Detail of "214769-28-5"

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Electrochemical analysis of heme functions of myoglobin using semi-artificial myoglobins

Electrochemical analysis of heme functions of myoglobin using semi-artificial myoglobins. Mie, Yasuhiro; Kishita, Midori; Neya, Saburo; Funasaki, Noriaki; Mizutani, Fumio; Nishiyama, Katsuhiko; Taniguchi, Isao (Department of Applied Chemistry and Biochemistry, Faculty of Engineering, Kumamoto University, Kurokami, Kumamoto 860-8555, Japan). Journal of Electroanalytical Chemistry, 588(2), 226-234 (English) 2006 Elsevier B. 214769-28-5 is just another one chemical used in this study.V. CODEN: JECHES. DOCUMENT TYPE: Journal CA Section: 6 (General Biochemistry) Section cross-reference(s): 72 To understand the roles of the vinyl groups of heme side chains of protoheme-IX in myoglobin (Mb), we replaced the protoheme-IX in native Mb with mesoheme-IX and deuteroheme-IX, and the bioelectrochem. properties of the substituted Mbs were compared with those of the native Mb. The cathodic peak and the formal potentials of the reconstituted Mbs examd. were more neg. by ~22-90 mV than those of the native Mb. The rates of autoxidn. for the oxy-forms of deutero-IX and meso-IX reconstituted Mbs at 35° and pH 7.0 were twice as fast than that of the native Mb. These results suggest that the vinyl groups of heme facilitate the redn. of Mbs, and prevent the autoxidn. of the heme iron. The dissocn. rate of cyanide ion from ferro-Mb was increased in the order of deutero(IX)Mb < meso(IX)Mb < native Mb. On the basis of the electroanal. studies of the reconstituted Mbs with mesoheme-III, mesoheme-XIII, deuteroheme-III, and deuteroheme-XIII, isomers of type IX, no significant influence of the side chain position of the porphyrin ring on the dissocn. property of the cyanide ion was obsd. The electron transfer kinetics of the reconstituted Mbs were also evaluated and compared with that of the native Mb. DeuteroMb exhibited a slower electron transfer rate const. than other Mbs. .