Literature summary for 1.13.11.49 extracted from

Suendermann, A.; Reif, M.M.; Hofbauer, S.; Obinger, C.; Oostenbrink, C.
Investigation of ion binding in chlorite dismutases by means of molecular dynamics simulations (2014), Biochemistry, 53, 4869-4879 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
molecular dynamics simulations for binding of cyanide, chlorite, and hypochlorite with the enzyme in the ferrous, ferric, and compound I state. During reaction, a large portion of hypochlorite escapes from the heme cavity and enters the bulk phase. Leakage of hypochlorite in the mutant R173A is higher than that in the wild-type protein	Nitrospira defluvii

Protein Variants

Protein Variants	Comment	Organism
R173A	leakage of hypochlorite during the reaction is higher than that in the wild-type protein	Nitrospira defluvii

Organism

Organism	UniProt	Comment	Textmining
Nitrospira defluvii	B3U4H7	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	chlorite binding to ferric Cld occurs spontaneously and residue Arg173 is important for recognition and to impair hypochlorite leakage from the reaction sphere	Nitrospira defluvii	?	-	?

Synonyms

Synonyms	Comment	Organism
CLD	-	Nitrospira defluvii

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Release 2023.1 (January 2023)