Monooxygenase activity of cytochrome c peroxidase.
نویسندگان
چکیده
منابع مشابه
Peroxidase activity enhancement of horse cytochrome c by dimerization.
The peroxidase activity of horse cytochrome c was enhanced by its dimerization, where its Compound III (oxy-form) and Compound I (oxoferryl porphyrin π-cation radical) species were detected in the reactions with hydrogen peroxide and meta-chloroperbenzoic acid, respectively. These results show that oligomeric cytochrome c can contribute as a proapoptotic conformer by the increased peroxidase ac...
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Apoproteins of cytochrome c peroxidase, horseradish peroxidase, and sperm whale myoglobin were recombined with manganese complexes of proto-, hemato-, meso-, and deuteroporphyrins to form manganese porphyrin-protein complexes. These complexes were purified by column chromatography. All the manganese porphyrin-containing cytochrome c peroxidases were crystallized. Light absorption maxima of mang...
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The three-dimensional conformation of yeast cytochrome c peroxidase has been determined from a 2.5 A electron density map computed with phases obtained from two isomorphous mercury derivatives. Partial sequence information that has recently become available aided in completion of the tracing of the polypeptide backbone, confirmed the presence of a proximal histidine heme ligand and aided in ide...
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Cytochrome bd is a prokaryotic terminal oxidase that catalyses the electrogenic reduction of oxygen to water using ubiquinol as electron donor. Cytochrome bd is a tri-haem integral membrane enzyme carrying a low-spin haem b558, and two high-spin haems: b595 and d. Here we show that besides its oxidase activity, cytochrome bd from Escherichia coli is a genuine quinol peroxidase (QPO) that reduce...
متن کاملInvestigation of electron tunneling between cytochrome c peroxidase and cytochrome c.
The nature of electron transfer between the bound complex cytochrome c and cytochrome c peroxidase has been investigated. Experimental verification of the predicted charge-transfer band provides evidence of electron tunneling as the mechanism of transfer between these molecules in solution at room temperature. The measured transfer distance is congruent to 7 angstroms between heme edges, which ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1992
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(19)50370-2