Detection of a High-Barrier Conformational Change in the Active Site of Cytochrome P45Ocam upon Binding of Putidaredoxin.

The article informs that Cytochrome CYP101 catalyzes the 5-exo-hydroxylation of camphor 1, the first step of catabolism of 1 by the soil bacterium Pseudomonas putida. Two electrons are required for turnover, and the second reduction, of the Fe(II) CYP101 ternary complex, is the rate-limiting step under physiological conditions. The ferredoxin putidaredoxin (Pdx) is the biological effector and reductant of CYP101. Structural perturbations have been observed spectroscopically in the CYP101 active site upon binding of Pdx, and it has been proposed that these perturbations are involved in the effector and/or electron-transfer activity of Pdx.