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H2 + (sulfide)n = hydrogen sulfide + (sulfide)n-1
H2 + (sulfide)n = hydrogen sulfide + (sulfide)n-1
mechanism
-
H2 + (sulfide)n = hydrogen sulfide + (sulfide)n-1
sulfur can be reduced with hydrogen as donor in the presence of hydrogenase
-
H2 + (sulfide)n = hydrogen sulfide + (sulfide)n-1
sulfur can be reduced with hydrogen as donor in the presence of hydrogenase
-
H2 + (sulfide)n = hydrogen sulfide + (sulfide)n-1
two enzymes are involved in the production of H2S: the sulfur reductase and the thiosulfate reductase
thermophilic iron-oxidizing bacterium strain TI-1
-
H2 + (sulfide)n = hydrogen sulfide + (sulfide)n-1
two enzymes: hydrogenase with sulfur reductase activity and an NADPH-utilizing polysulfide dehydrogenase are detected
-
H2 + (sulfide)n = hydrogen sulfide + (sulfide)n-1
polysulfide appears to be the soluble intermediate in the sulfur reduction
-
H2 + (sulfide)n = hydrogen sulfide + (sulfide)n-1
a sulfur-reducing complex including hydrogenase, a sulfur reductase and electron-transferring components described
-
H2 + (sulfide)n = hydrogen sulfide + (sulfide)n-1
a sulfur-reducing complex including hydrogenase, a sulfur reductase and electron-transferring components described
-
H2 + (sulfide)n = hydrogen sulfide + (sulfide)n-1
two proteins occur: polysulfide reductase and sulfide dehydrogenase or Sud or flavo-cytochrome-C-sulfide dehydrogenase or polysulfide-sulfur transferase, CAS REG. NO.: 128826-29-9, EC Number: 1.8._._, the second enzyme has been proposed to transfer polysulfide-sulfur to the active site of polysulfide reductase
-
H2 + (sulfide)n = hydrogen sulfide + (sulfide)n-1
-
-
-
-
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disulfide + electron donor
H2S
-
cystine and cystamine, minimal activities, PDH
-
?
H2 + benzyl viologen
H2S + reduced benzyl viologen
highest activity
-
-
?
H2 + methyl viologen
H2S + reduced methyl viologen
H2 + NADP+
H2S + NADPH + H+
-
-
-
-
r
H2 + polysulfide(n)
H2S + polysulfide(n-1)
H2S + NADH + H+
H2 + NAD+
-
NADH is a very inefficient electron carrier for sulfhydrogenase
-
-
r
H2S + NADPH + H+
H2 + NADP+
-
-
-
-
r
NADPH + H+ + polysulfide(n)
NADP+ + polysulfide(n-1)
-
-
-
r
organic trisulfides + electron donor
H2S + oxidized electron donor
polysulfide + electron donor
H2S + oxidized electron donor
polysulfide + H2
H2S
-
-
-
-
?
sulfur + electron donor
H2S + oxidized electron donor
sulfur + H2
H2S
-
in solubilized membrane fraction no activity is detected without the addition of electron carriers: 2,3-dimethylnaphthoquinone, plastoquinone or horse heart cytochrome c
-
-
?
tetrasulfide + electron donor
H2S + oxidized electron donor
-
comparable to colloidal sulfur
-
?
tetrathionate + H2
? + H+
-
-
-
-
?
additional information
?
-
H2 + methyl viologen
H2S + reduced methyl viologen
-
-
-
-
r
H2 + methyl viologen
H2S + reduced methyl viologen
-
-
-
?
H2 + polysulfide(n)
H2S + polysulfide(n-1)
-
-
-
-
r
H2 + polysulfide(n)
H2S + polysulfide(n-1)
-
-
-
r
organic trisulfides + electron donor
H2S + oxidized electron donor
-
-
-
-
?
organic trisulfides + electron donor
H2S + oxidized electron donor
-
i.e. (R-S-S-S-R)2, R: CH2CH2NH2
-
?
organic trisulfides + electron donor
H2S + oxidized electron donor
-
i.e. (R-S-S-S-R)2, R: CH2CH2NH2
-
-
?
organic trisulfides + electron donor
H2S + oxidized electron donor
-
R: CH2CH(COOH)NH2, CH2CH2SO3Na or CH2CH2COONa, reduced at a rate comparable to elemental sulfur
-
?
polysulfide + electron donor
H2S + oxidized electron donor
-
-
-
?
polysulfide + electron donor
H2S + oxidized electron donor
-
comparable to colloidal sulfur
-
?
polysulfide + electron donor
H2S + oxidized electron donor
-
highest activity, NADH and NADPH as electron donors for PDH, hydrogen alone can reduce polysulfide via sulfhydrogenase, but the amount of this activity is minimal compared with that of PDH
-
-
?
polysulfide + electron donor
H2S + oxidized electron donor
-
-
-
-
?
polysulfide + electron donor
H2S + oxidized electron donor
-
polysulfide appears to be the soluble intermediate in the sulfur reduction, electron-transport-coupled phosphorylation
-
?
polysulfide + electron donor
H2S + oxidized electron donor
-
polysulfide appears to be the soluble intermediate in the sulfur reduction, electron-transport-coupled phosphorylation
-
-
?
sulfur
H2S
-
constitutive membrane-bound enzyme
-
?
sulfur
H2S
-
constitutive membrane-bound enzyme
-
?
sulfur
H2S
-
reduction is coupled to the phosphorylation of ADP with phosphate in the catabolism of some anaerobic microorganisms
-
?
sulfur
H2S
-
functional sulfur reductase that operates in the electron transport chain from fumarate to sulfur together with formate dehydrogenase, a membrane-bound and a cytoplasmic sulfur reductase
-
?
sulfur
H2S
-
reduction is coupled to the phosphorylation of ADP with phosphate in the catabolism of some anaerobic microorganisms
-
?
sulfur + electron donor
H2S + oxidized electron donor
-
-
-
-
?
sulfur + electron donor
H2S + oxidized electron donor
-
-
-
-
?
sulfur + electron donor
H2S + oxidized electron donor
-
-
-
?
sulfur + electron donor
H2S + oxidized electron donor
-
-
-
?
sulfur + electron donor
H2S + oxidized electron donor
-
-
-
?
sulfur + electron donor
H2S + oxidized electron donor
-
-
-
?
sulfur + electron donor
H2S + oxidized electron donor
-
-
-
?
sulfur + electron donor
H2S + oxidized electron donor
-
-
-
?
sulfur + electron donor
H2S + oxidized electron donor
-
-
-
?
sulfur + electron donor
H2S + oxidized electron donor
-
-
-
?
sulfur + electron donor
H2S + oxidized electron donor
-
-
-
-
?
sulfur + electron donor
H2S + oxidized electron donor
-
electron donor: molecular hydrogen
-
-
?
sulfur + electron donor
H2S + oxidized electron donor
-
-
-
?
sulfur + electron donor
H2S + oxidized electron donor
-
-
-
?
sulfur + electron donor
H2S + oxidized electron donor
-
elemental: best results with colloidal Janek sulfur, hydrophilic sulfur yields generally lower activities
-
?
sulfur + electron donor
H2S + oxidized electron donor
thermophilic iron-oxidizing bacterium strain TI-1
-
electron donor: NADH, NADPH not
-
-
?
sulfur + electron donor
H2S + oxidized electron donor
-
electron donor: NADH or NAPDH
-
-
?
sulfur + electron donor
H2S + oxidized electron donor
-
electron donor: molecular hydrogen
-
?
sulfur + electron donor
H2S + oxidized electron donor
-
electron donor: molecular hydrogen
-
?
sulfur + electron donor
H2S + oxidized electron donor
-
electron donor: formate
-
?
sulfur + electron donor
H2S + oxidized electron donor
-
electron donor: formate
CO2
?
sulfur + electron donor
H2S + oxidized electron donor
-
colloidal sulfur but not sulfur flower or precipitated sulfur
-
?
additional information
?
-
-
no substrate: dimethyl sulfoxide, thiosulfate. Presence of NADPH increases the sulfur reducing activity. Hydrogenase reaction ond sulfur reduction by enzyme are energetically coupled but take place in two separate complexes. Electron transfer is mediated by quinones
-
-
?
additional information
?
-
ferredoxin from Pyrococcus furiosus is not an efficient electron carrier
-
-
?
additional information
?
-
-
ferredoxin from Pyrococcus furiosus is not an efficient electron carrier
-
-
?
additional information
?
-
-
ferredoxin is not an effective electron donor for Pyrococcus furiosus sulfhydrogenase. NAD+ is not reduced
-
-
?
additional information
?
-
-
sulfur can be reduced by photochemical reduction in the presence of phenosafranin
-
-
?
additional information
?
-
-
sulfur can be reduced by photochemical reduction in the presence of phenosafranin
-
-
?
additional information
?
-
-
sulfur can be reduced by photochemical reduction in the presence of phenosafranin
-
-
?
additional information
?
-
-
no substrates are sulfite, thiosulfate, tetrathionate
-
-
?
additional information
?
-
thermophilic iron-oxidizing bacterium strain TI-1
-
no substrates are sulfite, thiosulfate, tetrathionate
-
-
?
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dimer
-
2 * 85000, SDS-PAGE
homodimer
thermophilic iron-oxidizing bacterium strain TI-1
-
2 * 48000, SDS-PAGE
monomer
-
1 * 85033, calculated and crystallization data
tetramer
heterotetrameric complex where the alpha and delta subunits function as a hydrogenase (EC 1.12.1.3) while the beta and gamma subunits function as sulfur reductase
heterotetramer
-
four subunits, alpha: 45000, beta: 43000, gamma: 31000, delta: 28000, SDS-PAGE
heterotetramer
1 * 52000 + 1 * 39000 + 1 * 30000 + 1 * 24000, SDS-PAGE
heterotetramer
alphabetagammadelta hetreotetramer, 1 * 48700 + 1 * 41800 + 33200 + 29600
additional information
-
four subunits: 110000, 66000, 39000 and 29000 Da
additional information
-
three subunits: 54000, 36000 and 35000 Da, SDS-PAGE
additional information
-
three subunits: 54000, 36000 and 35000 Da, SDS-PAGE
-
additional information
-
nine major polypeptides with molecular masses of 82000, 72000, 65000, 50000, 47000, 42000, 40000, 30000 and 24000 Da
additional information
-
nine major polypeptides with molecular masses of 82000, 72000, 65000, 50000, 47000, 42000, 40000, 30000 and 24000 Da
additional information
-
SDS-PAGE, Psr A: 85000 Da and Psr B: 23000 Da, amount to approximately 70% of the total protein and are present at nearly equimolar quantities, Psr C not identified
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Zphel, A.; Kennedy, M.C.; Beinert, H.; Kroneck, P.M.H.
Investigations on microbial sulfur respiration
Arch. Microbiol.
150
72-77
1988
Desulfomicrobium baculatum, Desulfuromonas acetoxidans, Desulfuromonas acetexigens, Desulfuromusa succinoxidans, Sulfurospirillum deleyianum, Desulfuromonas acetexigens 2873, Desulfomicrobium baculatum 9974, Desulfuromonas acetoxidans 5071, Desulfuromusa succinoxidans Go20
-
brenda
Schrder, I.; Krger, A.; Macy, J.M.
Isolation of the sulphur reductase and reconstittutions of the sulphur respiration of Wolinella succinogenes
Arch. Microbiol.
149
572-579
1988
Wolinella succinogenes
-
brenda
Zphel, A.; Kennedy, M.C.; Beinert, H.; Kroneck, P.M.H.
Investigations on microbial sulfur respiration. Isolation, purification, and characterization of cellular components from Spirillum 5175
Eur. J. Biochem.
195
849-856
1991
Sulfurospirillum deleyianum
brenda
Klimmek, O.; Stein, T.; Pisa, R.; Simon, J.; Kroger, A.
The single cysteine residue of the Sud protein is required for its function as a polysulfide-sulfur transferase in Wolinella succinogenes
Eur. J. Biochem.
263
79-84
1999
Wolinella succinogenes
brenda
Fauque, G.D.; Klimmek, O.; Kroger, A.
Sulfur reductases from spirilloid mesophilic sulfur-reducing eubacteria
Methods Enzymol.
243
367-383
1994
Sulfurospirillum deleyianum, Wolinella succinogenes
-
brenda
Jankielewicz, A.; Schmitz, R.A.; Klimmek, O.; Kroeger, A.
Polysulfide reductase and formate dehydrogenase from Wolinella succinogenes contain molybdopterin guanine dinucleotide
Arch. Microbiol.
162
238-242
1994
Wolinella succinogenes
-
brenda
Arendsen, A.F.; Veenhuizen, P.T.M.; Hagen, W.R.
Redox properties of the sulfhydrogenase from Pyrococcus furiosus
FEBS Lett.
368
117-121
1995
Pyrococcus furiosus
brenda
Childers, S.E.; Noll, K.M.
Characterization and regulation of sulfur reductase activity in Thermotoga neapolitana
Appl. Environ. Microbiol.
60
2622-2626
1994
Thermotoga neapolitana
brenda
Dirmeier, R.; Keller, M.; Frey, G.; Huber, H.; Stetter, K.O.
Purification and properties of an extremely thermostable membrane-bound sulfur-reducing complex from the hyperthermophilic Pyrodictium abyssi
Eur. J. Biochem.
252
486-491
1998
Pyrodictium abyssi
brenda
Sugio, T.; Oda, K.; Matsumoto, K.; Takai, M.; Wakasa, S.; Kamimura, K.
Purification and characterization of sulfur reductase from a moderately thermophilic bacterial strain, TI-1, that oxidizes iron
Biosci. Biotechnol. Biochem.
62
705-709
1998
thermophilic iron-oxidizing bacterium strain TI-1
brenda
Keller, M.; Dirmeier, R.
Hydrogen-sulfur oxidoreductase complex from Pyrodictium abyssi
Methods Enzymol.
331
442-451
2001
Pyrodictium abyssi
brenda
Laska, S.; Kletzin, A.
Improved purification of the membrane-bound hydrogenase-sulfur-reductase complex from thermophilic archaea using e-aminocaproic acid-containing chromatography buffers
J. Chromatogr. B
737
151-160
2000
Acidianus ambivalens
brenda
Ng, K.Y.; Sawada, P.; Inoue, S.; Kamimura, K.; Sugio, T.
Purification and some properties of sulfur reductase from the iron-oxidizing bacterium Thiobacillus ferrooxidans NASF-1
J. Biosci. Bioeng.
90
199-203
2000
Acidithiobacillus ferrooxidans, Acidithiobacillus ferrooxidans NASF-1
brenda
Ma, K.; Weiss, R.; Adams, M.W.W.
Characterization of hydrogenase II from the hyperthermophilic archaeon Pyrococcus furiosus and assessment of its role in sulfur reduction
J. Bacteriol.
182
1864-1871
2000
Pyrococcus furiosus (E7FHC4 and E7FHN9 and E7FHW8 and E7FHF8), Pyrococcus furiosus
brenda
Ma, K.; Schicho, R.N.; Kelly, R.M.; Adams, M.W.W.
Hydrogenase of the hyperthermophile Pyrococcus furiosus is an elemental sulfur reductase or sulfhydrogenase: Evidence for a sulfur-reducing hydrogenase ancestor
Proc. Natl. Acad. Sci. USA
90
5341-5344
1993
Pyrococcus furiosus
brenda
Laska, S.; Lottspeich, F.; Kletzin, A.
Membrane-bound hydrogenase and sulfur reductase of the hyperthermophilic and acidophilic archaeon Acidianus ambivalens
Microbiology
149
2357-2371
2003
Acidianus ambivalens
brenda
Guiral, M.; Tron, P.; Aubert, C.; Gloter, A.; Iobbi-Nivol, C.; Giudici-Orticoni, M.T.
A membrane-bound multienzyme, hydrogen-oxidizing, and sulfur-reducing complex from the hyperthermophilic bacterium Aquifex aeolicus
J. Biol. Chem.
280
42004-42015
2005
Aquifex aeolicus
brenda
Schneider, F.; Lowe, F.; Huber, R.; Schindelin, H.; Kisker, C.; Knablein, J.
Crystal structure of dimethyl sulfoxide reductase from Rhodobacter capsulatus at 1.88 Ang resolution
J. Mol. Biol.
263
53-69
1996
Rhodobacter capsulatus
brenda
Yang, H.; Lipscomb, G.L.; Keese, A.M.; Schut, G.J.; Thomm, M.; Adams, M.W.; Wang, B.C.; Scott, R.A.
SurR regulates hydrogen production in Pyrococcus furiosus by a sulfur-dependent redox switch
Mol. Microbiol.
77
1111-1122
2010
Pyrococcus furiosus
brenda
Ma, K.; Hao, Z.; Adams, M.
Hydrogen production from pyruvate by enzymes purified from the hyperthermophilic archaeon, Pyrococcus furiosus: A key role for NADPH
FEMS Microbiol. Lett.
122
245-250
1994
Pyrococcus furiosus
-
brenda
Pedroni, P.; Della Volpe, A.; Galli, G.; Mura, G.M.; Pratesi, C.; Grandi, G.
Characterization of the locus encoding the [Ni-Fe] sulfhydrogenase from the archaeon Pyrococcus furiosus: evidence for a relationship to bacterial sulfite reductases
Microbiology
141
449-458
1995
Pyrococcus furiosus (E7FI44 and Q8U2E5 and E7FHU4 and Q8U2E4), Pyrococcus furiosus
brenda
Silva, P.; De Castro, B.; Hagen, W.
On the prosthetic groups of the NiFe sulfhydrogenase from Pyrococcus furiosus Topology, structure, and temperature-dependent redox chemistry
J. Biol. Inorg. Chem.
4
284-291
1999
Pyrococcus furiosus (E7FI44 AND Q8U2E5 AND Q8U2E4 AND E7FHU4), Pyrococcus furiosus
brenda
Selvaggi, A.; Tosi, C.; Barberini, U.; Franchi, E.; Rodriguez, F.; Pedroni, P.
In vitro hydrogen photoproduction using Pyrococcus furiosus sulfhydrogenase and TiO2
J. Photochem. Photobiol. A
125
107-112
1999
Pyrococcus furiosus (E7FI44 AND Q8U2E5 AND Q8U2E4 AND E7FHU4)
-
brenda