An Intermediate Conformational State of Cytochrome P450cam-CN in Complex with Putidaredoxin.

ABSTRACT: Cytochrome P450cam is an archetypal example of the vast family of heme monooxygenases and serves as a model for an enzyme that is highly specific for both its substrate and reductase. During catalysis, it undergoes significant conformational changes of the F and G helices upon binding its substrate and redox partner, putidaredoxin (Pdx). Recent studies have shown that Pdx binding to the closed camphor-bound form of ferric P450cam results in its conversion to a fully open state. However, during catalytic turnover, it remains unclear whether this same conformational change also occurs or whether it is coupled to the formation of the critical compound I intermediate. Here, we have examined P450cam bound simultaneously by camphor, CN^-, and Pdx as a mimic of the catalytically compete

SUBMITTER: Chuo SW 

PROVIDER: S-EPMC7185884 | biostudies-literature | 2019 May

REPOSITORIES: biostudies-literature