Oxygen surrogate

Yamazaki, H., Ueng, Y.F., Shimada, T. and Guengerich, F.P. (1995) Roles of divalent metal ions in oxidations catalyzed by recombinant cytochrome P450 3A4 and replacement of NADPH-cytochrome P450 reductase with other flavoproteins, ferredoxin, and oxygen surrogates. Biochemistry, 34, 8380—8389. 

Guengerich FP, Yun CH, Macdonald TL. Evidence for a 1-electron oxidation mechanism in N-dealkylation of N,N-dialkylanilines by cytochrome P450 2B1. Kinetic hydrogen isotope effects, linear free energy relationships, comparisons with horseradish peroxidase, and studies with oxygen surrogates. J Biol Chem 1996 271 27321-9. 

Modi et reported differences in product profiles of P450 2D6 reactions supported with artificial oxygene surrogates and NADPH-P450 reductase, and interpreted these as evidence for an allosteric influence of the reductase. Subsequent experiments in this laboratory did not support this conclusion and are in accord with some differences in the chemical mechanisms for the oxygen surrogates. ... 

Relatively little is known about the active site of P450 5A1 beyond the information about the reactions presented above. As indicated, the protein does not bind NADPH-P450 reductase. Presumably, the active site is rather specific, although iodosylbenzene could be utilized as an oxygen surrogate. 

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