Tetsutaro Iizuka

TL;DR: It has been found that temperature-dependent transitions exist in squares of effective Bohr magneton numbers for ferrihemoglobin cyanide, as seen in the case of ferrimyoglobin complexes, and thermal equilibria between high-spin and low-spin states of Fe 3+ in hemes are explained.

TL;DR: The protein structure of cytochrome b5 in comparison with that of cy tochrome c is compared based on the results above as well as those of X-ray studies by Dickerson, R. and Mathews, F.

TL;DR: In horse and sperm whale ferric myoglobins, pH-dependent shift of heme-ring methyl signals above p2H 10 was analyzed on the basis of rapid exchange between alkaline and acidic forms, and limiting shifts of three methyl signals were reasonably determined for purely alkaline form.

TL;DR: Results below pH 10 suggested the existence of a transient species in the isomerization reaction between the species with and without a 695 nm band, which suggests that the sixth ligand is still Met-80, although the protein conformation might be different from that at neutral pH.

TL;DR: Hyperfine shifts of these samples below −10 ppm showed abnormal temperature dependence, except purely low-spin complexes such as the imidazole complex of human hemoglobin and cyanide complexes of myoglobin and hemoglobin.