Kinetic and structural characterization of the interaction between the FMN binding domain of cytochrome P450 reductase and cytochrome c.

ABSTRACT: Cytochrome P450 reductase (CPR) is a diflavin enzyme that transfers electrons to many protein partners. Electron transfer from CPR to cyt c has been extensively used as a model reaction to assess the redox activity of CPR. CPR is composed of multiple domains, among which the FMN binding domain (FBD) is the direct electron donor to cyt c. Here, electron transfer and complex formation between FBD and cyt c are investigated. Electron transfer from FBD to cyt c occurs at distinct rates that are dependent on the redox states of FBD. When compared with full-length CPR, FBD reduces cyt c at a higher rate in both the semiquinone and hydroquinone states. The NMR titration experiments reveal the formation of dynamic complexes between FBD and cyt c on a fast exchange time scale. Chemical shift mappin

SUBMITTER: Huang R 

PROVIDER: S-EPMC4335224 | biostudies-literature | 2015 Feb

REPOSITORIES: biostudies-literature