On the Structure of Putidaredoxin and Cytochrome P-450cam and their Mode of Interaction

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Abstract
The 5-exo-methylene hydroxylase of D(+)-camphor of Pseudomonas putida requires three components, a flavoprotein called putidare-doxin reductase, an iron-sulfur protein, putidaredoxin, and a variant b-type cytochrome, P-450cam, all of which show good solubility in aqueous buffers and havebeen obtained in homogeneous form (Tsai et al., 1971). Cytochrome P-450cam, the substrate and oxygen reactive component, is reduced by putidaredoxin which also acts as an effector forming very tight complexes with the hemeprotein in the presence of substrate (Tyson et al., 1972). Since these complexes can be readily formed in vitro, and since the reductase is not very specific and can be effectively replaced by other flavo-proteins, the putidaredoxin-cytochrome P-450cam-substrate complexes are of great interest to the study of tne mechanism of electron transfer in this multienzyme system.

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