pH Induced Conformational And Structural Alterations On Choline Oxidase
نویسندگان
چکیده
منابع مشابه
Functional and structural alterations induced by copper in xanthine oxidase.
Xanthine oxidase (XO), a key enzyme in purine metabolism, produces reactive oxygen species causing vascular injuries and chronic heart failure. Here, copper's ability to alter XO activity and structure was investigated in vitro after pre-incubation of the enzyme with increasing Cu(2+) concentrations for various periods of time. The enzymatic activity was measured by following XO-catalyzed xanth...
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A reversible effect of pH on the ionization of amino-acid residues at the active center of choline oxidase was observed near the optimum pH (8). Inactivation of choline oxidase took place in the pH ranges 3-6 and 9-11, in which irreversible changes in the structure occur leading to the enzyme inactivation. The first order rate constants of the enzyme's inactivation at various pH values were est...
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The pH-induced conformational transition in the CuA domain of subunit II of cytochrome oxidase of Paracoccus denitrificans (PdII) has been investigated using various spectroscopic and stopped-flow kinetic methods. UV-visible absorption and circular dichroism studies showed that an increase in pH from 6 to 10 leads to a conformation change with pK(a) = 8.2 associated with the CuA site of the pro...
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Recently considerable attention has been centered upon the relation of choline oxidase activity to folic acid, the Leuconostoc citrovorum factor (LCF), ascorbic acid, and vitamin B,,. From this laboratory it has been indicated that rat liver choline oxidase can be stimulated in vitro under certain conditions by these factors, especially if the activity of the enzyme is previously decreased by d...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 2009
ISSN: 0006-3495
DOI: 10.1016/j.bpj.2008.12.3046