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Article

Structural and spectroscopic analysis of the F393H mutant of flavocytochrome P450 BM3.

Biochemistry - 13 Nov 2001

Ost T W, Munro A W, Mowat C G, Taylor P R, Pesseguiero A, Fulco A J, Cho A K, Cheesman M A, Walkinshaw M D, Chapman S K

Abstract excerpt

In the preceding paper in this issue [Ost, T. W. B., Miles, C. S., Munro, A. W., Murdoch, J., Reid, G. A., and Chapman, S. K. (2001) Biochemistry 40, 13421-13429], we have established that the primary role of the phylogenetically conserved phenylalanine in flavocytochrome P450 BM3 (F393) is to control the thermodynamic properties of the heme iron, so as to optimize electron-transfer both to the iron (from the...

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PMID: 11695889
DOI: 10.1021/bi010717e

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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Structural and spectroscopic analysis of the F393H mutant of flavocytochrome P450 BM3.PMID 11695889Read ↗

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