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Article

Hydrogen-bonding interactions in the active sites of cytochrome P450cam and its site-directed mutants.

Journal of the American Chemical Society - 17 Jan 2001

Deng T, Macdonald I D, Simianu M C, Sykora M, Kincaid J R, Sligar S G

Abstract excerpt

Resonance Raman spectroscopy is applied to the cyanide adducts of cytochrome P450cam and its T252A and D251N site-directed mutants, both in their substrate-free and camphor-bound forms, to probe active-site heme structure and, in particular, interactions of the FeCN fragment with potential active-site H-bond donors. In contrast to the ferrous CO and ferric NO adducts, which form only essentially linear (slightly...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 11456513
DOI: 10.1021/ja001517d

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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