منابع مشابه
Cobalt-substituted horseradish peroxidase.
Horseradish peroxidase can be reconstituted with cobalt porphyrin to give a cobaltic holoenzyme having physicochemical properties quite similar to those of the native ferric protein. The cobaltic protein (Co3+HRP) can be reduced to the cobaltous form (CoHRP), the analogue of ferroperoxidase and the reduced cobalt protein can bind O2 to form an analogue of oxyferroperoxidase (Compound III). Sinc...
متن کاملPhotooxidation of porphyrin in Mg-substituted horseradish peroxidase.
Upon photoirradiation under aerobic conditions, the porphyrin prosthetic group in Mg-substituted horseradish peroxidase was oxidized to a mixture of its pi-cation radical and an oxidized product with an absorption band at 448 nm. The 448 nm compound was then converted to a 489 nm compound in the dark and the activation energy for the conversion was 19.3 kcal/mol. About 1 mol of O2 was consumed ...
متن کاملStudies on Horseradish Peroxidase
The kinetics of the oxidation of p-cresol by Compound II of horseradish peroxidase has been studied by the stopped flow technique at an ionic strength of 0.11 from pH 2 to 11. In acid solution the reaction is kinetically first order in jcresol, but in the alkaline region a saturation effect attributable to complex formation is observed. At very high pH an additional second order reaction betwee...
متن کاملPeroxidase Isoenzymes from Horseradish Roots
The reactivity of histidine in horseradish peroxidase isoenzymes Al and C was determined by titrating with diazonium-lH-tetrazole. No exposed histidine residue was detected in the native isoenzymes. Upon removal of the heme prosthetic group, however, all three histidine residues became titratable. Studies with p-chloromercuribenzoate and 14C-iodoacetamide indicated that the 6 half-cystine resid...
متن کاملOxygen diffusion through horseradish peroxidase.
The quenching by molecular oxygen of the fluorescence from a protoporphyrin IX adduct of horseradish peroxidase has been investigated using both intensity and time-resolved techniques. The bimolecular quenching rate constant determined for this process, as evaluated by the conventional Stern-Volmer analysis, was 2 x 10(8) M-1 s-1, among the lowest observed for protein systems. This result sugge...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1977
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)39950-7