Literature summary for 1.15.1.1 extracted from

Miller, A.F.; Sorkin, D.L.; Padmakumar, K.
Anion binding properties of reduced and oxidized iron-containing superoxide dismutase reveal no requirement for tyrosine 34 (2005), Biochemistry, 44, 5969-5981.

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Protein Variants

Protein Variants	Comment	Organism
Y34F	unlike wild-type, F- binding is retained at high pH-values. N3- inhibitis Y34F with a 20fold lower KI-value than for wild-type	Escherichia coli

Inhibitors

Inhibitors	Comment	Organism	Structure
HS-	substrate analogue, formation of a green complex upon binding	Escherichia coli
N3-	-	Escherichia coli

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	pH-dependence of KM-value reflects the inhibition of anion binding by ionized Y34	Escherichia coli

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Iron	spectroscopic analysis of reduced and oxidized state of iron. In oxidized state, formation of a six-coordinate complex occurs. Two substrate analogues F- can bind to the oxidized enzymes active site	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0AGD3	FeSOD	-

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Release 2023.1 (January 2023)