Distal HISARG mutation in bovine myoglobin results in a ligand binding site similar to the abnormal beta site of hemoglobin Zurich (β63 HISARG)
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference13 articles.
1. Hemoglobin and Myoglobin in Their Reactions with Ligands;Antonini,1971
2. Hemoglobin;Dickerson,1983
3. Dynamic protein structures. Effects of pH on conformer stabilities at the ligand-binding site of bovine heart myoglobin carbonyl.
4. Evidence from infrared and 13C NMR spectra for discrete rapidly interconverting conformers at the carbon monoxide binding sites of hemoglobins A and Zurich.
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2. Tyrosine B10 Inhibits Stabilization of Bound Carbon Monoxide and Oxygen in Soybean Leghemoglobin;Biochemistry;2004-04-27
3. Iron ligand recognition by monomeric hemoglobins;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1996-07
4. [28] Fourier transform infrared analysis of carbonyl and nitrosyl complexes of cytochrome-c oxidase from Saccharomyces cerevisiae;Methods in Enzymology;1995
5. Specific modification of structure and property of myoglobin by the formation of tetrazolylhistidine 64(E7). Reaction of the modified myoglobin with molecular oxygen.;Journal of Biological Chemistry;1993-09
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