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Article

FTIR and resonance Raman studies of nitric oxide binding to H93G cavity mutants of myoglobin.

Biochemistry - 11 Dec 2001

Thomas M R, Brown D, Franzen S, Boxer S G

Abstract excerpt

Nitric oxide (NO) binds to the myoglobin (Mb) cavity mutant, H93G, forming either a five- or six-coordinate Fe-NO complex. The H93G mutation eliminates the covalent attachment between the protein and the proximal ligand, allowing NO to bind H93G possibly from the proximal side of the heme rather than the typical diatomic binding pocket on the distal side. The question of whether NO binds on the distal or proximal...

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Identifiers

PMID: 11732927
DOI: 10.1021/bi011440l

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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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