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Biochem J. 2001 Dec 15;360(Pt 3):717-26.

Influence of electrochemical properties in determining the sensitivity of [4Fe-4S] clusters in proteins to oxidative damage.

Author information

1
Department of Chemistry, Oxford University, OX1 3QR, England, U.K.

Abstract

Interconversion between [4Fe-4S] cubane and [3Fe-4S] cuboidal states represents one of the simplest structural changes an iron-sulphur cluster can undertake. This reaction is implicated in oxidative damage and in modulation of the activity and regulation of certain enzymes, and it is therefore important to understand the factors governing cluster stability and the processes that activate cluster conversion. In the present study, protein film voltammetry has been used to induce and monitor the oxidative conversion of [4Fe-4S] into [3Fe-4S] clusters in different variants of Azotobacter vinelandii ferredoxin I (AvFdI; the 8Fe form of the native protein), and DeltaThr(14)/DeltaAsp(15), Thr(14)-->Cys (T14C) and C42D mutants. The electrochemical results have been correlated with the differing oxygen sensitivities of [4Fe-4S] clusters, and comparisons have been drawn with other ferredoxins (Desulfovibrio africanus FdIII, Clostridium pasteurianum Fd, Thauera aromatica Fd and Pyrococcus furiosus Fd). In contrast with high-potential iron-sulphur proteins (HiPIPs) for which the oxidized species [4Fe-4S](3+) is inert to degradation and can be isolated, the hypervalent state in these ferredoxins (most obviously the 3+ level) is very labile, and the reduction potential at which this is formed is a key factor in determining the cluster's resistance to oxidative damage.

PMID:
11736664
PMCID:
PMC1222277
DOI:
10.1042/0264-6021:3600717
[Indexed for MEDLINE]
Free PMC Article

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