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Article

Effect of the distal residues on the vibrational modes of the Fe-CO bond in hemoglobin studied by protein engineering.

Biochemistry - 12 Jun 1990

Lin S H, Yu N T, Tame J, Shih D, Renaud J P, Pagnier J, Nagai K

Abstract excerpt

Using an Escherichia coli gene expression system, we have engineered human hemoglobin (Hb) mutants having the distal histidine (E7) and valine (E11) residues replaced by other amino acids. The interaction between the mutated distal residues and bound carbon monoxide has been studied by Soret-excited resonance Raman spectroscopy. The replacement of Val-E11 by Ala, Leu, Ile, and Met has no effect on the v(C-O),...

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PMID: 2201408
DOI: 10.1021/bi00475a021

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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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