Literature summary for 1.15.1.2 extracted from

Niviere, V.; Asso, M.; Weill, C.O.; Lombard, M.; Guigliarelli, B.; Favaudon, V.; Houee-Levin, C.
Superoxide reductase from Desulfoarculus baarsii: identification of protonation steps in the enzymatic mechanism (2004), Biochemistry, 43, 808-818.

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Protein Variants

Protein Variants	Comment	Organism
E47A	E47 is not the base responsible for pH transitions, and not involved in formation of the first reaction intermediate	Desulfarculus baarsii
K48I	K48 is not the base responsible for pH transitions, and not involved in formation of the first reaction intermediate	Desulfarculus baarsii

Organism

Organism	UniProt	Comment	Textmining
Desulfarculus baarsii	-	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
superoxide + reduced rubredoxin + 2 H+ = H2O2 + oxidized rubredoxin	in absence of O2.-, reduction potential and absorption spectrum of the iron center II exhibit a pH transition. First reaction intermediate is an iron(III)-peroxo species, second intermediate is an iron(III)-hydroperoxo species	Desulfarculus baarsii	a

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Release 2023.1 (January 2023)