Information on EC 1.12.98.4 - sulfhydrogenase

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The expected taxonomic range for this enzyme is: Archaea, Bacteria

EC NUMBER
COMMENTARY hide
1.12.98.4
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RECOMMENDED NAME
GeneOntology No.
sulfhydrogenase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
H2 + (sulfide)n = hydrogen sulfide + (sulfide)n-1
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Sulfur metabolism
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sulfur reduction I
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sulfur reduction II (via polysulfide)
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hydrogen production
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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].
CAS REGISTRY NUMBER
COMMENTARY hide
101637-43-8
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain NASF-1
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
strain 9974
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Manually annotated by BRENDA team
strain 9974
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Manually annotated by BRENDA team
strain 2873
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Manually annotated by BRENDA team
strain 2873
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Manually annotated by BRENDA team
strain 5071
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Manually annotated by BRENDA team
strain 5071
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Manually annotated by BRENDA team
strain Gö20
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Manually annotated by BRENDA team
strain Gö20
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Manually annotated by BRENDA team
thermophilic iron-oxidizing bacterium strain TI-1
production of H2S, when grown in a medium containing ferrous ions, elemental sulfur and L-glutamic acid
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
disulfide + electron donor
H2S
show the reaction diagram
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cystine and cystamine, minimal activities, PDH
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?
H2 + benzyl viologen
H2S + reduced benzyl viologen
show the reaction diagram
E7FHC4 and E7FHN9 and E7FHW8 and E7FHF8
highest activity
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-
?
H2 + methyl viologen
H2S + reduced methyl viologen
show the reaction diagram
H2 + NADP+
H2S + NADPH + H+
show the reaction diagram
-
-
-
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r
H2 + polysulfide(n)
H2S + polysulfide(n-1)
show the reaction diagram
H2S + NADH + H+
H2 + NAD+
show the reaction diagram
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NADH is a very inefficient electron carrier for sulfhydrogenase
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r
H2S + NADPH + H+
H2 + NADP+
show the reaction diagram
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-
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r
NADPH + H+ + polysulfide(n)
NADP+ + polysulfide(n-1)
show the reaction diagram
E7FHC4 and E7FHN9 and E7FHW8 and E7FHF8
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-
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r
organic trisulfides + electron donor
H2S + oxidized electron donor
show the reaction diagram
polysulfide + electron donor
H2S + oxidized electron donor
show the reaction diagram
polysulfide + H2
H2S
show the reaction diagram
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-
-
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?
S + H2
H2S
show the reaction diagram
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-
-
-
?
sulfur
H2S
show the reaction diagram
sulfur + electron donor
H2S + oxidized electron donor
show the reaction diagram
sulfur + H2
H2S
show the reaction diagram
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in solubilized membrane fraction no activity is detected without the addition of electron carriers: 2,3-dimethylnaphthoquinone, plastoquinone or horse heart cytochrome c
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-
?
tetrasulfide + electron donor
H2S + oxidized electron donor
show the reaction diagram
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comparable to colloidal sulfur
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?
tetrathionate + H2
? + H+
show the reaction diagram
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-
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?
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
sulfur
H2S
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
FAD
E7FHC4 and E7FHN9 and E7FHW8 and E7FHF8
contains 0.83 FAD per mol enzyme
molybdopterin
NADH
E7FHC4 and E7FHN9 and E7FHW8 and E7FHF8
NADPH and NADH are equally efficient as electron donors for H2 production
NADPH
[2Fe-2S]-center
E7FHC4 and E7FHN9 and E7FHW8 and E7FHF8
contains 1 [2Fe-2S] center
[4Fe-4S]-center
E7FHC4 and E7FHN9 and E7FHW8 and E7FHF8
contains 2 [4Fe-4S]-centers
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Cu
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1.2 mol per mol protein
Fe2+
E7FHC4 and E7FHN9 and E7FHW8 and E7FHF8
contains 21 atoms iron per mol enzyme
Iron
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sequence is predicted to carry four [4Fe-4S] clusters
Molybdenum
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bound to the cis-dithiolene group of only one molybdopterin guanine dinucleotide molecule
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,10-phenanthroline
thermophilic iron-oxidizing bacterium strain TI-1
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2-(n-heptyl)-4-hydroxyquinoline N-oxide
GSSG
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90% loss of activity
iodoacetic acid
thermophilic iron-oxidizing bacterium strain TI-1
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N-ethylmaleimide
thermophilic iron-oxidizing bacterium strain TI-1
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p-chloromercuribenzene sulfonic acid
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potassium tetrathionate
thermophilic iron-oxidizing bacterium strain TI-1
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Quinacrine
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strong
sodium dithionate
thermophilic iron-oxidizing bacterium strain TI-1
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sodium sulfite
thermophilic iron-oxidizing bacterium strain TI-1
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sodium thiosulfate
thermophilic iron-oxidizing bacterium strain TI-1
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additional information
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no inhibition by rotenone, dicoumarol, antimycin A, NaN3, sodium dithiocarbamate
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8-hydroxyquinoline
thermophilic iron-oxidizing bacterium strain TI-1
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anthraquinone-2-sulfonate
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activation, in vitro electron donor
cysteamine
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increase of activity
cysteine
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increase of activity
ethylenediaminetetraacetic acid
thermophilic iron-oxidizing bacterium strain TI-1
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NADPH
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presence of NADPH increases the sulfur reduction activity, but NADPH alone cannot be used as electron donor
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5
methyl viologen
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at pH 8.0, 80°C
3
NADH
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at pH 8.0, 80°C
0.04
NADP+
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at pH 8.0, 80°C
0.2
NADPH
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at pH 8.0, 80°C
0.15
Polysulfide
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PDH
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
Wolinella succinogenes
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liposomal preparation of enzyme : 2000 min-1; liposomal preparation of membrane fraction: 2600 min-1, sulfide oxidation, liposomal preparation of enzyme: 1300 min-1, sulfide oxidation
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.026
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crude extract
0.04
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crude extract
0.043
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crude extract
0.07
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crude extract
2.73
thermophilic iron-oxidizing bacterium strain TI-1
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7.56
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at 100°C
186
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sulfide oxidation
350
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preparation 2
700
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preparation 1
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8.1
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sulfide oxidation
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8
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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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60 - 70
thermophilic iron-oxidizing bacterium strain TI-1
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90
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optimum temperature is at least 90°C
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
thermophilic iron-oxidizing bacterium strain TI-1
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Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24000
E7FHC4 and E7FHN9 and E7FHW8 and E7FHF8
1 * 52000 + 1 * 39000 + 1 * 30000 + 1 * 24000, SDS-PAGE
30000
E7FHC4 and E7FHN9 and E7FHW8 and E7FHF8
1 * 52000 + 1 * 39000 + 1 * 30000 + 1 * 24000, SDS-PAGE
39000
E7FHC4 and E7FHN9 and E7FHW8 and E7FHF8
1 * 52000 + 1 * 39000 + 1 * 30000 + 1 * 24000, SDS-PAGE
48000
thermophilic iron-oxidizing bacterium strain TI-1
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2 * 48000, SDS-PAGE
85000
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2 * 85000, SDS-PAGE
85033
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1 * 85033, calculated and crystallization data
86000
thermophilic iron-oxidizing bacterium strain TI-1
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gel-filtration
135000
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gel-filtration
153300
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SDS-PAGE
200000
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calculated from sedimentation coefficient obtained by sucrose density gradient centrifugation and Stokes radius obtained from gel filtration
320000
E7FHC4 and E7FHN9 and E7FHW8 and E7FHF8
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 85000, SDS-PAGE
heterotetramer
homodimer
thermophilic iron-oxidizing bacterium strain TI-1
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2 * 48000, SDS-PAGE
monomer
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1 * 85033, calculated and crystallization data
tetramer
E7FI44 and Q8U2E5 and E7FHU4 and Q8U2E4
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
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sphericla protein consisting of four domains with a funnel-like cavity that leads to a freely accessible metal-ion redox center
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
8 - 10
thermophilic iron-oxidizing bacterium strain TI-1
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complete loss of activity below pH 5
437779
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
thermophilic iron-oxidizing bacterium strain TI-1
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100% activity for 30 min
70
thermophilic iron-oxidizing bacterium strain TI-1
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73% loss of activity for 30 min
80
thermophilic iron-oxidizing bacterium strain TI-1
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88% loss of activity for 30 min
90
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activity decreases with increasing temperatures above 90°C
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
anion exchange chromatography leads to severe loss of activity
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gel filtration leads to severe loss of activity
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glycerol does not stabilize during purification
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PMSF does not stabilize during purification
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sucrose density gradient centrifugation leads to severe loss of activity
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Triton X-100
additional information
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octyl-2-D-glucopyranoside, 78% of activity
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
enzyme labile under aerobic conditions, but stable under anaerobic conditions and in the presence of Na-hydrosulfite
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437782
PDH activity is oxygen labile in crude extracts
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437777
the sulfur-reducing activity is irreversibly damaged by oxygen, anaerobic conditions: no loss of activity after one week, aerobic conditions: 80% loss of activity in 24 h
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437778, 437780
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
room temperature, exposed to air, 24 h, 80% loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
aerobic and anaerobic conditions
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DEAE column chromatography, hydroxyapatite column chromatography, phenyl Sepharose column chromatography, and Superdex 200 gel filtration
E7FHC4 and E7FHN9 and E7FHW8 and E7FHF8
enzyme complex
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hydroxyapatite chromatography; purified with 2-octylglucoside, not perchlorate or urea
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isolation and incorporation into liposomes
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partial, solubilized with Triton X-100
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purification of enzyme by solubilísation with sodium deoxycholate, in presence of ACA and glycerol
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Q Sepharose column chromatography, hydroxyapatite column chromatography, and Mono Q column chromatography
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
the SR gene cluster encompasses five ORFs with a total length of 7389 bp. The sreA gene encodes the 110000 Da subunit of SR. sreB encodes an FeS protein, sreC encodes a hydrophobic protein with 10 predicted transmembrane helices. The sreD gene encodes a putative hydrophilic FeS protein with 26 cysteine residues and of unknown cluster composition. The sreE gene encodes a protein with similarity to reductase assembly proteins
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression is repressed by SurR an archaeal transcriptional regulator and a key regulator involved in primary sulfur response
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