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Article

Fluoride as a probe for H-bonding interactions in the active site of heme proteins: the case of Thermobifida fusca hemoglobin.

Journal of the American Chemical Society - 28 Dec 2011

Nicoletti Francesco P, Droghetti Enrica, Boechi Leonardo, Bonamore Alessandra, Sciamanna Natascia, Estrin Darío A, Feis Alessandro, Boffi Alberto, Smulevich Giulietta

Abstract excerpt

The structural and functional properties of the active site of the bacterial hemoglobin from Thermobifida fusca are largely determined by three polar amino acids: TrpG8, TyrCD1, and TyrB10. We have exploited the availability of a combinatorial set of mutants, in each of which these three amino acids have been singly, doubly, or triply replaced by a Phe residue, to perform a detailed study on H-bonding...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 22091531
DOI: 10.1021/ja209312k

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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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