The synucleins are a family of redox-active copper binding proteins

Davies, Paul, Wang, Xiaoyan, Sarell, Claire J., Drewett, Alex, Marken, Frank, Viles, John H. and Brown, David R. (2011) The synucleins are a family of redox-active copper binding proteins. Biochemistry, 50 (1) . pp. 37-47. ISSN 0006-2960 [Article] (doi:10.1021/bi101582p)


Thermodynamic studies in conjunction with EPR confirm that α-synuclein, β-synuclein, and γ-synuclein bind copper(II) in a high affinity 1:1 stoichiometry. γ-Synuclein demonstrates the highest affinity, in the picomolar range, while α-synuclein and β-synuclein both bind copper(II) with nanomolar affinity. The copper center on all three proteins demonstrates reversible or partly reversible redox cycling. Various mutations show that the primary coordinating ligand for copper(II) is located within the N-terminal regions between residues 2-9. There is also a contribution from the C-terminus in conjunction with the histidine at position 50 in α-synuclein and position 65 in β-synuclein, although these regions appear to have little effect on overall coordination stability. These histidines and the C-terminus, however, appear to be critical to the redox engine of the proteins.

Item Type: Article
Research Areas: A. > School of Science and Technology > Natural Sciences
Item ID: 11272
Depositing User: Devika Mohan
Date Deposited: 18 Sep 2013 08:38
Last Modified: 13 Oct 2016 14:27

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