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J Biol Chem, Vol. 274, Issue 14, 9363-9369, April 2, 1999

Putidaredoxin-Cytochrome P450_cam Interaction
SPIN STATE OF THE HEME IRON MODULATES PUTIDAREDOXIN STRUCTURE

From the Department of Biochemistry, School of Medicine, Keio University, Shinano-machi, Shinjuku-ku, Tokyo 160-8582, Japan

Futoshi Masuya, Takashi Obata, and Hiroshi Hori

From the Division of Biophysical Engineering, Graduate School of Engineering Science, Osaka University, Toyonaka, Osaka 560-8531, Japan

During the monooxygenase reaction catalyzed by cytochrome P450_cam (P450_cam), a ternary complex of P450_cam, reduced putidaredoxin, and d-camphor is formed as an obligatory reaction intermediate. When ligands such as CO, NO, and O₂ bind to the heme iron of P450_cam in the intermediate complex, the EPR spectrum of reduced putidaredoxin with a characteristic signal at 346 millitesla at 77 K changed into a spectrum having a new signal at 348 millitesla. The experiment with O₂ was carried out by employing a mutant P450_cam with Asp²⁵¹  Asn or Gly where the rate of electron transfer from putidaredoxin to oxyferrous P450_cam is considerably reduced. Such a ligand-induced EPR spectral change of putidaredoxin was also shown in situ in Pseudomonas putida. Mutations introduced into the neighborhood of the iron-sulfur cluster of putidaredoxin revealed that a Ser⁴⁴  Gly mutation mimicked the ligand-induced spectral change of putidaredoxin. Arg¹⁰⁹ and Arg¹¹², which are in the putative putidaredoxin binding site of P450_cam, were essential for the spectral changes of putidaredoxin in the complex. These results indicate that a change in the P450_cam active site that is the consequence of an altered spin state is transmitted to putidaredoxin within the ternary complex and produces a conformational change of the 2Fe-2S active center.

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