Electrochemical and homogeneous electron transfers to the Alzheimer amyloid-beta copper complex follow a preorganization mechanism.

Abstract:

:Deciphering the electron transfer reactivity characteristics of amyloid β-peptide copper complexes is an important task in connection with the role they are assumed to play in Alzheimer's disease. A systematic analysis of this question with the example of the amyloid β-peptide copper complex by means of its electrochemical current-potential responses and of its homogenous reactions with electrogenerated fast electron exchanging osmium complexes revealed a quite peculiar mechanism: The reaction proceeds through a small fraction of the complex molecules in which the peptide complex is "preorganized" so as the distances and angles in the coordination sphere to vary minimally upon electron transfer, thus involving a remarkably small reorganization energy (0.3 eV). This preorganization mechanism and its consequences on the reactivity should be taken into account for reactions involving dioxygen and hydrogen peroxide that are considered to be important in Alzheimer's disease through the production of harmful reactive oxygen species.

authors

Balland V,Hureau C,Savéant JM

doi

10.1073/pnas.1011315107

subject

Has Abstract

pub_date

2010-10-05 00:00:00

pages

17113-8

issue

40

eissn

0027-8424

issn

1091-6490

pii

1011315107

journal_volume

107

pub_type

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