Literature summary for 1.15.1.2 extracted from

Mathe, C.; Weill, C.O.; Mattioli, T.A.; Berthomieu, C.; Houee-Levin, C.; Tremey, E.; Niviere, V.
Assessing the role of the active-site cysteine ligand in the superoxide reductase from Desulfoarculus baarsii (2007), J. Biol. Chem., 282, 22207-22216.

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Cloned(Commentary)

Cloned (Comment)	Organism
gene sor, complementation of the Escherichia coli QC2375 mutant strain	Desulfarculus baarsii

Protein Variants

Protein Variants	Comment	Organism
E114A	the mutant shows significantly modified pulse radiolysis kinetics for the protonation process of the first reaction intermediate compared to the wild-type enzyme, mutation results in both a strengthening of the S-Fe bond and an increase in the extent of freeze-trapping of a Fe-peroxo species after treatment with H2O2 by a specific strengthening of the Fe-O bond, spectroscopic mutant analysis, overview	Desulfarculus baarsii

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	kinetics, resonance Raman spectroscopy	Desulfarculus baarsii

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Fe2+	the active site consists of an unusual non-heme Fe2+ center in a [His4 Cys1] square pyramidal pentacoordination	Desulfarculus baarsii

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
reduced rubredoxin + superoxide + H+	Desulfarculus baarsii	the enzyme catalyzes the one-electron reduction of O2 to H2O2, providing an antioxidant defense in some bacteria	rubredoxin + H2O2	-	?

Organism

Organism	UniProt	Comment	Textmining
Desulfarculus baarsii	Q46495	gene sor	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
reduced rubredoxin + superoxide + 2 H+	the active site consists of an unusual non-heme Fe2+ center in a [His4 Cys1] square pyramidal pentacoordination, the reaction procedes via a Fe3+-peroxo intermediate	Desulfarculus baarsii	rubredoxin + H2O2	-	?
reduced rubredoxin + superoxide + H+	the enzyme catalyzes the one-electron reduction of O2 to H2O2, providing an antioxidant defense in some bacteria	Desulfarculus baarsii	rubredoxin + H2O2	-	?

Cofactor

Cofactor	Comment	Organism	Structure
reduced rubredoxin	-	Desulfarculus baarsii

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Release 2023.1 (January 2023)