Pseudomonas Cytochrome c Peroxidase. XIII. pH-Denaturation of the Enzyme.
نویسندگان
چکیده
منابع مشابه
Isolation and properties of cytochrome c peroxidase from Pseudomonas denitrificans.
The isolation of cytochrome c peroxidase, cytochrome c4, cytochrome c-551 and azurin from Pseudomonas dentrificans is described. The peroxidase has a molecular weight of 63,000 and an isoelectric point of 5.6. Its absorption spectrum suggests that it contains two haem c groups/molecule. Preliminary steady-state kinetic data are reported with cytochromes c-551 and c4 and azurin as the second sub...
متن کاملThe crystal structure of cytochrome c peroxidase.
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...
متن کاملA quantitative model for the mechanism of action of the cytochrome c peroxidase of Pseudomonas aeruginosa.
Each of the elementary reaction steps in both the activation process and catalytic cycle of the cytochrome c peroxidase of Pseudomonas aeruginosa was characterized using stopped-flow methods. A synthesis of these data led to the establishment of a quantitative model for the action of this enzyme. Comparisons were made between experimental data and calculations over a wide range of enzyme, reduc...
متن کاملStudies 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 کامل-cytochrome c variants: Comparison with solvent denaturation
Thermal denaturation studies as a function of pH were carried out on wild-type iso-I-cytochrome c and three variants of this protein at the solvent-exposed position 73 of the sequence. By examining the enthalpy and T, at various pH values, the heat capacity increment (AC,,), which is dominated by the degree of change in nonpolar hydration upon protein unfolding, was found for the wild type wher...
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: 1977
ISSN: 0904-213X
DOI: 10.3891/acta.chem.scand.31b-0604