Literature summary for 1.7.2.2 extracted from

Trofimov, A.A.; Polyakov, K.M.; Lazarenko, V.A.; Popov, A.N.; Tikhonova, T.V.; Tikhonov, A.V.; Popov, V.O.
Structural study of the X-ray-induced enzymatic reaction of octahaem cytochrome C nitrite reductase (2015), Acta Crystallogr. Sect. D, 71, 1087-1094 .

Cloned(Commentary)

Cloned (Comment)	Organism
-	Thioalkalivibrio nitratireducens

Crystallization (Commentary)

Crystallization (Comment)	Organism
diffraction data sets with increasing absorbed doses. The structures reveal gradual changes associated with the reduction of the catalytic hemes by X-rays. The conversion of the nitrite ions bound in the active sites to NO species is observed, which is the beginning of the catalytic reaction. For the free form, an increase in the distance between the oxygen ligand bound to the catalytic heme and the iron ion of the heme takes place. In the sulfite complex no enzymatic reaction is detected	Thioalkalivibrio nitratireducens

Crystallization (Comment)

Organism

diffraction data sets with increasing absorbed doses. The structures reveal gradual changes associated with the reduction of the catalytic hemes by X-rays. The conversion of the nitrite ions bound in the active sites to NO species is observed, which is the beginning of the catalytic reaction. For the free form, an increase in the distance between the oxygen ligand bound to the catalytic heme and the iron ion of the heme takes place. In the sulfite complex no enzymatic reaction is detected

Thioalkalivibrio nitratireducens

Organism

Organism	UniProt	Comment	Textmining
Thioalkalivibrio nitratireducens	L0DSL2	-	-
Thioalkalivibrio nitratireducens DSM 14787	L0DSL2	-	-

Synonyms

Synonyms	Comment	Organism
cytochrome c-552	-	Thioalkalivibrio nitratireducens
NiR	-	Thioalkalivibrio nitratireducens

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Release 2023.1 (January 2023)