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3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
3-deacetyl-3-vinylbacteriochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + H+
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
bacteriochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
3-acetyl-3-devinylchlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + H+
-
-
-
-
?
chlorophyllide a + AH2 + ATP + H2O
3-deacetyl-3-vinylbacteriochlorophyllide a + A + ADP + phosphate
protochlorophyllide + reduced dithionite + ATP + H2O + H+
chlorophyllide a + oxidized dithionite + ADP + phosphate
-
-
-
-
?
protochlorophyllide + reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + H+
chlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
-
-
-
-
?
additional information
?
-
3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
-
-
-
?
3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
-
-
-
?
3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
-
-
-
?
3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
-
-
-
?
3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
-
-
-
?
3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
-
-
-
?
3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
-
-
-
?
3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
-
-
-
?
3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
-
-
-
?
3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
-
-
-
?
3-deacetyl-3-vinylbacteriochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + H+
-
-
-
-
?
3-deacetyl-3-vinylbacteriochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + H+
-
-
-
-
?
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
the substrate is purified from the Rhodobacter capsulatus strain CB1200
-
-
?
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
the substrate is purified from the Rhodobacter capsulatus strain CB1200
-
-
?
chlorophyllide a + AH2 + ATP + H2O
3-deacetyl-3-vinylbacteriochlorophyllide a + A + ADP + phosphate
-
-
-
-
?
chlorophyllide a + AH2 + ATP + H2O
3-deacetyl-3-vinylbacteriochlorophyllide a + A + ADP + phosphate
-
the enzyme catalyses trans-reduction of the B-ring of chlorophyllide a. The product has the (7R,8R)-configuration
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-
?
additional information
?
-
holoenzyme is composed of subunits BchX, BchY, and BchZ, and reduces ring B of chlorophyllide a using NADH under anaerobic conditions. It generates superoxide at low O2 concentrations. Superoxide is generated not from FMN of reductase subunit BchX but from heme of subunit BchZ
-
-
?
additional information
?
-
-
holoenzyme is composed of subunits BchX, BchY, and BchZ, and reduces ring B of chlorophyllide a using NADH under anaerobic conditions. It generates superoxide at low O2 concentrations. Superoxide is generated not from FMN of reductase subunit BchX but from heme of subunit BchZ
-
-
?
additional information
?
-
holoenzyme is composed of subunits BchX, BchY, and BchZ, and reduces ring B of chlorophyllide a using NADH under anaerobic conditions. It generates superoxide at low O2 concentrations. Superoxide is generated not from FMN of reductase subunit BchX but from heme of subunit BchZ
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-
?
additional information
?
-
enzyme COR has an alternative 8VR activity in addition to the B-ring C7=C8 double bond reduction activity, cf. EC 1.3.7.13 or EC 1.3.1.75
-
-
-
additional information
?
-
-
enzyme COR has an alternative 8VR activity in addition to the B-ring C7=C8 double bond reduction activity, cf. EC 1.3.7.13 or EC 1.3.1.75
-
-
-
additional information
?
-
enzyme COR has an alternative 8VR activity in addition to the B-ring C7=C8 double bond reduction activity, cf. EC 1.3.7.13 or EC 1.3.1.75
-
-
-
additional information
?
-
enzyme COR has an alternative 8VR activity in addition to the B-ring C7=C8 double bond reduction activity, cf. EC 1.3.7.13 or EC 1.3.1.75
-
-
-
additional information
?
-
enzyme COR has an alternative 8VR activity in addition to the B-ring C7=C8 double bond reduction activity, cf. EC 1.3.7.13 or EC 1.3.1.75
-
-
-
additional information
?
-
for the standard DPOR/COR activity assay, a cell-free Escherichia coli extract containing overproduced Chlorobaculum tepidum DPOR subunits, BchN, BchB and BchL, is used in combination with purified recombinant COR subcomplexes, BchX2 and (BchY/BchZ)2. When using the chemical reducing agent, dithionite, instead of the natural electron donor (which might be a ferredoxin), it is essential to conduct control reactions in the absence of BchX2 and (BchY/BchZ)2 to ensure the dependence of the observed COR activity on both protein subcomplexes. The maximum COR activity is only achieved using an optimal ratio between BchX2 and (BchY/BchZ)2. Protein-protein interaction of BchX2 and (BchY/BchZ)2 is investigated in the presence of an analogue of the cosubstrate ATP, MgADP-AlF4-. Assay method evaluation, overview
-
-
-
additional information
?
-
for the standard DPOR/COR activity assay, a cell-free Escherichia coli extract containing overproduced Chlorobaculum tepidum DPOR subunits, BchN, BchB and BchL, is used in combination with purified recombinant COR subcomplexes, BchX2 and (BchY/BchZ)2. When using the chemical reducing agent, dithionite, instead of the natural electron donor (which might be a ferredoxin), it is essential to conduct control reactions in the absence of BchX2 and (BchY/BchZ)2 to ensure the dependence of the observed COR activity on both protein subcomplexes. The maximum COR activity is only achieved using an optimal ratio between BchX2 and (BchY/BchZ)2. Protein-protein interaction of BchX2 and (BchY/BchZ)2 is investigated in the presence of an analogue of the cosubstrate ATP, MgADP-AlF4-. Assay method evaluation, overview
-
-
-
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3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
3-deacetyl-3-vinylbacteriochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + H+
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
bacteriochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
3-acetyl-3-devinylchlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + H+
-
-
-
-
?
chlorophyllide a + AH2 + ATP + H2O
3-deacetyl-3-vinylbacteriochlorophyllide a + A + ADP + phosphate
-
-
-
-
?
protochlorophyllide + reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + H+
chlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
-
-
-
-
?
3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
-
-
-
?
3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
-
-
-
?
3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
-
-
-
?
3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
-
-
-
?
3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
-
-
-
?
3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
-
-
-
?
3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
-
-
-
?
3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
-
-
-
?
3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
-
-
-
?
3-acetyl-3-devinylchlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + 2 H+
bacteriochlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
-
-
-
?
3-deacetyl-3-vinylbacteriochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + H+
-
-
-
-
?
3-deacetyl-3-vinylbacteriochlorophyllide a + oxidized ferredoxin [iron-sulfur] cluster + ADP + phosphate
chlorophyllide a + reduced ferredoxin [iron-sulfur] cluster + ATP + H2O + H+
-
-
-
-
?
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
8-vinyl chlorophyllide a + 2 reduced ferredoxin [iron-sulfur] cluster + 2 H+
chlorophyllide a + 2 oxidized ferredoxin [iron-sulfur] cluster
-
-
-
?
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evolution
BciA (EC 1.3.1.75, NADPH-dependent C8 divinyl reductase) is a much faster and less energy consuming catalytic enzyme than the chlorophyllide oxidoreductase (COR). This finding implies that the bciA gene was acquired in each ancestral lineage by multiple horizontal gene transfer events after the establishment of anoxygenic photosynthesis. The high demand of Chl for large antenna complexes might have a major selective pressure for the evolutionary acquisition of an auxiliary divinyl reductase, BciA. Compared to the enzymatic activity of a-COR, BciA from Rhodobacter capsulatus has a lower affinity for DV-Chlide a but a much higher specific activity
evolution
-
the light-independent chlorophyllide reductase BchXYZ is common to all anoxygenic phototrophic bacteria, including those with a type-I and those with a type-II photosynthetic reaction center. The phylogenetic analysis includes cultured phototrophic bacteria from several phyla, including Proteobacteria (138 species), Chloroflexi (five species), Chlorobi (six species), as well as Heliobacterium modesticaldum (Firmicutes), Chloracidobacterium acidophilum (Acidobacteria), and Gemmatimonas phototrophica (Gemmatimonadetes). Phylogenetic relationships based on a photosynthesis tree (PS tree, including sequences of PufHLM-BchXYZ) are compared with those of 16S rRNA gene sequences (RNS tree). Despite some significant differences, large parts are congruent between the 16S rRNA phylogeny and photosynthesis proteins. The phylogenetic relations demonstrate that bacteriochlorophyll biosynthesis had evolved in ancestors of phototrophic green bacteria much earlier as compared to phototrophic purple bacteria and that multiple events independently formed different lineages of aerobic phototrophic purple bacteria, many of which have very ancient roots. The Rhodobacterales clearly represent the youngest group, which is separated from other Proteobacteria by a large evolutionary gap
evolution
-
the light-independent chlorophyllide reductase BchXYZ is common to all anoxygenic phototrophic bacteria, including those with a type-I and those with a type-II photosynthetic reaction center. The phylogenetic analysis includes cultured phototrophic bacteria from several phyla, including Proteobacteria (138 species), Chloroflexi (five species), Chlorobi (six species), as well as Heliobacterium modesticaldum (Firmicutes), Chloracidobacterium acidophilum (Acidobacteria), and Gemmatimonas phototrophica (Gemmatimonadetes). Phylogenetic relationships based on a photosynthesis tree (PS tree, including sequences of PufHLM-BchXYZ) are compared with those of 16S rRNA gene sequences (RNS tree). Despite some significant differences, large parts are congruent between the 16S rRNA phylogeny and photosynthesis proteins. The phylogenetic relations demonstrate that bacteriochlorophyll biosynthesis had evolved in ancestors of phototrophic green bacteria much earlier as compared to phototrophic purple bacteria and that multiple events independently formed different lineages of aerobic phototrophic purple bacteria, many of which have very ancient roots. The Rhodobacterales clearly represent the youngest group, which is separated from other Proteobacteria by a large evolutionary gap
evolution
A0A143BJ63; A0A143BQ39
the light-independent chlorophyllide reductase BchXYZ is common to all anoxygenic phototrophic bacteria, including those with a type-I and those with a type-II photosynthetic reaction center. The phylogenetic analysis includes cultured phototrophic bacteria from several phyla, including Proteobacteria (138 species), Chloroflexi (five species), Chlorobi (six species), as well as Heliobacterium modesticaldum (Firmicutes), Chloracidobacterium acidophilum (Acidobacteria), and Gemmatimonas phototrophica (Gemmatimonadetes). Phylogenetic relationships based on a photosynthesis tree (PS tree, including sequences of PufHLM-BchXYZ) are compared with those of 16S rRNA gene sequences (RNS tree). Despite some significant differences, large parts are congruent between the 16S rRNA phylogeny and photosynthesis proteins. The phylogenetic relations demonstrate that bacteriochlorophyll biosynthesis had evolved in ancestors of phototrophic green bacteria much earlier as compared to phototrophic purple bacteria and that multiple events independently formed different lineages of aerobic phototrophic purple bacteria, many of which have very ancient roots. The Rhodobacterales clearly represent the youngest group, which is separated from other Proteobacteria by a large evolutionary gap
evolution
B0TBQ4; B0TBQ9; B0TBQ8
the light-independent chlorophyllide reductase BchXYZ is common to all anoxygenic phototrophic bacteria, including those with a type-I and those with a type-II photosynthetic reaction center. The phylogenetic analysis includes cultured phototrophic bacteria from several phyla, including Proteobacteria (138 species), Chloroflexi (five species), Chlorobi (six species), as well as Heliobacterium modesticaldum (Firmicutes), Chloracidobacterium acidophilum (Acidobacteria), and Gemmatimonas phototrophica (Gemmatimonadetes). Phylogenetic relationships based on a photosynthesis tree (PS tree, including sequences of PufHLM-BchXYZ) are compared with those of 16S rRNA gene sequences (RNS tree). Despite some significant differences, large parts are congruent between the 16S rRNA phylogeny and photosynthesis proteins. The phylogenetic relations demonstrate that bacteriochlorophyll biosynthesis had evolved in ancestors of phototrophic green bacteria much earlier as compared to phototrophic purple bacteria and that multiple events independently formed different lineages of aerobic phototrophic purple bacteria, many of which have very ancient roots. The Rhodobacterales clearly represent the youngest group, which is separated from other Proteobacteria by a large evolutionary gap
evolution
-
the light-independent chlorophyllide reductase BchXYZ is common to all anoxygenic phototrophic bacteria, including those with a type-I and those with a type-II photosynthetic reaction center. The phylogenetic analysis includes cultured phototrophic bacteria from several phyla, including Proteobacteria (138 species), Chloroflexi (five species), Chlorobi (six species), as well as Heliobacterium modesticaldum (Firmicutes), Chloracidobacterium acidophilum (Acidobacteria), and Gemmatimonas phototrophica (Gemmatimonadetes). Phylogenetic relationships based on a photosynthesis tree (PS tree, including sequences of PufHLM-BchXYZ) are compared with those of 16S rRNA gene sequences (RNS tree). Despite some significant differences, large parts are congruent between the 16S rRNA phylogeny and photosynthesis proteins. The phylogenetic relations demonstrate that bacteriochlorophyll biosynthesis had evolved in ancestors of phototrophic green bacteria much earlier as compared to phototrophic purple bacteria and that multiple events independently formed different lineages of aerobic phototrophic purple bacteria, many of which have very ancient roots. The Rhodobacterales clearly represent the youngest group, which is separated from other Proteobacteria by a large evolutionary gap
evolution
-
the light-independent chlorophyllide reductase BchXYZ is common to all anoxygenic phototrophic bacteria, including those with a type-I and those with a type-II photosynthetic reaction center. The phylogenetic analysis includes cultured phototrophic bacteria from several phyla, including Proteobacteria (138 species), Chloroflexi (five species), Chlorobi (six species), as well as Heliobacterium modesticaldum (Firmicutes), Chloracidobacterium thermophilum (representative of Acidobacteria phylum), and Gemmatimonas phototrophica (Gemmatimonadetes). Phylogenetic relationships based on a photosynthesis tree (PS tree, including sequences of PufHLM-BchXYZ) are compared with those of 16S rRNA gene sequences (RNS tree). Despite some significant differences, large parts are congruent between the 16S rRNA phylogeny and photosynthesis proteins. The phylogenetic relations demonstrate that bacteriochlorophyll biosynthesis had evolved in ancestors of phototrophic green bacteria much earlier as compared to phototrophic purple bacteria and that multiple events independently formed different lineages of aerobic phototrophic purple bacteria, many of which have very ancient roots. The Rhodobacterales clearly represent the youngest group, which is separated from other Proteobacteria by a large evolutionary gap
evolution
-
BciA (EC 1.3.1.75, NADPH-dependent C8 divinyl reductase) is a much faster and less energy consuming catalytic enzyme than the chlorophyllide oxidoreductase (COR). This finding implies that the bciA gene was acquired in each ancestral lineage by multiple horizontal gene transfer events after the establishment of anoxygenic photosynthesis. The high demand of Chl for large antenna complexes might have a major selective pressure for the evolutionary acquisition of an auxiliary divinyl reductase, BciA. Compared to the enzymatic activity of a-COR, BciA from Rhodobacter capsulatus has a lower affinity for DV-Chlide a but a much higher specific activity
-
evolution
-
the light-independent chlorophyllide reductase BchXYZ is common to all anoxygenic phototrophic bacteria, including those with a type-I and those with a type-II photosynthetic reaction center. The phylogenetic analysis includes cultured phototrophic bacteria from several phyla, including Proteobacteria (138 species), Chloroflexi (five species), Chlorobi (six species), as well as Heliobacterium modesticaldum (Firmicutes), Chloracidobacterium acidophilum (Acidobacteria), and Gemmatimonas phototrophica (Gemmatimonadetes). Phylogenetic relationships based on a photosynthesis tree (PS tree, including sequences of PufHLM-BchXYZ) are compared with those of 16S rRNA gene sequences (RNS tree). Despite some significant differences, large parts are congruent between the 16S rRNA phylogeny and photosynthesis proteins. The phylogenetic relations demonstrate that bacteriochlorophyll biosynthesis had evolved in ancestors of phototrophic green bacteria much earlier as compared to phototrophic purple bacteria and that multiple events independently formed different lineages of aerobic phototrophic purple bacteria, many of which have very ancient roots. The Rhodobacterales clearly represent the youngest group, which is separated from other Proteobacteria by a large evolutionary gap
-
evolution
-
BciA (EC 1.3.1.75, NADPH-dependent C8 divinyl reductase) is a much faster and less energy consuming catalytic enzyme than the chlorophyllide oxidoreductase (COR). This finding implies that the bciA gene was acquired in each ancestral lineage by multiple horizontal gene transfer events after the establishment of anoxygenic photosynthesis. The high demand of Chl for large antenna complexes might have a major selective pressure for the evolutionary acquisition of an auxiliary divinyl reductase, BciA. Compared to the enzymatic activity of a-COR, BciA from Rhodobacter capsulatus has a lower affinity for DV-Chlide a but a much higher specific activity
-
evolution
-
the light-independent chlorophyllide reductase BchXYZ is common to all anoxygenic phototrophic bacteria, including those with a type-I and those with a type-II photosynthetic reaction center. The phylogenetic analysis includes cultured phototrophic bacteria from several phyla, including Proteobacteria (138 species), Chloroflexi (five species), Chlorobi (six species), as well as Heliobacterium modesticaldum (Firmicutes), Chloracidobacterium acidophilum (Acidobacteria), and Gemmatimonas phototrophica (Gemmatimonadetes). Phylogenetic relationships based on a photosynthesis tree (PS tree, including sequences of PufHLM-BchXYZ) are compared with those of 16S rRNA gene sequences (RNS tree). Despite some significant differences, large parts are congruent between the 16S rRNA phylogeny and photosynthesis proteins. The phylogenetic relations demonstrate that bacteriochlorophyll biosynthesis had evolved in ancestors of phototrophic green bacteria much earlier as compared to phototrophic purple bacteria and that multiple events independently formed different lineages of aerobic phototrophic purple bacteria, many of which have very ancient roots. The Rhodobacterales clearly represent the youngest group, which is separated from other Proteobacteria by a large evolutionary gap
-
evolution
-
BciA (EC 1.3.1.75, NADPH-dependent C8 divinyl reductase) is a much faster and less energy consuming catalytic enzyme than the chlorophyllide oxidoreductase (COR). This finding implies that the bciA gene was acquired in each ancestral lineage by multiple horizontal gene transfer events after the establishment of anoxygenic photosynthesis. The high demand of Chl for large antenna complexes might have a major selective pressure for the evolutionary acquisition of an auxiliary divinyl reductase, BciA. Compared to the enzymatic activity of a-COR, BciA from Rhodobacter capsulatus has a lower affinity for DV-Chlide a but a much higher specific activity
-
metabolism
bacteriochlorophyll a (BChl) is an essential pigment for anoxygenic photosynthesis. In late steps of the BChl biosynthesis of Rhodobacter capsulatus, the C8 vinyl group and C7=C8 double bond of 8-vinyl chlorophyllide a (8 V-Chlide) are reduced by a C8 vinyl reductase (8VR), BciA (EC 1.3.1.75) or BciB (EC 1.3.7.13), and a nitrogenase-like enzyme, chlorophyllide a oxidoreductase (COR), respectively, to produce 3-vinyl-bacteriochlorphyllide a. BciB is a FAD-containing FeS protein that uses reduced ferredoxin as the reductant for the 8-vinyl reduction of 8 V-Chlide or 8 V-PChlide, while BciA utilizes NADPH
metabolism
the biosynthesis of all bacteriochlorophylls involves the two-electron reduction of the C7-C8 double bond of the green pigment chlorophyllide, which is catalyzed by the nitrogenase-like two-component metalloenzyme chlorophyllide oxidoreductase (COR), whereas in all methanogenic microbes, another nitrogenase-like system, CfbC/D, is responsible for the sophisticated six-electron reduction of Ni2+-sirohydrochlorin a,c-diamide in the course of coenzyme F430 biosynthesis
metabolism
-
bacteriochlorophyll a (BChl) is an essential pigment for anoxygenic photosynthesis. In late steps of the BChl biosynthesis of Rhodobacter capsulatus, the C8 vinyl group and C7=C8 double bond of 8-vinyl chlorophyllide a (8 V-Chlide) are reduced by a C8 vinyl reductase (8VR), BciA (EC 1.3.1.75) or BciB (EC 1.3.7.13), and a nitrogenase-like enzyme, chlorophyllide a oxidoreductase (COR), respectively, to produce 3-vinyl-bacteriochlorphyllide a. BciB is a FAD-containing FeS protein that uses reduced ferredoxin as the reductant for the 8-vinyl reduction of 8 V-Chlide or 8 V-PChlide, while BciA utilizes NADPH
-
metabolism
-
the biosynthesis of all bacteriochlorophylls involves the two-electron reduction of the C7-C8 double bond of the green pigment chlorophyllide, which is catalyzed by the nitrogenase-like two-component metalloenzyme chlorophyllide oxidoreductase (COR), whereas in all methanogenic microbes, another nitrogenase-like system, CfbC/D, is responsible for the sophisticated six-electron reduction of Ni2+-sirohydrochlorin a,c-diamide in the course of coenzyme F430 biosynthesis
-
metabolism
-
bacteriochlorophyll a (BChl) is an essential pigment for anoxygenic photosynthesis. In late steps of the BChl biosynthesis of Rhodobacter capsulatus, the C8 vinyl group and C7=C8 double bond of 8-vinyl chlorophyllide a (8 V-Chlide) are reduced by a C8 vinyl reductase (8VR), BciA (EC 1.3.1.75) or BciB (EC 1.3.7.13), and a nitrogenase-like enzyme, chlorophyllide a oxidoreductase (COR), respectively, to produce 3-vinyl-bacteriochlorphyllide a. BciB is a FAD-containing FeS protein that uses reduced ferredoxin as the reductant for the 8-vinyl reduction of 8 V-Chlide or 8 V-PChlide, while BciA utilizes NADPH
-
metabolism
-
bacteriochlorophyll a (BChl) is an essential pigment for anoxygenic photosynthesis. In late steps of the BChl biosynthesis of Rhodobacter capsulatus, the C8 vinyl group and C7=C8 double bond of 8-vinyl chlorophyllide a (8 V-Chlide) are reduced by a C8 vinyl reductase (8VR), BciA (EC 1.3.1.75) or BciB (EC 1.3.7.13), and a nitrogenase-like enzyme, chlorophyllide a oxidoreductase (COR), respectively, to produce 3-vinyl-bacteriochlorphyllide a. BciB is a FAD-containing FeS protein that uses reduced ferredoxin as the reductant for the 8-vinyl reduction of 8 V-Chlide or 8 V-PChlide, while BciA utilizes NADPH
-
physiological function
heterologous expression of subunits bchXYZ in Synechocystis sp. PCC6803 results in decrease in photosynthetic growth. An increase in cytosolic superoxide dismutase level in the recombinant Synechocystis sp. PCC6803 completely reversed the growth cessation, demonstraing that chlorophyllide a reductase generates superoxide in Synechocystis sp. PCC6803
physiological function
the bchA locus contains three genes bchX, Y and Z, which are essential for the reduction of 2-devinyl-2-hydroxyethyl chlorophyllide a. BchX may supply electrons for reduction of 2-devinyl-2-hydroxyethyl chlorophyllide a
physiological function
bacteriochlorophyll a (BChl) is an essential pigment for anoxygenic photosynthesis. In late steps of the BChl biosynthesis of Rhodobacter capsulatus, the C8 vinyl group and C7=C8 double bond of 8-vinyl chlorophyllide a (8 V-Chlide) are reduced by a C8 vinyl reductase (8VR), BciA (EC 1.3.1.75) or BciB (EC 1.3.7.13), and a nitrogenase-like enzyme, chlorophyllide a oxidoreductase (COR), respectively, to produce 3-vinyl-bacteriochlorphyllide a. The COR activity can act as a third 8VR, confirmed in vivo by the loss of 8VR activity mutants lacking bciA and genes encoding subunits of COR. In contrast to BciA and BciB, COR is a nitrogenase-like complex enzyme consisting of two separable components, the X protein (a BchX dimer) and the YZ protein (a BchY-BchZ heterotetramer). The X protein serves as the reductase component by transferring electrons from a [4Fe-4S] cluster held in the interface between the BchX homodimer and the YZ protein. The YZ protein is the catalytic component, as it accepts electrons from the X protein and transfers them to the Chlide substrate via a [4Fe-4S] cluster, to produce 3-vinyl bacteriochlorophyllide a (3 V-BChlide). 3 V-BChlide is produced via Chlide rather than via 3,8-divinyl BChlide (81,82-didehydro-3 V-BChlide)
physiological function
chlorophyllide (Chlide) oxidoreductase, COR, is a unique BChl biosynthesis enzyme which shows distinct substrate recognition and hydrogen addition activities, depending on the host strain. COR in BChl a-producing phototrophic bacteria (a-COR) catalyzes the C7=C8 double bond reduction of Chlide a, whereas COR in BChl b- and BChl g-producing bacteria (b/g-COR) forms the C8-ethylidene group using DV-Chlide a as the substrate. Chlorophyllide oxidoreductase (COR) reduces the C7=C8 double bond of chlorophyllide a (Chlide a) bearing the C8-ethyl group, but also potentially catalyzes the reduction of the C8-vinyl group of divinyl-chlorophyllide a (DV-Chlide a). DV-Chlide a is a universal precursor for chlorophyll or bacteriochlorophyll biosynthesis in all photosynthetic organisms
physiological function
the biosynthesis of all bacteriochlorophylls involves the two-electron reduction of the C7-C8 double bond of the green pigment chlorophyllide, which is catalyzed by the nitrogenase-like two-component metalloenzyme chlorophyllide oxidoreductase (COR), whereas in all methanogenic microbes, another nitrogenase-like system, CfbC/D, is responsible for the sophisticated six-electron reduction of Ni2+-sirohydrochlorin a,c-diamide in the course of coenzyme F430 biosynthesis
physiological function
-
heterologous expression of subunits bchXYZ in Synechocystis sp. PCC6803 results in decrease in photosynthetic growth. An increase in cytosolic superoxide dismutase level in the recombinant Synechocystis sp. PCC6803 completely reversed the growth cessation, demonstraing that chlorophyllide a reductase generates superoxide in Synechocystis sp. PCC6803
-
physiological function
-
bacteriochlorophyll a (BChl) is an essential pigment for anoxygenic photosynthesis. In late steps of the BChl biosynthesis of Rhodobacter capsulatus, the C8 vinyl group and C7=C8 double bond of 8-vinyl chlorophyllide a (8 V-Chlide) are reduced by a C8 vinyl reductase (8VR), BciA (EC 1.3.1.75) or BciB (EC 1.3.7.13), and a nitrogenase-like enzyme, chlorophyllide a oxidoreductase (COR), respectively, to produce 3-vinyl-bacteriochlorphyllide a. The COR activity can act as a third 8VR, confirmed in vivo by the loss of 8VR activity mutants lacking bciA and genes encoding subunits of COR. In contrast to BciA and BciB, COR is a nitrogenase-like complex enzyme consisting of two separable components, the X protein (a BchX dimer) and the YZ protein (a BchY-BchZ heterotetramer). The X protein serves as the reductase component by transferring electrons from a [4Fe-4S] cluster held in the interface between the BchX homodimer and the YZ protein. The YZ protein is the catalytic component, as it accepts electrons from the X protein and transfers them to the Chlide substrate via a [4Fe-4S] cluster, to produce 3-vinyl bacteriochlorophyllide a (3 V-BChlide). 3 V-BChlide is produced via Chlide rather than via 3,8-divinyl BChlide (81,82-didehydro-3 V-BChlide)
-
physiological function
-
chlorophyllide (Chlide) oxidoreductase, COR, is a unique BChl biosynthesis enzyme which shows distinct substrate recognition and hydrogen addition activities, depending on the host strain. COR in BChl a-producing phototrophic bacteria (a-COR) catalyzes the C7=C8 double bond reduction of Chlide a, whereas COR in BChl b- and BChl g-producing bacteria (b/g-COR) forms the C8-ethylidene group using DV-Chlide a as the substrate. Chlorophyllide oxidoreductase (COR) reduces the C7=C8 double bond of chlorophyllide a (Chlide a) bearing the C8-ethyl group, but also potentially catalyzes the reduction of the C8-vinyl group of divinyl-chlorophyllide a (DV-Chlide a). DV-Chlide a is a universal precursor for chlorophyll or bacteriochlorophyll biosynthesis in all photosynthetic organisms
-
physiological function
-
the biosynthesis of all bacteriochlorophylls involves the two-electron reduction of the C7-C8 double bond of the green pigment chlorophyllide, which is catalyzed by the nitrogenase-like two-component metalloenzyme chlorophyllide oxidoreductase (COR), whereas in all methanogenic microbes, another nitrogenase-like system, CfbC/D, is responsible for the sophisticated six-electron reduction of Ni2+-sirohydrochlorin a,c-diamide in the course of coenzyme F430 biosynthesis
-
physiological function
-
bacteriochlorophyll a (BChl) is an essential pigment for anoxygenic photosynthesis. In late steps of the BChl biosynthesis of Rhodobacter capsulatus, the C8 vinyl group and C7=C8 double bond of 8-vinyl chlorophyllide a (8 V-Chlide) are reduced by a C8 vinyl reductase (8VR), BciA (EC 1.3.1.75) or BciB (EC 1.3.7.13), and a nitrogenase-like enzyme, chlorophyllide a oxidoreductase (COR), respectively, to produce 3-vinyl-bacteriochlorphyllide a. The COR activity can act as a third 8VR, confirmed in vivo by the loss of 8VR activity mutants lacking bciA and genes encoding subunits of COR. In contrast to BciA and BciB, COR is a nitrogenase-like complex enzyme consisting of two separable components, the X protein (a BchX dimer) and the YZ protein (a BchY-BchZ heterotetramer). The X protein serves as the reductase component by transferring electrons from a [4Fe-4S] cluster held in the interface between the BchX homodimer and the YZ protein. The YZ protein is the catalytic component, as it accepts electrons from the X protein and transfers them to the Chlide substrate via a [4Fe-4S] cluster, to produce 3-vinyl bacteriochlorophyllide a (3 V-BChlide). 3 V-BChlide is produced via Chlide rather than via 3,8-divinyl BChlide (81,82-didehydro-3 V-BChlide)
-
physiological function
-
chlorophyllide (Chlide) oxidoreductase, COR, is a unique BChl biosynthesis enzyme which shows distinct substrate recognition and hydrogen addition activities, depending on the host strain. COR in BChl a-producing phototrophic bacteria (a-COR) catalyzes the C7=C8 double bond reduction of Chlide a, whereas COR in BChl b- and BChl g-producing bacteria (b/g-COR) forms the C8-ethylidene group using DV-Chlide a as the substrate. Chlorophyllide oxidoreductase (COR) reduces the C7=C8 double bond of chlorophyllide a (Chlide a) bearing the C8-ethyl group, but also potentially catalyzes the reduction of the C8-vinyl group of divinyl-chlorophyllide a (DV-Chlide a). DV-Chlide a is a universal precursor for chlorophyll or bacteriochlorophyll biosynthesis in all photosynthetic organisms
-
physiological function
-
bacteriochlorophyll a (BChl) is an essential pigment for anoxygenic photosynthesis. In late steps of the BChl biosynthesis of Rhodobacter capsulatus, the C8 vinyl group and C7=C8 double bond of 8-vinyl chlorophyllide a (8 V-Chlide) are reduced by a C8 vinyl reductase (8VR), BciA (EC 1.3.1.75) or BciB (EC 1.3.7.13), and a nitrogenase-like enzyme, chlorophyllide a oxidoreductase (COR), respectively, to produce 3-vinyl-bacteriochlorphyllide a. The COR activity can act as a third 8VR, confirmed in vivo by the loss of 8VR activity mutants lacking bciA and genes encoding subunits of COR. In contrast to BciA and BciB, COR is a nitrogenase-like complex enzyme consisting of two separable components, the X protein (a BchX dimer) and the YZ protein (a BchY-BchZ heterotetramer). The X protein serves as the reductase component by transferring electrons from a [4Fe-4S] cluster held in the interface between the BchX homodimer and the YZ protein. The YZ protein is the catalytic component, as it accepts electrons from the X protein and transfers them to the Chlide substrate via a [4Fe-4S] cluster, to produce 3-vinyl bacteriochlorophyllide a (3 V-BChlide). 3 V-BChlide is produced via Chlide rather than via 3,8-divinyl BChlide (81,82-didehydro-3 V-BChlide)
-
physiological function
-
chlorophyllide (Chlide) oxidoreductase, COR, is a unique BChl biosynthesis enzyme which shows distinct substrate recognition and hydrogen addition activities, depending on the host strain. COR in BChl a-producing phototrophic bacteria (a-COR) catalyzes the C7=C8 double bond reduction of Chlide a, whereas COR in BChl b- and BChl g-producing bacteria (b/g-COR) forms the C8-ethylidene group using DV-Chlide a as the substrate. Chlorophyllide oxidoreductase (COR) reduces the C7=C8 double bond of chlorophyllide a (Chlide a) bearing the C8-ethyl group, but also potentially catalyzes the reduction of the C8-vinyl group of divinyl-chlorophyllide a (DV-Chlide a). DV-Chlide a is a universal precursor for chlorophyll or bacteriochlorophyll biosynthesis in all photosynthetic organisms
-
physiological function
-
the bchA locus contains three genes bchX, Y and Z, which are essential for the reduction of 2-devinyl-2-hydroxyethyl chlorophyllide a. BchX may supply electrons for reduction of 2-devinyl-2-hydroxyethyl chlorophyllide a
-
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Nomata, J.; Mizoguchi, T.; Tamiaki, H.; Fujita, Y.
A second nitrogenase-like enzyme for bacteriochlorophyll biosynthesis: reconstitution of chlorophyllide a reductase with purified X-protein (BchX) and YZ-protein (BchY-BchZ) from Rhodobacter capsulatus
J. Biol. Chem.
281
15021-15028
2006
Rhodobacter capsulatus
brenda
Kim, E.; Kim, J.; Rhee, H.; Lee, J.
Growth arrest of Synechocystis sp. PCC6803 by superoxide generated from heterologously expressed Rhodobacter sphaeroides chlorophyllide a reductase
FEBS Lett.
583
219-223
2009
Cereibacter sphaeroides (B9KK02), Cereibacter sphaeroides, Cereibacter sphaeroides KD131 (B9KK02)
brenda
Kim, E.J.; Kim, J.S.; Lee, I.H.; Rhee, H.J.; Lee, J.K.
Superoxide generation by chlorophyllide a reductase of Rhodobacter sphaeroides
J. Biol. Chem.
283
3718-3730
2008
Cereibacter sphaeroides (B9KK02), Cereibacter sphaeroides, Cereibacter sphaeroides KD131 (B9KK02)
brenda
McGlynn, P.; Hunter, C.N.
Genetic analysis of the bchC and bchA genes of Rhodobacter sphaeroides
Mol. Gen. Genet.
236
227-234
1993
Cereibacter sphaeroides (Q02431), Cereibacter sphaeroides DSM 158 (Q02431)
brenda
Harada, J.; Mizoguchi, T.; Tsukatani, Y.; Yokono, M.; Tanaka, A.; Tamiaki, H.
Chlorophyllide a oxidoreductase works as one of the divinyl reductases specifically involved in bacteriochlorophyll a biosynthesis
J. Biol. Chem.
289
12716-12726
2014
Cereibacter sphaeroides, Cereibacter sphaeroides J001
brenda
Nomata, J.; Terauchi, K.; Fujita, Y.
Stoichiometry of ATP hydrolysis and chlorophyllide formation of dark-operative protochlorophyllide oxidoreductase from Rhodobacter capsulatus
Biochem. Biophys. Res. Commun.
470
704-709
2016
Rhodobacter capsulatus
brenda
Kiesel, S.; Waetzlich, D.; Lange, C.; Reijerse, E.; Broecker, M.J.; Ruediger, W.; Lubitz, W.; Scheer, H.; Moser, J.; Jahn, D.
Iron-sulfur cluster-dependent catalysis of chlorophyllide a oxidoreductase from Roseobacter denitrificans
J. Biol. Chem.
290
1141-1154
2015
Roseobacter denitrificans
brenda
Gupta, R.S.; Khadka, B.
Evidence for the presence of key chlorophyll-biosynthesis-related proteins in the genus Rubrobacter (Phylum Actinobacteria) and its implications for the evolution and origin of photosynthesis
Photosynth. Res.
127
201-218
2016
no activity in Rubrobacter xylanophilus, no activity in Rubrobacter radiotolerans
brenda
Yamamoto, H.; Mizoguchi, T.; Tsukatani, Y.; Tamiaki, H.; Kurisu, G.; Fujita, Y.
Chlorophyllide a oxidoreductase preferentially catalyzes 8-vinyl reduction over B-ring reduction of 8-vinyl chlorophyllide a in the late steps of bacteriochlorophyll biosynthesis
ChemBioChem
21
1760-1766
2020
Rhodobacter capsulatus (P26177), Rhodobacter capsulatus, Rhodobacter capsulatus NBRC 16581 (P26177), Rhodobacter capsulatus ATCC BAA-309 (P26177), Rhodobacter capsulatus SB1003 (P26177)
brenda
Azai, C.; Kobayashi, M.; Mizoguchi, T.; Tamiaki, H.; Terauchi, K.; Tsukatani, Y.
Rapid C8-vinyl reduction of divinyl-chlorophyllide a by BciA from Rhodobacter capsulatus
J. Photochem. Photobiol. A
353
661-666
2018
Rhodobacter capsulatus (P26177 AND P26178 AND P26179), Rhodobacter capsulatus NBRC 16581 (P26177 AND P26178 AND P26179), Rhodobacter capsulatus ATCC BAA-309 (P26177 AND P26178 AND P26179), Rhodobacter capsulatus SB1003 (P26177 AND P26178 AND P26179)
-
brenda
Moser, J.; Jasper, J.; Ramos, J.; Sowa, S.; Layer, G.
Expression, purification, and activity analysis of chlorophyllide oxidoreductase and Ni2+-sirohydrochlorin a,c-diamide reductase
Methods Mol. Biol.
1876
125-140
2019
Roseobacter denitrificans (P26277 AND Q16DU8 AND Q16DU7), Roseobacter denitrificans ATCC 33942 (P26277 AND Q16DU8 AND Q16DU7)
brenda
Imhoff, J.; Rahn, T.; Kuenzel, S.; Neulinger, S.
Phylogeny of anoxygenic photosynthesis based on sequences of photosynthetic reaction center proteins and a key enzyme in bacteriochlorophyll biosynthesis, the chlorophyllide reductase
Microorganisms
7
576
2019
Proteobacteria, Chloroflexi, Chlorobi, Chloracidobacterium thermophilum b, Gemmatimonas phototrophica (A0A143BJ63 AND A0A143BQ39), Gemmatimonas phototrophica, Heliomicrobium modesticaldum (B0TBQ4 AND B0TBQ9 AND B0TBQ8), Heliomicrobium modesticaldum, Heliomicrobium modesticaldum Ice1 (B0TBQ4 AND B0TBQ9 AND B0TBQ8), Heliomicrobium modesticaldum ATCC 51547 (B0TBQ4 AND B0TBQ9 AND B0TBQ8)
brenda