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Article

Ligand migration in the truncated hemoglobin-II from Mycobacterium tuberculosis: the role of G8 tryptophan.

The Journal of biological chemistry - 30 Jan 2009

Guallar Victor, Lu Changyuan, Borrelli Kenneth, Egawa Tsuyoshi, Yeh Syun-Ru

Abstract excerpt

Resonance Raman studies show that the heme-bound CO in trHbO, a truncated-II hemoglobin from Mycobacterium tuberculosis, is exposed to an environment with a positive electrostatic potential. The mutation of Trp(G8), an absolutely conserved residue in group II and III truncated hemoglobins, to Phe introduces two new Fe-CO conformers, both of which exhibit reduced electrostatic potentials. Computer simulations...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 19019831
DOI: 10.1074/jbc.M806183200
PMCID: PMC6430104

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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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