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Article

Structural evidence: a single charged residue affects substrate binding in cytochrome P450 BM-3.

Biochemistry - 1 Oct 2013

Catalano Jaclyn, Sadre-Bazzaz Kianoush, Amodeo Gabriele A, Tong Liang, McDermott Ann

Abstract excerpt

Cytochrome P450 BM-3 is a bacterial enzyme with sequence similarity to mammalian P450s that catalyzes the hydroxylation of fatty acids with high efficiency. Enzyme-substrate binding and dynamics has been an important topic of study for cytochromes P450 because most of the crystal structures of substrate-bound structures show the complex in an inactive state. We have determined a new crystal structure for...

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Identifiers

PMID: 23829560
DOI: 10.1021/bi4000645
PMCID: PMC5945292

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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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