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The Journal of Biological Chemistry|July 25, 1993
The porphyrin-iron hybrid hemoglobins. Absence of the Fe-His bonds in one type of subunits favors a deoxy-like structure with low oxygen affinityM Fujii, H Hori, G Miyazaki, et al.The Journal of Biological Chemistry|October 25, 1978
Studies on cobalt myoglobins and hemoglobins. Proton magnetic resonance investigation of the subunit interaction in iron-cobalt hybrid hemoglobinsM Ikeda-Saito, T Inubushi, G G McDonald, et al.The Journal of Biological Chemistry|August 25, 1986
Resonance Raman study on cytochrome c peroxidase and its intermediate. Presence of the Fe(IV) = O bond in compound ES and heme-linked ionizationS Hashimoto, J Teraoka, T Inubushi, et al.The Journal of Biological Chemistry|June 10, 1984
Geminate combination of oxygen with iron-cobalt hybrid hemoglobinsR J Morris, Q H Gibson, M Ikeda-Saito, et al.Biochemistry|July 23, 1991
Experimental resolution of cooperative free energies for the ten ligation species of cobalt(II)/iron(II)-CO hemoglobinP C Speros, V J LiCata, T Yonetani, et al.Proceedings of the National Academy of Sciences of the United States of America|April 1, 1971
Structural measurements in hemoprotiens: use of spin-labeled protoheme as a probe of heme environmentT Asakura, J S Leigh, H R Drott, et al.The Journal of Biological Chemistry|January 25, 1977
Studies on cobalt myoglobins and hemoglobins. Preparation of isolated chains containing cobaltous protoporphyrin IX and characterization of their equilibrium and kinetic properties of oxygenation and EPR spectraM Ikeda-Saito, H Yamamoto, K Imai, et al.The Journal of Biological Chemistry|July 25, 1977
Studies on cobalt myoglobins and hemoglobins. Interaction of sperm whale myoglobin and Glycera hemoglobin with molecular oxygenM Ikeda-Saito, T Iizuka, H Yamamoto, et al.Proceedings of the National Academy of Sciences of the United States of America|April 30, 1996
Heterometallic hybrids of homometallic human hemoglobinsY Huang, T Yonetani, A Tsuneshige, et al.Biochemistry|August 18, 1992
Hydrogen bonding to the bound dioxygen in oxy cobaltous myoglobin reduces the superhyperfine coupling to the proximal histidineH C Lee, M Ikeda-Saito, T Yonetani, et al.Pageof 9