The rich electrochemistry and redox reactions of the copper sites in the cellular prion protein

被引：33

作者：

Zhou, Feimeng ^{[1
]}

Millhauser, Glenn L. ^{[2
]}

机构：

[1] Calif State Univ Los Angeles, Dept Chem & Biochem, Los Angeles, CA 90032 USA

[2] Univ Calif Santa Cruz, Dept Chem & Biochem, Santa Cruz, CA 95064 USA

来源：

COORDINATION CHEMISTRY REVIEWS | 2012年 / 256卷 / 19-20期

关键词：

Prion protein; Copper binding; Electrochemistry; Redox reactions; Oxidative stress; OCTAPEPTIDE REPEAT REGION; PARKINSONS-DISEASE; AMYLOID-BETA; ALZHEIMERS-DISEASE; HYDROGEN-PEROXIDE; SUPEROXIDE-DISMUTASE; PH-DEPENDENCE; ASCORBIC-ACID; CATALYZED OXIDATION; COORDINATION MODES;

D O I：

10.1016/j.ccr.2012.04.035

中图分类号：

O61 [无机化学];

学科分类号：

070301 ; 081704 ;

摘要：

This paper reviews recent electrochemical studies of the copper complexes of prion protein (PrP) and its related peptides, and correlates their redox behavior to chemical and biologically relevant reactions. Particular emphasis is placed on the difference in redox properties between copper in the octarepeat (OR) and the non-OR domains of PrP, as well as differences between the high and low copper occupancy states in the OR domain. Several discrepancies in the literature concerning these differences are discussed and reconciled. The PrP copper complexes, in comparison to copper complexes of other amyloidogenic proteins/peptides, display a more diverse and richer redox chemistry. The specific protocols and caveats that need to be considered in studying the electrochemistry and redox reactions of copper complexes of PrP, PrP-derived peptides, and other related amyloidogenic proteins are summarized. (C) 2012 Elsevier B.V. All rights reserved.

引用

页码：2285 / 2296

页数：12

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