Identification of the iron-carbonyl stretch in distal histidine mutants of carbonmonoxymyoglobin.
Soret-excitation resonance Raman (RR) spectra are reported for six distal histidine mutants of carbonmonoxymyoglobin including H64A, H64V, H64L, H64I, H64W, and H64W/L29F. Based on 13CO isotope shifts, the iron-carbonyl stretching vibrations are unambiguously identified. The correct assignment of these modes eliminates the differences in the conformational substate occupations predicted by the RR versus IR data.
Ling
J
J
Department of Chemistry, University of California, Riverside 92521-0403.
Li
T
T
Olson
J S
JS
Bocian
D F
DF
D001665:Binding Sites; D006639:Histidine / Q000737:chemistry*; D006801:Humans; D008968:Molecular Conformation; D009211:Myoglobin / Q000737:chemistry* / Q000235:genetics
D009211:Myoglobin; C018013:carboxymyoglobin; D006639:Histidine