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Human endonuclease III/NTH1: focusing on the [4Fe-4S] cluster and the N-terminal domain.

Elin MoeCélia M SilveiraLidia ZuccarelloFilipe RolloMeike StelterSalvatore De BonisCatharina Kulka-PeschkeSagie KatzPeter HildebrandtIngo ZebgerJoanna TimminsSmilja Todorovic
Published in: Chemical communications (Cambridge, England) (2022)
Human Endonuclease III (EndoIII), hNTH1, is an FeS containing enzyme which repairs oxidation damaged bases in DNA. We report here the first comparative biophysical study of full-length and an N-terminally truncated hNTH1, with a domain architecture homologous to bacterial EndoIII. Vibrational spectroscopy, spectroelectrochemistry and SAXS experiments reveal distinct properties of the two enzyme forms, and indicate that the N-terminal domain is important for DNA binding at the onset of damage recognition.
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