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Residues in the Distal Heme Pocket of Neuroglobin
Journal of Biological Chemistry
Amino acid residues in the ligand binding pocket of human neuroglobin have been identified by site-directed mutagenesis and their properties investigated by resonance Raman and flash photolysis methods. Wildtype neuroglobin has been shown to have six-coordinate heme in both ferric and ferrous states. Substitution of His 96 by alanine leads to complete loss of heme, indicating that His 96 is the proximal ligand. The resonance Raman spectra of M69L and K67T mutants were similar to those ofdoi:10.1074/jbc.m311748200 pmid:14645216 fatcat:citc6tkhlnc25fjfej3vzufhhm