in the green alga Mesotaenium caldariorum
J. Biol. Chem.
272
25700-25705
1997
Mesotaenium caldariorum
brenda
Tu, S.L.; Gunn, A.; Toney, M.D.; Britt, R.D.; Lagarias, J.C.
Biliverdin reduction by cyanobacterial phycocyanobilin:ferredoxin oxidoreductase (PcyA) proceeds via linear tetrapyrrole radical intermediates
J. Am. Chem. Soc.
126
8682-8693
2004
Anabaena sp.
brenda
Frankenberg, N.; Lagarias, J.C.
Phycocyanobilin:ferredoxin oxidoreductase of Anabaena sp. PCC 7120. Biochemical and spectroscopic
J. Biol. Chem.
278
9219-9226
2003
Anabaena sp.
brenda
Kami, C.; Mukougawa, K.; Muramoto, T.; Yokota, A.; Shinomura, T.; Lagarias, J.C.; Kohchi, T.
Complementation of phytochrome chromophore-deficient Arabidopsis by expression of phycocyanobilin:ferredoxin oxidoreductase
Proc. Natl. Acad. Sci. USA
101
1099-1104
2004
Synechocystis sp.
brenda
Mukougawa, K.; Kanamoto, H.; Kobayashi, T.; Yokota, A.; Kohchi, T.
Metabolic engineering to produce phytochromes with phytochromobilin, phycocyanobilin, or phycoerythrobilin chromophore in Escherichia coli
FEBS Lett.
580
1333-1338
2006
Synechococcus sp., Synechococcus sp. W8020
brenda
Hagiwara, Y.; Sugishima, M.; Takahashi, Y.; Fukuyama, K.
Induced-fitting and electrostatic potential change of PcyA upon substrate binding demonstrated by the crystal structure of the substrate-free form
FEBS Lett.
580
3823-3828
2006
Synechocystis sp.
brenda
Tu, S.L.; Sughrue, W.; Britt, R.D.; Lagarias, J.C.
A conserved histidine-aspartate pair is required for exovinyl reduction of biliverdin by a cyanobacterial phycocyanobilin:ferredoxin oxidoreductase
J. Biol. Chem.
281
3127-3136
2006
Nostoc sp., Nostoc sp. PCC 7120
brenda
Zhao, K.H.; Su, P.; Li, J.; Tu, J.M.; Zhou, M.; Bubenzer, C.; Scheer, H.
Chromophore attachment to phycobiliprotein beta-subunits: phycocyanobilin:cysteine-beta84 phycobiliprotein lyase activity of CpeS-like protein from Anabaena Sp. PCC7120
J. Biol. Chem.
281
8573-8581
2006
Anabaena sp., Anabaena sp. PCC 7120
brenda
Hagiwara, Y.; Sugishima, M.; Takahashi, Y.; Fukuyama, K.
Crystal structure of phycocyanobilin:ferredoxin oxidoreductase in complex with biliverdin IXalpha, a key enzyme in the biosynthesis of phycocyanobilin
Proc. Natl. Acad. Sci. USA
103
27-32
2006
Synechocystis sp. (Q55891), Synechocystis sp.
brenda
Tu, S.L.; Rockwell, N.C.; Lagarias, J.C.; Fisher, A.J.
Insight into the radical mechanism of phycocyanobilin-ferredoxin oxidoreductase (PcyA) revealed by X-ray crystallography and biochemical measurements
Biochemistry
46
1484-1494
2007
Nostoc sp. PCC 7120 = FACHB-418 (Q93TN0)
brenda
Zhang, W.; Guan, X.; Yang, Y.; Ge, B.; Chen, H.; Li, F.; Qin, S.
Biosynthesis of fluorescent allophycocyanin alpha-subunits by autocatalysis in Escherichia coli
Biotechnol. Appl. Biochem.
52
135-140
2009
Synechocystis sp. (Q55891)
brenda
Stoll, S.; Gunn, A.; Brynda, M.; Sughrue, W.; Kohler, A.C.; Ozarowski, A.; Fisher, A.J.; Lagarias, J.C.; Britt, R.D.
Structure of the biliverdin radical intermediate in phycocyanobilin:ferredoxin oxidoreductase identified by high-field EPR and DFT
J. Am. Chem. Soc.
131
1986-1995
2009
Synechocystis sp. (Q55891), Synechocystis sp., Nostoc sp. PCC 7120 = FACHB-418 (Q93TN0)
brenda
Wada, K.; Hagiwara, Y.; Yutani, Y.; Fukuyama, K.
One residue substitution in PcyA leads to unexpected changes in tetrapyrrole substrate binding
Biochem. Biophys. Res. Commun.
402
373-377
2010
Synechocystis sp. (Q55891)
brenda
Okada, K.
HO1 and PcyA proteins involved in phycobilin biosynthesis form a 1:2 complex with ferredoxin-1 required for photosynthesis
FEBS Lett.
583
1251-1256
2009
Thermosynechococcus vestitus
brenda
Hagiwara, Y.; Sugishima, M.; Khawn, H.; Kinoshita, H.; Inomata, K.; Shang, L.; Lagarias, J.C.; Takahashi, Y.; Fukuyama, K.
Structural insights into vinyl reduction regiospecificity of phycocyanobilin:ferredoxin oxidoreductase (PcyA)
J. Biol. Chem.
285
1000-1007
2010
Synechocystis sp. (Q55891), Synechocystis sp.
brenda
Kabasakal, B.; Gae, D.D.; Li, J.; Clark Lagarias, J.; Koehl, P.; Fisher, A.J.
His74 conservation in the bilin reductase PcyA family reflects an important role in protein-substrate structure and dynamics
Arch. Biochem. Biophys.
537
233-242
2013
Synechocystis sp.
brenda
Shang, L.; Rockwell, N.C.; Martin, S.S.; Lagarias, J.C.
Biliverdin amides reveal roles for propionate side chains in bilin reductase recognition and in holophytochrome assembly and photoconversion
Biochemistry
49
6070-6082
2010
Anabaena sp., Anabaena sp. PCC 7120
brenda
Kohler, A.C.; Gae, D.D.; Richley, M.A.; Stoll, S.; Gunn, A.; Lim, S.; Martin, S.S.; Doukov, T.I.; Britt, R.D.; Ames, J.B.; Lagarias, J.C.; Fisher, A.J.
Structural basis for hydration dynamics in radical stabilization of bilin reductase mutants
Biochemistry
49
6206-6218
2010
Synechocystis sp.
brenda
Alvey, R.M.; Biswas, A.; Schluchter, W.M.; Bryant, D.A.
Attachment of noncognate chromophores to CpcA of Synechocystis sp. PCC 6803 and Synechococcus sp. PCC 7002 by heterologous expression in Escherichia coli
Biochemistry
50
4890-4902
2011
Synechococcus sp., Synechococcus sp. 7002
brenda
Alvey, R.M.; Biswas, A.; Schluchter, W.M.; Bryant, D.A.
Effects of modified phycobilin biosynthesis in the cyanobacterium Synechococcus sp. strain PCC 7002
J. Bacteriol.
193
1663-1671
2011
Synechococcus sp.
brenda
Ceron-Carrasco, J.; Jacquemin, D.; Laurent, A.
First computational step towards the understanding of the antioxidant activity of the phycocyanobilin ferredoxin oxidoreductase in complex with biliverdin IXalpha
Comput. Theoret. Chem.
1077
58-64
2016
Synechocystis sp. PCC 6803 (Q55891)
-
brenda
Hagiwara, Y.; Wada, K.; Irikawa, T.; Sato, H.; Unno, M.; Yamamoto, K.; Fukuyama, K.; Sugishima, M.
Atomic-resolution structure of the phycocyanobilin ferredoxin oxidoreductase I86D mutant in complex with fully protonated biliverdin
FEBS Lett.
590
3425-3434
2016
Synechocystis sp. PCC 6803 (Q55891)
brenda
Iijima, E.; Gleeson, M.; Unno, M.; Mori, S.
QM/MM investigation for protonation states in a bilin reductase PcyA-biliverdin IXalpha complex
ChemPhysChem
19
1809-1813
2018
Synechocystis sp. PCC 6803 (Q55891)
brenda
Miyake, K.; Fushimi, K.; Kashimoto, T.; Maeda, K.; Ni-Ni-Win, K.; Kimura, H.; Sugishima, M.; Ikeuchi, M.; Narikawa, R.
Functional diversification of two bilin reductases for light perception and harvesting in unique cyanobacterium Acaryochloris marina MBIC 11017
FEBS J.
287
4016-4031
2020
Acaryochloris marina (A8ZMS5), Acaryochloris marina (B0CAR8), Acaryochloris marina, Synechocystis sp. PCC 6803 (Q55891), Acaryochloris marina MBIC 11017 (A8ZMS5), Acaryochloris marina MBIC 11017 (B0CAR8)
brenda
Zhang, W.; Zhong, H.; Lu, H.; Zhang, Y.; Deng, X.; Huang, K.; Duanmu, D.
Characterization of ferredoxin-dependent biliverdin reductase PCYA1 reveals the dual function in retrograde bilin biosynthesis and interaction with light-dependent protochlorophyllide oxidoreductase LPOR in Chlamydomonas reinhardtii
Front. Plant Sci.
9
676
2018
Chlamydomonas reinhardtii (A8HUP3), Chlamydomonas reinhardtii, Chlamydomonas reinhardtii 4A+ (A8HUP3)
brenda