Blue Myoglobin Reconstituted with an Iron Porphycene Shows Extremely High Oxygen Affinity

• Published in: Journal of the American Chemical Society Vol. 124; no. 38; pp. 11226 - 11227
• Main Authors: Hayashi, Takashi, Dejima, Hirohisa, Matsuo, Takashi, Sato, Hideaki, Murata, Dai, Hisaeda, Yoshio
• Format: Journal Article
• Language: English
• Published: WASHINGTON American Chemical Society 25.09.2002; Amer Chemical Soc
• Subjects: Analytical, structural and metabolic biochemistry; Biological and medical sciences; Chemistry; Chemistry, Multidisciplinary; Fundamental and applied biological sciences. Psychology; Heme - chemistry; Kinetics; Metalloproteins; Myoglobin - chemistry; Myoglobin - metabolism; Other metalloproteins; Oxidation-Reduction; Oxygen - chemistry; Oxygen - metabolism; Physical Sciences; Porphyrins - chemistry; Proteins; Science & Technology; HEME; AUTOOXIDATION; CARBON-MONOXIDE; O-2; COORDINATION; CHEMICAL-MODIFICATION; SUBSTITUTED HEMINS; LIGAND; CO; BINDING; Myoglobin; Affinity; Oxygen; Iron

Myoglobin will be a good scaffold for engineering a function into proteins. To modulate the physiological function of myoglobin, almost all approaches have been demonstrated by site-directed mutagenesis, however, there are few studies which show a significant improvement in the function. In contrast...