Studies on the equilibria and kinetics of the reactions of peroxidases with ligands. I. The reaction of ferroperoxidases with carbon monoxide.
Studies on the equilibria and kinetics of the reactions of peroxidases with ligands. I. The reaction of ferroperoxidases with carbon monoxide.
复制标题
过氧化物酶与配体反应的平衡和动力学研究。
DOI:
10.1021/bi00888a016
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发表时间:
1965
期刊:
影响因子:
2.9
通讯作者:
R. Zito
中科院分区:
文献类型:
--
作者:
D. Kertesz;E. Antonini;M. Brunori;J. Wyman;R. Zito
Denis Kertesz, Eraldo Antonini, Maurizio Brunori, Jeffries Wyman, and Romano Zito abstract: The equilibrium and kinetics of the reaction of horseradish and fig ferroperoxidases with carbon monoxide have been studied. For both peroxidases, at 20, the equilibrium constant (L) is about 4.5 X 106 m_1 and the combination velocity constant (/') about 4 X 103 M-1sec-1.. L eroxidases are a heterogeneous group of heme pro-teins which may act as catalysts in reactions between peroxides and an electron donor (Paul, 1963; Nichols, 1962; Saunders et al., 1964). The ferri form of peroxi-dase is thought to combine with peroxidesto give a series of complexes whichin turn react with the oxi-dizable substrates (Keilin and Mann, 1937; Theorell, 1941; Chance, 1951).