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Article

Covalent heme binding to CYP4B1 via Glu310 and a carbocation porphyrin intermediate.

Biochemistry - 22 Apr 2003

Zheng Yi-Min, Baer Brian R, Kneller M Byron, Henne Kirk R, Kunze Kent L, Rettie Allan E

Abstract excerpt

Recently we found that CYP4B1, and several other members of the CYP4 family of enzymes, are covalently linked to their prosthetic heme group through an ester linkage. In the current study, we mutated a conserved CYP4 I-helix residue, E310 in rabbit CYP4B1, to glycine, alanine, and aspartate to examine the effect of these mutations on the extent of covalent heme binding and catalysis. All mutants expressed well in...

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PMID: 12693958
DOI: 10.1021/bi020667t

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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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