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

doi:10.1021/bi00475a021

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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-exci...

Topics

Binding Sites
Carbon Monoxide
Escherichia coli
Hemoglobins
Humans
Iron
Molecular Structure
Mutation
Protein Engineering
Spectrum Analysis, Raman
X-Ray Diffraction

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