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Article

Mutagenesis of a single hydrogen bond in cytochrome P-450 alters cation binding and heme solvation.

The Journal of biological chemistry - 5 Apr 1990

Di Primo C, Hui Bon Hoa G, Douzou P, Sligar S

Abstract excerpt

Cytochrome P-450cam, a monoxygenase responsible for the regiospecific hydroxylation of camphor, binds its substrate through complimentary van der Waals contacts and the formation of a single hydrogen bond between tyrosine 96 and the ketone group of camphor. Substrate association is positively regulated through the binding of a monovalent cation and the oxidation-reduction potential modulated by the spin state of...

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PMID: 2318818

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

Source receipt: pubmed, retrieved 7 Sept 2026.

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Mutagenesis of a single hydrogen bond in cytochrome P-450 alters cation binding and heme solvation.PMID 2318818Read ↗

Conformational Heterogeneity and the Affinity of Substrate Molecular Recognition by Cytochrome P450cam.Semantic proximity Read ↗

Exceptionally stable salt bridges in cytochrome P450cam have functional roles.Semantic proximity Read ↗

Tyrosine-96 as a natural spectroscopic probe of the cytochrome P-450cam active site.Semantic proximity Read ↗

Redox control of the P450cam catalytic cycle: effects of Y96F active site mutation and binding of a non-natural substrate.Semantic proximity Read ↗

Hydroxylation Regiochemistry Is Robust to Active Site Mutations in Cytochrome P450cam (CYP101A1).Semantic proximity Read ↗

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

Synergistic effects of mutations in cytochrome P450cam designed to mimic CYP101D1.Semantic proximity Read ↗

Efficient catalytic turnover of cytochrome P450(cam) is supported by a T252N mutation.Semantic proximity Read ↗

Quantum mechanical/molecular mechanical calculated reactivity networks reveal how cytochrome P450cam and Its T252A mutant select their oxidation pathways.Semantic proximity Read ↗

Structural alterations of the heme environment of cytochrome P450cam and the Y96F mutant as deduced by resonance Raman spectroscopy.Semantic proximity Read ↗

Specific effects of potassium ion binding on wild-type and L358P cytochrome P450cam.Semantic proximity Read ↗

Detection of substrate-dependent conformational changes in the P450 fold by nuclear magnetic resonance.Semantic proximity Read ↗

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