Literature summary for 7.1.1.7 extracted from

Siletsky, S.A.; Dyuba, A.V.; Elkina, D.A.; Monakhova, M.V.; Borisov, V.B.
Spectral-kinetic analysis of recombination reaction of heme centers of bd-type quinol oxidase from Escherichia coli with carbon monoxide (2017), Biochemistry, 82, 1354-1366 .

Search for more literature for 7.1.1.7

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0ABJ9 and P0ABK2 and P56100	P0ABJ9 i.e. subunit cydA, P0ABK2 i.e. subunit cydB, P56100 i.e. subunit cydX	-

General Information

General Information	Comment	Organism
physiological function	the unresolved photodissociation of CO is followed by a four-phased recombination with characteristic times of about 20 micros, 250 micros, 1.1 ms, and 24 ms. The 20x02micros phase most likely reflects bimolecular recombination of CO with heme d. The 250x02micros phase is heterogeneous and includes recombination of CO with about 7% of heme b595 and transition of heme d from a pentacoordinate to a transient hexacoordinate state in this enzyme population. The 24x02ms transition probably reflects a return of heme d to the pentacoordinate state in the same protein fraction. The 1.1x02ms phase reflects a recombination of CO with about 15% of heme b558	Escherichia coli

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)