Ligand and Redox Partner Binding Generates a New Conformational State in Cytochrome P450cam (CYP101A1).

ABSTRACT: It has become increasingly clear that cytochromes P450 can cycle back and forth between two extreme conformational states termed the closed and open states. In the well-studied cytochrome P450cam, the binding of its redox partner, putidaredoxin (Pdx), shifts P450cam toward the open state. Shifting to the open state is thought to be important in the formation of a proton relay network essential for O-O bond cleavage and formation of the active Fe(IV)═O intermediate. Another important intermediate is the oxy-P450cam complex when bound to Pdx. Trapping this intermediate in crystallo is challenging owing to its instability, but the CN^- complex is both stable and an excellent mimic of the O₂ complex. Here we present the P450cam-Pdx structure complexed with CN^-.

SUBMITTER: Follmer AH 

PROVIDER: S-EPMC8917899 | biostudies-literature | 2019 Feb

REPOSITORIES: biostudies-literature