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Article

Formation of transient oxygen complexes of cytochrome p450 BM3 and nitric oxide synthase under high pressure.

Biophysical journal - 1 Nov 2003

Marchal Stéphane, Girvan Hazel Mary, Gorren Antonius C F, Mayer Bernd, Munro Andrew William, Balny Claude, Lange Reinhard

Abstract excerpt

The kinetics of formation and transformation of oxygen complexes of two heme-thiolate proteins (the F393H mutant of cytochrome P450 BM3 and the oxygenase domain of endothelial nitric oxide synthase, eNOS) were studied under high pressure. For BM3, oxygen-binding characteristics (rate and activation volume) matched those measured for CO-binding. In contrast, pressure revealed a different CO- and oxygen-binding...

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Identifiers

PMID: 14581231
DOI: 10.1016/S0006-3495(03)74749-3
PMCID: PMC1303607

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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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