Structure of the open conformation of a functional chimeric NADPH cytochrome P450 reductase.
Two catalytic domains, bearing FMN and FAD cofactors, joined by a connecting domain, compose the core of the NADPH cytochrome P450 reductase (CPR). The FMN domain of CPR mediates electron shuttling from the FAD domain to cytochromes P450. Together, both enzymes form the main mixed-function oxidase s...
| Main Authors: | , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
2009
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