BRENDA - Enzyme Database show
show all sequences of 1.8.99.5

The crystal structure of Desulfovibrio vulgaris dissimilatory sulfite reductase bound to DsrC provides novel insights into the mechanism of sulfate respiration

Oliveira, T.F.; Vonrhein, C.; Matias, P.M.; Venceslau, S.S.; Pereira, I.A.; Archer, M.; J. Biol. Chem. 283, 34141-34149 (2008)

Data extracted from this reference:

Cloned(Commentary)
Commentary
Organism
structure with the alpha and beta subunits bound to the DsrC protein. The alpha2beta2gamma2 assembly contains two siroheme-[4Fe4S] cofactors bound by DsrB, two sirohydrochlorins and two [4Fe-4S]-centers bound by DsrA, and another four [4Fe-4S]-centers in the ferredoxin domains. A sulfite molecule, coordinating the siroheme, is found at the active site. The DsrC protein is bound in a cleft between DsrA and DsrB with its conserved C-terminal cysteine reaching the distal side of the siroheme. The process of sulfite reduction may involve DsrAB, DsrC, and the DsrMKJOP membrane complex (a membrane complex with putative disulfide/thiol reductase activity), in which two of the six electrons for reduction of sulfite derive from the membrane quinone pool
Desulfovibrio vulgaris
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Desulfovibrio vulgaris
P45574 and P45575
P45574 i.e. subunit alpha, P45575 i.e. subunit beta
-
Desulfovibrio vulgaris Hildenborough
P45574 and P45575
P45574 i.e. subunit alpha, P45575 i.e. subunit beta
-
Cofactor
Cofactor
Commentary
Organism
Structure
siroheme
protein complex contains two siroheme-[4Fe4S] cofactors bound by subunit DsrB, two sirohydrochlorins and two [4Fe-4S]-centers bound by subunit DsrA, and another four [4Fe-4S]-centers in the ferredoxin domains
Desulfovibrio vulgaris
[4Fe-4S]-center
protein complex contains two siroheme-[4Fe4S] cofactors bound by subunit DsrB, two sirohydrochlorins and two [4Fe-4S]-centers bound by subunit DsrA, and another four [4Fe-4S]-centers in the ferredoxin domains
Desulfovibrio vulgaris
Cloned(Commentary) (protein specific)
Commentary
Organism
structure with the alpha and beta subunits bound to the DsrC protein. The alpha2beta2gamma2 assembly contains two siroheme-[4Fe4S] cofactors bound by DsrB, two sirohydrochlorins and two [4Fe-4S]-centers bound by DsrA, and another four [4Fe-4S]-centers in the ferredoxin domains. A sulfite molecule, coordinating the siroheme, is found at the active site. The DsrC protein is bound in a cleft between DsrA and DsrB with its conserved C-terminal cysteine reaching the distal side of the siroheme. The process of sulfite reduction may involve DsrAB, DsrC, and the DsrMKJOP membrane complex (a membrane complex with putative disulfide/thiol reductase activity), in which two of the six electrons for reduction of sulfite derive from the membrane quinone pool
Desulfovibrio vulgaris
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
siroheme
protein complex contains two siroheme-[4Fe4S] cofactors bound by subunit DsrB, two sirohydrochlorins and two [4Fe-4S]-centers bound by subunit DsrA, and another four [4Fe-4S]-centers in the ferredoxin domains
Desulfovibrio vulgaris
[4Fe-4S]-center
protein complex contains two siroheme-[4Fe4S] cofactors bound by subunit DsrB, two sirohydrochlorins and two [4Fe-4S]-centers bound by subunit DsrA, and another four [4Fe-4S]-centers in the ferredoxin domains
Desulfovibrio vulgaris
Other publictions for EC 1.8.99.5
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
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742577
Leavitt
Sulfur isotope effects of dis ...
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6
1392
2015
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The octahaem MccA is a haem c ...
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520
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2015
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743053
Lee
-
Construction of aligned datab ...
Chlorobium phaeobacteroides, Chlorobium phaeobacteroides BS1, Chlorobium phaeobacteroides DSM 266, Desulfitobacterium dichloroeliminans, Desulfitobacterium dichloroeliminans LMG P-21439, Desulfosporosinus orientis, Desulfosporosinus orientis DSM 765, Desulfovibrio vulgaris, Desulfovibrio vulgaris DP4, Desulfovibrio vulgaris Hildenborough, Thermaerobacter marianensis, Thermaerobacter marianensis AB011495
J. Korean Soc. Appl. Biol. Chem.
57
419-427
2014
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12
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741792
Mori
Dominance of green sulfur bac ...
Candidatus Ruthia magnifica, Candidatus Thiobios zoothamnicoli, Chlorobium limicola, Chlorobium phaeovibrioides, Halochromatium salexigens, Magnetospirillum gryphiswaldense, Pelodictyon luteolum
Arch. Microbiol.
195
303-312
2013
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741814
Venceslau
Redox states of Desulfovibrio ...
Desulfovibrio vulgaris
Biochem. Biophys. Res. Commun.
441
732-736
2013
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725901
Holkenbrink
Sulfur globule oxidation in gr ...
Chlorobaculum tepidum, Chlorobaculum tepidum DSM 12025
Microbiology
157
1229-1239
2011
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1
1
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710741
Ogata
Purification, crystallization ...
Desulfovibrio vulgaris, Desulfovibrio vulgaris Miyazaki F
Acta Crystallogr. Sect. F
66
1470-1472
2010
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11
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710943
Moreau
Diversity of dissimilatory sul ...
Soil bacterium
Appl. Environ. Microbiol.
76
4819-4828
2010
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1
1
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688412
Schiffer
Structure of the dissimilatory ...
Archaeoglobus fulgidus
J. Mol. Biol.
379
1063-1074
2008
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688700
Oliveira
Purification, crystallization ...
Desulfovibrio vulgaris, Desulfovibrio vulgaris Hildenborough
J. Struct. Biol.
164
236-239
2008
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698846
Oliveira
The crystal structure of Desul ...
Desulfovibrio vulgaris, Desulfovibrio vulgaris Hildenborough
J. Biol. Chem.
283
34141-34149
2008
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673621
Mander
X-ray structure of the gamma-s ...
Archaeoglobus fulgidus
FEBS Lett.
579
4600-4604
2005
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733771
Cort
Solution structure of Pyrobacu ...
Pyrobaculum aerophilum, Pyrobaculum aerophilum DSM 7523
Eur. J. Biochem.
268
5842-5850
2001
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722213
Larsen
Dissimilatory sulfite reductas ...
Archaeoglobus profundus, Archaeoglobus profundus DSM 5631, Desulfofundulus thermocisternus
Extremophiles
3
63-70
1999
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734636
Pott
-
Sirohaem sulfite reductase and ...
Allochromatium vinosum, Allochromatium vinosum DSM 180
Microbiology
144
1881-1894
1998
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734637
Molitor
A dissimilatory sirohaem-sulfi ...
Pyrobaculum islandicum
Microbiology
144
529-541
1998
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733765
Marritt
Dissimilatory sulfite reductas ...
Desulfovibrio vulgaris
Eur. J. Biochem.
238
724-727
1996
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394066
Steuber
Molecular properties of the di ...
Desulfovibrio desulfuricans, Desulfovibrio desulfuricans Essex
Eur. J. Biochem.
233
873-879
1995
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394063
Lui
Conformational gating of the d ...
Desulfovibrio vulgaris, Desulfovibrio vulgaris Hildenborough
Biochemistry
33
11209-11216
1994
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394068
Wolfe
Desulfoviridin, a multimeric-d ...
Desulfovibrio vulgaris, Desulfovibrio vulgaris Hildenborough
Eur. J. Biochem.
223
79-89
1994
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3
394040
Seki
Characterization of a dissimil ...
Desulfovibrio africanus, Desulfovibrio africanus Benghazi
J. Biochem.
98
1535-1543
1985
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394898
Harrison
Purification and characterizat ...
Clostridium pasteurianum
Arch. Microbiol.
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72-78
1984
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394043
Hatchikian
Characterization of a new type ...
Thermodesulfobacterium commune
J. Bacteriol.
153
1211-1220
1983
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