title: Spectral properties unique to the myoglobins lacking the usual distal histidine residue.
abstract: Myoglobins can be divided into two groups. One group contains the usual myoglobins that have histidine at the distal (E7) position, and the other contains a few, but interesting myoglobins that lack the usual distal histidine residue. Spectroscopic examinations have shown that there is a remarkable difference in the Soret band between the two types of myoglobin, and an absorbance ratio of the Soret peak of the acidic met-form to that of the oxy-form seems to be very useful as a simple criterion for predicting whether or not a myoglobin has the usual distal histidine residue.
authors.affiliation: Biological Institute, Faculty of Science, Tohoku University, Sendai, Japan.
authors.forename: K
authors.initials: K
authors.lastname: Shikama
authors.forename: A
authors.initials: A
authors.lastname: Matsuoka
mesh_terms: D000818:Animals; D001048:Aplysia; D006639:Histidine; D008786:Metmyoglobin; D009211:Myoglobin; D013057:Spectrum Analysis
chemical_list: D009211:Myoglobin; C017595:oxymyoglobin; D008786:Metmyoglobin; D006639:Histidine