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Article

Specific effects of potassium ion binding on wild-type and L358P cytochrome P450cam.

Biochemistry - 5 Dec 2006

OuYang Bo, Pochapsky Susan Sondej, Pagani Gina M, Pochapsky Thomas C

Abstract excerpt

The camphor monoxygenase cytochrome P450cam (CYP101) requires potassium ion (K+) to drive formation of the characteristic high-spin state of the heme Fe+3 upon substrate binding. Amide 1H, 15N correlations in perdeuterated [U-15N] CYP101 were monitored as a function of K+ concentration by 2D-TROSY-HSQC in both camphor-bound oxidized (CYP-S) and camphor- and CO-bound reduced CYP101 (CYP-S-CO). In both forms,...

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Identifiers

PMID: 17128977
DOI: 10.1021/bi0617355
PMCID: PMC1764623

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Source receipt: pubmed, retrieved 7 Sept 2026.

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