Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1,1'-dimethyl-4,4'-bipyridinium dichloride + NADPH
NADPH + oxidized 1,1'-dimethyl-4,4'-bipyridinium dichloride
-
i.e. paraquat, a herbicide
-
-
?
hydrogen sulfide + 3 NADP+ + 3 H2O
sulfite + 3 NADPH + 3 H+
-
-
-
-
?
hydrogen sulfide + NADP+ + H2O
sulfite + NADPH + H+
-
-
-
-
?
hydroxylamine + NADPH
ammonia + NADP+
NADP+ + ferrocytochrome c
NADPH + H+ + ferricytochrome c
-
-
-
-
r
NADP+ + reduced methyl viologen
NADPH + oxidized methyl viologen
-
-
-
-
?
nitrite + NADPH
ammonia + NADP+
sulfite + 3 NADPH + 3 H+
hydrogen sulfide + 3 NADP+ + 3 H2O
sulfite + NADPH
hydrogen sulfide + NADP+ + H2O
-
-
-
-
?
sulfite + NADPH
sulfide + NADP+ + H2O
sulfite + NADPH + H+
sulfide + NADP+ + H2O
sulfite + reduced F420
sulfide + oxidized F420
-
-
-
-
?
additional information
?
-
hydroxylamine + NADPH
ammonia + NADP+
-
-
-
-
?
hydroxylamine + NADPH
ammonia + NADP+
-
-
-
?
hydroxylamine + NADPH
ammonia + NADP+
-
NADPH can be replaced by reduced methyl viologen
-
?
hydroxylamine + NADPH
ammonia + NADP+
-
-
-
-
?
nitrite + NADPH
ammonia + NADP+
-
-
-
-
?
nitrite + NADPH
ammonia + NADP+
-
-
-
?
nitrite + NADPH
ammonia + NADP+
-
-
-
?
nitrite + NADPH
ammonia + NADP+
-
NADPH can be replaced by reduced methyl viologen, the latter reaction is catalyzed by hemoprotein subunit alone
-
-
?
nitrite + NADPH
ammonia + NADP+
-
-
-
-
?
nitrite + NADPH
ammonia + NADP+
-
-
-
-
?
nitrite + NADPH
ammonia + NADP+
-
-
-
-
?
sulfite + 3 NADPH + 3 H+
hydrogen sulfide + 3 NADP+ + 3 H2O
-
-
-
-
?
sulfite + 3 NADPH + 3 H+
hydrogen sulfide + 3 NADP+ + 3 H2O
-
-
-
?
sulfite + 3 NADPH + 3 H+
hydrogen sulfide + 3 NADP+ + 3 H2O
-
-
-
?
sulfite + 3 NADPH + 3 H+
hydrogen sulfide + 3 NADP+ + 3 H2O
-
-
-
?
sulfite + 3 NADPH + 3 H+
hydrogen sulfide + 3 NADP+ + 3 H2O
-
essential enzyme in the global sulfur cycle
-
-
?
sulfite + 3 NADPH + 3 H+
hydrogen sulfide + 3 NADP+ + 3 H2O
the electron transfer occurs via multiple pathways, bypassing the need for electrons to move intra-molecularly from the NADH to the FAD to the FMN and then in cis to SiRHP. In this way, SiR effectively raises the local concentration of electrons relative to SiRHP active sites to facilitate the full six electron reduction of SO32- to S2-
-
-
?
sulfite + 3 NADPH + 3 H+
hydrogen sulfide + 3 NADP+ + 3 H2O
-
-
-
?
sulfite + NADPH
sulfide + NADP+ + H2O
-
-
-
-
?
sulfite + NADPH
sulfide + NADP+ + H2O
-
-
-
-
ir
sulfite + NADPH
sulfide + NADP+ + H2O
-
reduction of sulfite by reduced methyl viologen is catalyzed by hemoprotein subunit alone
-
-
?
sulfite + NADPH
sulfide + NADP+ + H2O
-
NADPH can be replaced by reduced methyl viologen
-
-
?
sulfite + NADPH
sulfide + NADP+ + H2O
-
NADPH can be replaced by reduced methyl viologen
-
?
sulfite + NADPH
sulfide + NADP+ + H2O
-
-
-
-
ir
sulfite + NADPH
sulfide + NADP+ + H2O
-
sole compound reduced
-
-
?
sulfite + NADPH
sulfide + NADP+ + H2O
-
-
-
-
?
sulfite + NADPH
sulfide + NADP+ + H2O
-
reduction of sulfite by reduced methyl viologen is catalyzed by hemoprotein subunit alone
-
-
?
sulfite + NADPH
sulfide + NADP+ + H2O
-
NADPH can be replaced by reduced methyl viologen
-
-
?
sulfite + NADPH
sulfide + NADP+ + H2O
-
benzyl viologen
-
-
?
sulfite + NADPH
sulfide + NADP+ + H2O
-
sole compound reduced
-
-
?
sulfite + NADPH
sulfide + NADP+ + H2O
-
-
-
-
?
sulfite + NADPH
sulfide + NADP+ + H2O
-
reduction of sulfite by reduced methyl viologen is catalyzed by hemoprotein subunit alone
-
-
?
sulfite + NADPH + H+
sulfide + NADP+ + H2O
-
no physiological nitrite reductase
-
-
?
sulfite + NADPH + H+
sulfide + NADP+ + H2O
-
-
-
-
?
additional information
?
-
the enzyme catalyzes the reduction of sulfite to sulfide
-
-
-
additional information
?
-
the enzyme catalyzes the reduction of sulfite to sulfide
-
-
-
additional information
?
-
the enzyme catalyzes the reduction of sulfite to sulfide
-
-
-
additional information
?
-
-
transfer of hydrogen from NADPH to 3-acetylpyridineadenine dinucleotide phosphate
-
-
?
additional information
?
-
-
transfer of hydrogen from NADPH to 3-acetylpyridineadenine dinucleotide phosphate
-
-
?
additional information
?
-
-
transfer of hydrogen from NADPH to 3-acetylpyridineadenine dinucleotide phosphate
-
-
?
additional information
?
-
-
reduction of sulfite, nitrite, and hydroxylamine by NADPH requires catalytic activities of both subunits, reduction of sulfite, nitrite, and hydroxylamine by methyl viologen requires hemoprotein subunit
-
-
?
additional information
?
-
-
reduction of sulfite, nitrite, and hydroxylamine by NADPH requires catalytic activities of both subunits, reduction of sulfite, nitrite, and hydroxylamine by methyl viologen requires hemoprotein subunit
-
-
?
additional information
?
-
-
reduction of sulfite, nitrite, and hydroxylamine by NADPH requires catalytic activities of both subunits, reduction of sulfite, nitrite, and hydroxylamine by methyl viologen requires hemoprotein subunit
-
-
?
additional information
?
-
-
reactions of FMN depleted enzyme
-
-
?
additional information
?
-
-
reactions catalyzed by flavoprotein subunit alone: transfer of electrons from NADPH to cytochrome c, ferricyanide, dichlorphenolindophenol, menadione, FMN, FAD, O2
-
-
?
additional information
?
-
-
reactions catalyzed by flavoprotein subunit alone: transfer of electrons from NADPH to cytochrome c, ferricyanide, dichlorphenolindophenol, menadione, FMN, FAD, O2
-
-
?
additional information
?
-
-
reactions catalyzed by flavoprotein subunit alone: transfer of electrons from NADPH to cytochrome c, ferricyanide, dichlorphenolindophenol, menadione, FMN, FAD, O2
-
-
?
additional information
?
-
-
reactions catalyzed by flavoprotein subunit alone: transfer of electrons from NADPH to cytochrome c, ferricyanide, dichlorphenolindophenol, menadione, FMN, FAD, O2
-
-
?
additional information
?
-
-
can generate tyrosil radicals e.g. for transfer of electrons to the iron center of metR2, small subunit of ribonucletide reductase
-
-
?
additional information
?
-
-
transfer of hydrogen from NADPH to 3-acetylpyridineadenine dinucleotide phosphate
-
-
?
additional information
?
-
-
reduction of sulfite, nitrite, and hydroxylamine by NADPH requires catalytic activities of both subunits, reduction of sulfite, nitrite, and hydroxylamine by methyl viologen requires hemoprotein subunit
-
-
?
additional information
?
-
-
reactions of FMN depleted enzyme
-
-
?
additional information
?
-
-
overview on assay methods
-
-
?
additional information
?
-
-
reactions catalyzed by flavoprotein subunit alone: transfer of electrons from NADPH to cytochrome c, ferricyanide, dichlorphenolindophenol, menadione, FMN, FAD, O2
-
-
?
additional information
?
-
-
reactions catalyzed by flavoprotein subunit alone: transfer of electrons from NADPH to cytochrome c, ferricyanide, dichlorphenolindophenol, menadione, FMN, FAD, O2
-
-
?
additional information
?
-
-
reactions catalyzed by flavoprotein subunit alone: transfer of electrons from NADPH to cytochrome c, ferricyanide, dichlorphenolindophenol, menadione, FMN, FAD, O2
-
-
?
additional information
?
-
-
reactions catalyzed by flavoprotein subunit alone: transfer of electrons from NADPH to cytochrome c, ferricyanide, dichlorphenolindophenol, menadione, FMN, FAD, O2
-
-
?
additional information
?
-
-
by production of the population synchronizer H2S involved in ultradian metabolic oscillation
-
-
?
additional information
?
-
-
transfer of hydrogen from NADPH to 3-acetylpyridineadenine dinucleotide phosphate
-
-
?
additional information
?
-
-
transfer of hydrogen from NADPH to 3-acetylpyridineadenine dinucleotide phosphate
-
-
?
additional information
?
-
-
reduction of sulfite, nitrite, and hydroxylamine by NADPH requires catalytic activities of both subunits, reduction of sulfite, nitrite, and hydroxylamine by methyl viologen requires hemoprotein subunit
-
-
?
additional information
?
-
-
reduction of sulfite, nitrite, and hydroxylamine by NADPH requires catalytic activities of both subunits, reduction of sulfite, nitrite, and hydroxylamine by methyl viologen requires hemoprotein subunit
-
-
?
additional information
?
-
-
reactions of FMN depleted enzyme
-
-
?
additional information
?
-
-
reactions catalyzed by flavoprotein subunit alone: transfer of electrons from NADPH to cytochrome c, ferricyanide, dichlorphenolindophenol, menadione, FMN, FAD, O2
-
-
?
additional information
?
-
-
reactions catalyzed by flavoprotein subunit alone: transfer of electrons from NADPH to cytochrome c, ferricyanide, dichlorphenolindophenol, menadione, FMN, FAD, O2
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Hatefi, Y.; Stiggall, D.L.
Metal-containing flavoprotein dehydrogenases
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
13
175-297
1976
Saccharomyces cerevisiae, Escherichia coli, Neurospora crassa, Salmonella enterica subsp. enterica serovar Typhimurium
-
brenda
Coves, J.; Niviere, V.; Eschenbrenner, M.; Fontecave, M.
NADPH-Sulfite reductase from Escherichia coli. A flavin reductase participating in the generation of the free radical of ribonucleotide reductase
J. Biol. Chem.
268
18604-18609
1993
Escherichia coli
brenda
Ostrowski, J.; Barber, M.J.; Rueger, D.C.; Miller, B.E.; Siegel, L.M.; Kredich, N.M.
Characterization of the flavoprotein moieties of NADPH-sulfite reductase from Salmonella typhimurium and Escherichia coli. Physicochemical and catalytic properties, amino acid sequence deduced from DNA sequence of cysJ, and comparison with NADPH-cytochrome P-450 reductase
J. Biol. Chem.
264
15796-15808
1989
Escherichia coli, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Young, L.J.; Siegel, L.M.
Activated conformers of Escherichia coli sulfite reductase heme protein subunit [published erratum appears in Biochemistry 1988 Dec 27;27(26):9226]
Biochemistry
27
4991-4999
1988
Escherichia coli
brenda
McRee, D.E.; Richardson, D.C.; Richardson, J.S.; Siegel, L.M.
The heme and Fe4S4 cluster in the crystallographic structure of Escherichia coli sulfite reductase
J. Biol. Chem.
261
10277-10281
1986
Escherichia coli
brenda
Kobayashi, K.; Yoshimoto, A.
Studies on yeast sulfite reductase. V. Effects of ionic strength on enzyme activities
Biochim. Biophys. Acta
709
38-45
1982
Saccharomyces cerevisiae
brenda
Kobayashi, K.; Yoshimoto, A.
Studies on yeast sulfite reductase. VI. Use of the effects of ionic strength as a probe for enzyme structure and mechanism
Biochim. Biophys. Acta
709
46-52
1982
Saccharomyces cerevisiae
brenda
Kobayashi, K.; Yoshimoto, A.
Studies on yeast sulfite reductase. IV. Structure and steady-state kinetics
Biochim. Biophys. Acta
705
348-356
1982
Saccharomyces cerevisiae
brenda
Siegel, L.M.; Rueger, D.C.; Barber, M.J.; Krueger, R.J.; Orme-Johnson, N.R.; Orme-Johnson, W.H.
Escherichia coli sulfite reductase hemoprotein subunit. Prosthetic groups, catalytic parameters, and ligand complexes
J. Biol. Chem.
257
6343-6350
1982
Escherichia coli
brenda
Dott, W.; Truper, H.G.
Sulfite formation by wine yeasts III. Properties of sulfite reductase.
Arch. Microbiol.
108
99-104
1976
Saccharomyces cerevisiae, Saccharomyces bayanus
-
brenda
Murphy, M.J.; Siegel, L.M.; Kamin, H.
Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. VI. The reaction of carbon monoxide with the Escherichia coli holoenzyme, the hemoprotein, and free siroheme
J. Biol. Chem.
249
1610-1614
1974
Escherichia coli
brenda
Siegel, L.M.; Davis, P-S.
Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. IV. The Escherichia coli hemoflavoprotein: subunit structure and dissociation into hemoprotein and flavoprotein components
J. Biol. Chem.
249
1587-1598
1974
Escherichia coli
brenda
Faeder, E.J.; Davis, P.S.; Siegel, L.M.
Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. V. Studies with the Escherichia coli hemoflavoprotein depleted of flavin mononucleotide: distinct roles for the flavin adenine dinucleotide and flavin mononucleotide prosthetic groups in catalysis
J. Biol. Chem.
249
1599-1609
1974
Escherichia coli
brenda
Siegel, L.M.; Davis, P.S.; Kamin, H.
Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. 3. The Escherichia coli hemoflavoprotein: catalytic parameters and the sequence of electron flow
J. Biol. Chem.
249
1572-1586
1974
Escherichia coli
brenda
Murphy, M.J.; Siegel, L.M.
Siroheme and sirohydrochlorin. The basis for a new type of porphyrin-related prosthetic group common to both assimilatory and dissimilatory sulfite reductases
J. Biol. Chem.
248
6911-6919
1973
Desulfotomaculum nigrificans
brenda
Murphy, M.J.; Siegel, L.M.; Kamin, H.
Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. II. Identification of a new class of heme prosthetic group: an iron-tetrahydroporphyrin (isobacteriochlorin type) with eight carboxylic acid groups
J. Biol. Chem.
248
2801-2814
1973
Escherichia coli
brenda
Siegel, L.M.; Murphy, M.J.; Kamin, H.
Reduced nicotinamide adenine dinucleotide phosphate-sulfite reductase of enterobacteria. I. The Escherichia coli hemoflavoprotein: molecular parameters and prosthetic groups
J. Biol. Chem.
248
251-264
1973
Escherichia coli
brenda
Siegel, L.M.; Kamin, H.
TPNH-Sulfite reductase (Escherichia coli)
Methods Enzymol.
17B
539-545
1971
Escherichia coli
-
brenda
Yoshimoto, A.; Naiki, N.; Sato, R.
Sulfite reductase (bakers yeast)
Methods Enzymol.
17B
520-528
1971
Saccharomyces cerevisiae
-
brenda
Hoeksema, W.D.; Schoenhard, D.E.
Characterization of a thermolabile sulfite reductase from Salmonella pullorum
J. Bacteriol.
108
154-158
1971
Salmonella enterica subsp. enterica serovar Pullorum
brenda
Yoshimoto, A.; Sato, R.
Studies on yeast sulfite reductase. I. Purification and characterization
Biochim. Biophys. Acta
153
555-575
1968
Saccharomyces cerevisiae
brenda
Yoshimoto, A.; Sato, R.
Studies on yeast sulfite reductase. II. Partial purification and properties of genetically incomplete sulfite reductases
Biochim. Biophys. Acta
153
576-588
1968
Saccharomyces cerevisiae
brenda
Prabhakararao, K.; Nicholas, D.J.D.
Sulphite reductase from bakers yeast: a haemoflavoprotein
Biochim. Biophys. Acta
180
253-263
1969
Saccharomyces cerevisiae
brenda
Yoshimoto, A.; Sato, R.
Studies on yeast sulfite reductase. 3. Further characterization
Biochim. Biophys. Acta
220
190-205
1970
Saccharomyces cerevisiae
brenda
Tei, H.; Murata, K.; Kimura, A.
Molecular cloning of the cys genes (cysC, cysD, cysH, cysI, cysJ, and cysG) responsible for cysteine biosynthesis in Escherichia coli K-12
Biotechnol. Appl. Biochem.
12
212-216
1990
Escherichia coli
brenda
Li, C.; Peck, H.D.; Przybyla, A.E.
Cloning of the 3-phosphoadenylyl sulfate reductase and sulfite reductase genes from Escherichia coli K-12
Gene
53
227-234
1987
Escherichia coli
brenda
McRee, D.E.; Richardson, D.C.
Preliminary X-ray diffraction studies on the hemoprotein subunit of Escherichia coli sulfite reductase
J. Mol. Biol.
154
179-180
1982
Escherichia coli
brenda
Scott, A.I.; Irwin, A.J.; Siegel, L.M.; Schoolery, J.N.
Sirohydrochlorin. Prosthetic group of sulfite and nitrite reductases and its role in the biosynthesis of vitamin B12
J. Am. Chem. Soc.
100
7987-7994
1978
Propionibacterium freudenreichii subsp. shermanii
-
brenda
Arendsen, A.F.; Verhagen, M.F.J.M.; Wolbert, R.B.G.; Pierik, A.J.; Stams, A.J.M.; Jetten, M.S.M.; Hagen, W.R.
The dissimilatory sulfite reductase from Desulfosarcina variabilis is a desulforubidin containing uncoupled metalated sirohemes and S = 9/2 iron-sulfur clusters
Biochemistry
32
10323-10330
1993
Desulfosarcina variabilis
brenda
Coves, J.; Zeghouf, M.; Macherel, D.; Guigliarelli, B.; Asso, M.; Fontecave, M.
Flavin mononucleotide-binding domain of the flavoprotein component of the sulfite reductase from Escherichia coli
Biochemistry
36
5921-5928
1997
Escherichia coli
brenda
Coves, J.; Lebrun, C.; Gervasi, G.; Dalbon, P.; Fontecave, M.
Overexpression of the FAD-binding domain of the sulphite reductase flavoprotein component from Escherichia coli and its inhibition by iodonium diphenyl chloride
Biochem. J.
342
465-472
1999
Escherichia coli
brenda
Willson, P.J.; Gerlach, G.F.; Klashinsky, S.; Potter, A.A.
Cloning and characterization of the gene coding for NADPH-sulfite reductase hemoprotein from Actinobacillus pleuropneumoniae and use of the protein product as a vaccine
Can. J. Vet. Res.
65
206-212
2001
Actinobacillus pleuropneumoniae
brenda
Gaudu, P.; Fontecave, M.
The NADPH:sulfite reductase of Escherichia coli is a paraquat reductase
Eur. J. Biochem.
226
459-463
1994
Escherichia coli
brenda
Eschenbrenner, M.; Coves, J.; Fontecave, M.
NADPH-sulfite reductase flavoprotein from Escherichia coli: contribution to the flavin content and subunit interaction
FEBS Lett.
374
82-84
1995
Escherichia coli
brenda
Gruez, A.; Pignol, D.; Zeghouf, M.; Coves, J.; Fontecave, M.; Ferrer, J.L.; Fontecilla-Camps, J.C.
Four Crystal Structures of the 60 kDa Flavoprotein Monomer of the Sulfite Reductase Indicate a Disordered Flavodoxin-like Module
J. Mol. Biol.
299
199-212
2000
Escherichia coli (P38038), Escherichia coli
brenda
Sohn, H.Y.; Kuriyama, H.
Ultradian metabolic oscillation of Saccharomyces cerevisiae during aerobic continuous culture: hydrogen sulphide, a population synchronizer, is produced by sulphite reductase
Yeast
18
125-135
2001
Saccharomyces cerevisiae
brenda
Gruez, A.; Zeghouf, M.; Bertrand, J.; Eschenbrenner, M.; Coves, J.; Fontecave, M.; Pignol, D.; Fontecilla-Camps, J.C.
The FNR-like domain of the Escherichia coli sulfite reductase flavoprotein component: crystallization and preliminary X-ray analysis
Acta Crystallogr. Sect. D
54
135-136
1998
Escherichia coli
brenda
Yin, L.J.; Lin, H.Y.; Jiang, S.T.
Purification and characterization of Escherichia coli sulfite reductase and its application in surimi processing
J. Food Sci.
67
3329-3334
2002
Escherichia coli
brenda
Johnson, E.F.; Mukhopadhyay, B.
A new type of sulfite reductase, a novel coenzyme F420-dependent enzyme, from the methanarchaeon Methanocaldococcus jannaschii
J. Biol. Chem.
280
38776-38786
2005
Methanocaldococcus jannaschii
brenda
Zeng, J.; Wang, M.; Zhang, X.; Wang, Y.; Ai, C.; Liu, J.; Qiu, G.
Expression, purification and characterization of the sulfite reductase hemo-subunit, SiR-HP, from Acidithiobacillus ferrooxidans
Biotechnol. Lett.
30
1239-1244
2008
Acidithiobacillus ferrooxidans
brenda
Cordente, A.G.; Heinrich, A.; Pretorius, I.S.; Swiegers, J.H.
Isolation of sulfite reductase variants of a commercial wine yeast with significantly reduced hydrogen sulfide production
FEMS Yeast Res.
9
446-459
2009
Saccharomyces cerevisiae
brenda
Miller, E.N.; Jarboe, L.R.; Turner, P.C.; Pharkya, P.; Yomano, L.P.; York, S.W.; Nunn, D.; Shanmugam, K.T.; Ingram, L.O.
Furfural inhibits growth by limiting sulfur assimilation in ethanologenic Escherichia coli strain LY180
Appl. Environ. Microbiol.
75
6132-6141
2009
Escherichia coli, Escherichia coli LY180
brenda
Askenasy, I.; Pennington, J.M.; Tao, Y.; Marshall, A.G.; Young, N.L.; Shang, W.; Stroupe, M.E.
The N-terminal domain of Escherichia coli assimilatory NADPH-sulfite reductase hemoprotein is an oligomerization domain that mediates holoenzyme assembly
J. Biol. Chem.
290
19319-19333
2015
Escherichia coli (P17846), Escherichia coli
brenda
Gholami-Shabani, M.; Shams-Ghahfarokhi, M.; Gholami-Shabani, Z.; Akbarzadeh, A.; Riazi, G.; Ajdari, S.; Amani, A.; Razzaghi-Abyaneh, M.
Enzymatic synthesis of gold nanoparticles using sulfite reductase purified from Escherichia coli A green eco-friendly approach
Process Biochem.
50
1076-1085
2015
Escherichia coli, Escherichia coli PTCC 1330
-
brenda
Askenasy, I.; Murray, D.T.; Andrews, R.M.; Uversky, V.N.; He, H.; Stroupe, M.E.
Structure-function relationships in the oligomeric NADPH-dependent assimilatory sulfite reductase
Biochemistry
57
3764-3772
2018
Escherichia coli
brenda
Cepeda, M.R.; McGarry, L.; Pennington, J.M.; Krzystek, J.; Stroupe, M.E.
The role of extended Fe4S4 cluster ligands in mediating sulfite reductase hemoprotein activity
Biochim. Biophys. Acta Proteins Proteom.
1866
933-940
2018
Escherichia coli (P17846), Escherichia coli K12 (P17846)
brenda
Nguyen, P.T.; Toh-E, A.; Nguyen, N.H.; Imanishi-Shimizu, Y.; Watanabe, A.; Kamei, K.; Shimizu, K.
Identification and characterization of a sulfite reductase gene and new insights regarding the sulfur-containing amino acid metabolism in the basidiomycetous yeast Cryptococcus neoformans
Curr. Genet.
67
115-128
2021
Cryptococcus neoformans var. neoformans (Q5KDH3), Cryptococcus neoformans var. neoformans ATCC MYA-565 (Q5KDH3), Cryptococcus neoformans var. neoformans JEC21 (Q5KDH3)
brenda
Tavolieri, A.M.; Murray, D.T.; Askenasy, I.; Pennington, J.M.; McGarry, L.; Stanley, C.B.; Stroupe, M.E.
NADPH-dependent sulfite reductase flavoprotein adopts an extended conformation unique to this diflavin reductase
J. Struct. Biol.
205
170-179
2019
Escherichia coli (W8SX42)
brenda
Murray, D.T.; Weiss, K.L.; Stanley, C.B.; Nagy, G.; Stroupe, M.E.
Small-angle neutron scattering solution structures of NADPH-dependent sulfite reductase
J. Struct. Biol.
213
107724
2021
Escherichia coli (W8SX42 AND P17846)
brenda