A necessary step in understanding biological function in multiple metalloprotein redox systems is the description of protein-protein binding and electron transfer between two distant metal centers. In this communication, we present experimental and theoretical analyses of the residues that are involved in the binding and the electron transfer pathways of the cytochrome P450cam (CYP101) and putidaredoxin (Pdx) protein complex. The combined result from theory and experiments allows us to present a detailed molecular model for the interaction of putidaredoxin and CYP101. Residues at the protein-protein interface are tagged as being important for binding and/or electron transfer while predicting a possible electron transfer pathway.
Citation: Journal of the American Chemical Society
Pub Type: Journals
biocatalysis, cytochrome P450, electron transfer