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

Elin Moe, Célia M. Silveira, Lidia Zuccarello, Filipe Rollo, Meike Stelter, Salvatore De Bonis, Catharina Kulka-Peschke, Sagie Katz, Peter Hildebrandt, Ingo Zebger, Joanna Timmins, Smilja Todorovic

Research output: Contribution to journalArticlepeer-review

2 Citations (Scopus)

Abstract

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.

Original languageEnglish
JournalChemical Communications
Volume244
DOIs
Publication statusPublished - 24 Oct 2022

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