BRENDA - Enzyme Database
show all sequences of 1.8.1.19

Novel structure and redox chemistry of the prosthetic groups of the iron-sulfur flavoprotein sulfide dehydrogenase from Pyrococcus furiosus; evidence for a [2Fe-2S] cluster with Asp(Cys)3 ligands

Hagen, W.R.; Silva, P.J.; Amorim, M.A.; Hagedoorn, P.L.; Wassink, H.; Haaker, H.; Robb, F.T.; J. Biol. Inorg. Chem. 5, 527-534 (2000)

Data extracted from this reference:

Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
30686
-
1 * 52598 (alpha-subunit, SudA) + 1 * 30686 (beta-subunit, SudB), calculated from sequence
Pyrococcus furiosus
52598
-
1 * 52598 (alpha-subunit, SudA) + 1 * 30686 (beta-subunit, SudB), calculated from sequence
Pyrococcus furiosus
Organism
Organism
UniProt
Commentary
Textmining
Pyrococcus furiosus
Q8U195 and Q8U194
Q8U195: subunit alpha, and Q8U194: subunit beta
-
Subunits
Subunits
Commentary
Organism
heterodimer
1 * 52598 (alpha-subunit, SudA) + 1 * 30686 (beta-subunit, SudB), calculated from sequence
Pyrococcus furiosus
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
both the alpha-subunit and the beta-subunit contains one FAD
Pyrococcus furiosus
Fe-S center
the alpha-subunit carries a [2Fe-2S]2+,+ prosthetic group. It exhibits EPR g-values, 2.035, 1.908, 1.786, and reduction potential, Em,8 = +80 mV, reminiscent of Rieske-type clusters. Comparative sequence analysis indicates that this cluster is coordinated by a novel motif of one Asp and three Cys ligands. The beta-subunit carries a [3Fe-4S]+,0 cluster, and a [4Fe-4S]2+,+ cluster. The 3Fe cluster has an unusually high reduction potential, Em,8 = +230 mV. The reduced 4Fe cluster exhibits a complex EPR signal, presumably resulting from magnetic interaction of its S = 1/2 spin with the S=2 spin of the reduced 3Fe cluster. The 4Fe cluster can be reduced with deazaflavin/EDTA/light but not with sodium dithionite, however, it is readily reduced with NADPH
Pyrococcus furiosus
NADPH
both the alpha-subunit and the beta-subunit carry one putative nucleotide binding site for NADPH
Pyrococcus furiosus
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
both the alpha-subunit and the beta-subunit contains one FAD
Pyrococcus furiosus
Fe-S center
the alpha-subunit carries a [2Fe-2S]2+,+ prosthetic group. It exhibits EPR g-values, 2.035, 1.908, 1.786, and reduction potential, Em,8 = +80 mV, reminiscent of Rieske-type clusters. Comparative sequence analysis indicates that this cluster is coordinated by a novel motif of one Asp and three Cys ligands. The beta-subunit carries a [3Fe-4S]+,0 cluster, and a [4Fe-4S]2+,+ cluster. The 3Fe cluster has an unusually high reduction potential, Em,8 = +230 mV. The reduced 4Fe cluster exhibits a complex EPR signal, presumably resulting from magnetic interaction of its S = 1/2 spin with the S=2 spin of the reduced 3Fe cluster. The 4Fe cluster can be reduced with deazaflavin/EDTA/light but not with sodium dithionite, however, it is readily reduced with NADPH
Pyrococcus furiosus
NADPH
both the alpha-subunit and the beta-subunit carry one putative nucleotide binding site for NADPH
Pyrococcus furiosus
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
30686
-
1 * 52598 (alpha-subunit, SudA) + 1 * 30686 (beta-subunit, SudB), calculated from sequence
Pyrococcus furiosus
52598
-
1 * 52598 (alpha-subunit, SudA) + 1 * 30686 (beta-subunit, SudB), calculated from sequence
Pyrococcus furiosus
Subunits (protein specific)
Subunits
Commentary
Organism
heterodimer
1 * 52598 (alpha-subunit, SudA) + 1 * 30686 (beta-subunit, SudB), calculated from sequence
Pyrococcus furiosus
Other publictions for EC 1.8.1.19
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
Synonyms
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)
722535
Bridger
Deletion strains reveal metabo ...
Pyrococcus furiosus
J. Bacteriol.
193
6498-6504
2011
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722825
Hagen
Novel structure and redox chem ...
Pyrococcus furiosus
J. Biol. Inorg. Chem.
5
527-534
2000
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2
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722483
Ma
Sulfide dehydrogenase from the ...
Pyrococcus furiosus
J. Bacteriol.
176
6509-6517
1994
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