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Article

Reversible pressure deformation of a thermophilic cytochrome P450 enzyme (CYP119) and its active-site mutants.

Journal of the American Chemical Society - 18 Apr 2001

Tschirret-Guth R A, Koo L S, Hoa G H, Ortiz De Montellano P R

Abstract excerpt

The pressure stability of the thermophilic CYP119 from Sulfolobus solfataricus and its active-site Thr213 and Thr214 mutants was investigated. At 20 degrees C and pH 6.5, the protein undergoes a reversible P450-to-P420 inactivation with a midpoint at 380 MPa and a reaction volume change of -28 mL/mol. The volume of activation of the process was -9.5 mL/mol. The inactivation transition was retarded, and the...

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Identifiers

PMID: 11472111
DOI: 10.1021/ja003947+

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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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