منابع مشابه
Studies on Cytochrome c Peroxidase
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...
متن کاملKinetic studies on [methionine sulphoxide] cytochrome c.
A cytochrome c haem ligand, methionine-80, was photo-oxidized to methionine sulphoxide and the subsequent changes in redox properties and ligand binding were monitored kinetically. Isoelectric focusing of the product showed the presence of a single oxidized species, capable of binding CO when reduced. The binding of CO to the reduced protein was followed in stopped-flow experiments, which revea...
متن کاملComplex-formation between cytochrome c and cytochrome c peroxidase. Equilibrium and titration studies.
1. Physical studies of complex-formation between cytochrome c and yeast peroxidase are consistent with kinetic predictions that these complexes participate in the catalytic activity of yeast peroxidase towards ferrocytochrome c. Enzyme-ferricytochrome c complexes have been detected both by the analytical ultracentrifuge and by column chromatography, whereas an enzyme-ferrocytochrome c complex w...
متن کاملSpectral studies of horse heart porphyrin cytochrome c.
Removal of the heme iron from cytochrome c to generate porphyrin cytochrome c relieves the quenching of porphyrin fluorescence and enhances the fluorescence of the single tryptophan residue and the 4 tyrosine residues. The intensity of the porphyrin fluorescence is not perturbed by denaturation of the protein at neutral pH using either urea or guanidine hydrochloride. However, the amplitude of ...
متن کاملStudies on Cytochrome Oxidase. Vi. Kinetics of the Aerobic Oxidation of Ferrocytochrome C by Cytochrome Oxidase.
The rate of reaction can be determined by measuring the rate of either oxygen consumption or ferrocytochrome c oxidation. When the rate of oxygen consumption is measured either manometrically or polarographically, a mixture of a limited amount of cytochrome c and an excess of reducing agent, instead of excess ferrocytochrome c, is used as an electron donor system. In this case the true electron...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Acta Chemica Scandinavica
سال: 1955
ISSN: 0904-213X
DOI: 10.3891/acta.chem.scand.09-0538