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Article

Investigation of the low frequency dynamics of heme proteins: native and mutant cytochrome P450(cam) and redox partner complexes.

The journal of physical chemistry. B - 12 May 2011

Karunakaran Venugopal, Denisov Ilia, Sligar Stephen G, Champion Paul M

Abstract excerpt

Vibrational coherence spectroscopy (VCS) is used to investigate the low-frequency dynamics of camphor-free and camphor-bound cytochrome P450(cam) (CYP 101) and its L358P mutant. The low-frequency heme vibrations are found to be perturbed upon binding to the electron transfer partner putidaredoxin (Pdx). A strong correlation between the "detuned" vibrational coherence spectrum, which monitors frequencies between...

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Identifiers

PMID: 21391540
DOI: 10.1021/jp112298y
PMCID: PMC3088772

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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Investigation of the low frequency dynamics of heme proteins: native and mutant cytochrome P450(cam) and redox partner complexes.PMID 21391540Read ↗

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

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Effector Roles of Putidaredoxin on Cytochrome P450cam Conformational States.Semantic proximity Read ↗

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