Any feedback?
Information on EC 1.12.98.4 - sulfhydrogenase
for references in articles please use BRENDA:EC1.12.98.4Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
1.12.98.4 sulfhydrogenaseIUBMB Comments
An iron-sulfur protein. The enzyme from the hyperthermophilic archaeon Pyrococcus furiosus is part of two heterotetrameric complexes where the beta and gamma subunits function as sulfur reductase and the alpha and delta subunits function as hydrogenases (EC 1.12.1.3, hydrogen dehydrogenase [NADP+] and EC 1.12.1.4, hydrogen dehydrogenase [NAD(P)+], respectively). Sulfur can also be used as substrate, but since it is insoluble in aqueous solution and polysulfide is generated abiotically by the reaction of hydrogen sulfide and sulfur, polysulfide is believed to be the true substrate .
Specify your search results
Word Map
- 1.12.98.4
- h2s
- hydrogenases
- succinogenes
-
wolinella
- pasteurianum
-
sulfur-reducing
- tetrathionate
-
chemolithotrophic
-
sulfur-dependent
-
molybdoenzyme
- energy production
The enzyme appears in viruses and cellular organisms
Synonyms
hydrogenase ii, sulfur reductase, polysulfide reductase, sulfhydrogenase, polysulfide dehydrogenase, sulhydrogenase, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 1.97.1.3
-
-
formerly
-
H2:sulfuroxidoreductase complex
-
-
-
-
reductase, sulfur
-
-
-
-
sulfhydrogenase
sulfhydrogenase
-
bifunctional enzyme using both elementar sulfur and polysulfide as substrates for H2S production
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYSTEMATIC NAME
IUBMB Comments
H2:polysulfide oxidoreductase
An iron-sulfur protein. The enzyme from the hyperthermophilic archaeon Pyrococcus furiosus is part of two heterotetrameric complexes where the beta and gamma subunits function as sulfur reductase and the alpha and delta subunits function as hydrogenases (EC 1.12.1.3, hydrogen dehydrogenase [NADP+] and EC 1.12.1.4, hydrogen dehydrogenase [NAD(P)+], respectively). Sulfur can also be used as substrate, but since it is insoluble in aqueous solution and polysulfide is generated abiotically by the reaction of hydrogen sulfide and sulfur, polysulfide is believed to be the true substrate [2].
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
101637-43-8
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
disulfide + electron donor
H2S
-
cystine and cystamine, minimal activities, PDH
-
?
H2 + benzyl viologen
H2S + reduced benzyl viologen
highest activity
-
-
?
H2S + NADH + H+
H2 + NAD+
-
NADH is a very inefficient electron carrier for sulfhydrogenase
-
-
r
NADPH + H+ + polysulfide(n)
NADP+ + polysulfide(n-1)
-
-
-
r
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
-
?
H2 + methyl viologen
H2S + reduced methyl viologen
-
-
-
?
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 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
-
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
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADH
NADPH and NADH are equally efficient as electron donors for H2 production
[Ni-Fe]-center
the alpha-subunit carries the NiFe dinuclear center
-
FAD
the gamma-subunit contains one FAD molecule
NADPH
NADPH and NADH are equally efficient as electron donors for H2 production
[2Fe-2S]-center
contains 1 [2Fe-2S] center
[2Fe-2S]-center
the gamma-subunit contains one 2Fe-2S cluster
[4Fe-4S]-center
contains 2 [4Fe-4S]-centers
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe
Fe2+
contains 21 atoms iron per mol enzyme
Iron
Mo
Molybdenum
-
bound to the cis-dithiolene group of only one molybdopterin guanine dinucleotide molecule
Ni
Ni2+
Nickel
the alpha-subunit carries the NiFe dinuclear center
Iron
the alpha-subunit carries the NiFe dinuclear center
Mo
-
enzym contains molybdenum 0.006 mmol/g protein bound to a pterin dinucleotide
Mo
-
molybdo-enzyme containing molybdopterin guanine dinucleotide, enzyme preparation 1: 0.0026 mmol/g protein, enzyme preparation 2: 0.006 mol/g protein
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
no inhibition by rotenone, dicoumarol, antimycin A, NaN3, sodium dithiocarbamate
-
2-(n-heptyl)-4-hydroxyquinoline N-oxide
-
strong in manometric assay
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NADPH
-
presence of NADPH increases the sulfur reduction activity, but NADPH alone cannot be used as electron donor
additional information
-
no quinione, but enzyme complex contains cytochrome c and has two additional cytochromes, probably of b-type
-
additional information
-
no quinione, but enzyme complex contains cytochrome c and has two additional cytochromes, probably of b-type
-
additional information
-
all organisms except Spirillum sp. require an external hydrogenase for assay
-
additional information
-
no lipophilic quinone, e.g. menaquinone (vitamin K2) involved, cytochrome b, c or covalently bound FAD are no cofactors
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
liposomal preparation of membrane fraction: 2600 min-1, sulfide oxidation, liposomal preparation of enzyme: 1300 min-1, sulfide oxidation
-
additional information
additional information
-
liposomal preparation of enzyme : 2000 min-1
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
spec. act. for the PDH are 12 to 48fold higher than for sulfhydrogenase
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8
-
no activity is observed below pH 6.0, the activity gradually increases up to pH 8.0, above pH 8.0 the rate of non-enzymic sulfur disproportionation reaction is higher than the enzymic rate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8
-
no activity is observed below pH 6.0, the activity gradually increases up to pH 8.0, above pH 8.0 the rate of non-enzymic sulfur disproportionation reaction is higher than the enzymic rate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
thermophilic iron-oxidizing bacterium strain TI-1
production of H2S, when grown in a medium containing ferrous ions, elemental sulfur and L-glutamic acid
-
-
brenda
E7FI44: alpha-subunit, Q8U2E5: beta-subunit, Q8U2E4: gamma-subunit, E7FHU4: delta-subunit
SwissProt
brenda
E7FI44: subunit alpha, Q8U2E5: subunit beta, E7FHU4: subunit delta, Q8U2E4: subunit gamma. 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
SwissProt
brenda
subunits alpha, beta, gamma and delta
UniProt
brenda
formerly called Spirillum sp. strain 5175, enzyme formed during growth with sulfur, DSM 6946
-
-
brenda
enzyme formed during growth at the expense of sulfur reduction by formate
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE