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活性位点氨基酸残基对Cu2Zn2SOD催化活性的作用。

The role of the active site amino acid residues on the catalytic activity of Cu2Zn2SOD.

作者信息

Scozzafava A, Viezzoli M S

机构信息

Department of Chemistry, University of Florence, Italy.

出版信息

Mol Chem Neuropathol. 1993 May-Jun;19(1-2):193-204. doi: 10.1007/BF03160179.

DOI:10.1007/BF03160179
PMID:8363704
Abstract

Copper, zinc superoxide dismutase, the enzyme that catalyzes the dismutation of the superoxide ion, is a key enzyme for neurodegenerative processes caused by the formation into tissues of this reactive free radical. Although the structure of enzyme is known, the catalytic mechanism has not yet fully elucidated. The copper ion represents the center, which exchanges electrons with the superoxide ion, but other residues present in the active site seem to play a relevant role. The most recent advancements in clarifying the structure-function relationship in this enzyme are discussed.

摘要

铜锌超氧化物歧化酶是一种催化超氧离子歧化反应的酶,是由这种活性自由基在组织中形成所引发的神经退行性过程的关键酶。尽管该酶的结构已知,但其催化机制尚未完全阐明。铜离子是与超氧离子交换电子的中心,但活性位点中的其他残基似乎也发挥着重要作用。本文讨论了在阐明该酶结构-功能关系方面的最新进展。

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