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P450cin from Citrobacter braakii is a three-component class I P450 system except that its flavin-containing components resemble class II P450s
redox partner binding stabilizes the open low-spin conformation of P450cam and greatly decreases the stability of the oxy complex
the two electrons necessary for the conversion of 1,8-cineole to 2beta-hydroxy-1,8-cineole are supplied by NADPH and transferred via a FAD-containing cindoxin reductase (CinB), and an FMN-containing cindoxin (CinC) to the heme iron in the active site of P450cin (CinA). The flow of electrons in this multicomponent P450cin system is from NADPH to Fpr via CinC to CinA
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