| Literature DB >> 17599416 |
Amie K Boal1, Eylon Yavin, Jacqueline K Barton.
Abstract
The [4Fe-4S] cluster is ubiquitous to a class of base excision repair enzymes in organisms ranging from bacteria to man and was first considered as a structural element, owing to its redox stability under physiological conditions. When studied bound to DNA, two of these repair proteins (MutY and Endonuclease III from Escherichia coli) display DNA-dependent reversible electron transfer with characteristics typical of high potential iron proteins. These results have inspired a reexamination of the role of the [4Fe-4S] cluster in this class of enzymes. Might the [4Fe-4S] cluster be used as a redox cofactor to search for damaged sites using DNA-mediated charge transport, a process well known to be highly sensitive to lesions and mismatched bases? Described here are experiments demonstrating the utility of DNA-mediated charge transport in characterizing these DNA-binding metalloproteins, as well as efforts to elucidate this new function for DNA as an electronic signaling medium among the proteins.Entities:
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Year: 2007 PMID： 17599416 PMCID： PMC2094209 DOI： 10.1016/j.jinorgbio.2007.05.001
Source DB: PubMed Journal: J Inorg Biochem ISSN： 0162-0134 Impact factor: 4.155