title: ATP-stimulated, DNA-mediated redox signaling by XPD, a DNA repair and transcription helicase.
abstract: Using DNA-modified electrodes, we show DNA-mediated signaling by XPD, a helicase that contains a [4Fe-4S] cluster and is critical for nucleotide excision repair and transcription. The DNA-mediated redox signal resembles that of base excision repair proteins, with a DNA-bound redox potential of ~80 mV versus NHE. Significantly, this signal increases with ATP hydrolysis. Moreover, the redox signal is substrate-dependent, reports on the DNA conformational changes associated with enzymatic function, and may reflect a general biological role for DNA charge transport.
authors.affiliation: Division of Chemistry and Chemical Engineering, California Institute of Technology, Pasadena, California 91125, USA.
authors.forename: Timothy P
authors.initials: TP
authors.lastname: Mui
authors.forename: Jill O
authors.initials: JO
authors.lastname: Fuss
authors.forename: Justin P
authors.initials: JP
authors.lastname: Ishida
authors.forename: John A
authors.initials: JA
authors.lastname: Tainer
authors.forename: Jacqueline K
authors.initials: JK
authors.lastname: Barton
mesh_terms: D000255:Adenosine Triphosphate / Q000737:chemistry / Q000378:metabolism*; D004247:DNA / Q000737:chemistry / Q000378:metabolism*; D004260:DNA Repair; D008958:Models, Molecular; D010084:Oxidation-Reduction; D015398:Signal Transduction; D051759:Xeroderma Pigmentosum Group D Protein / Q000737:chemistry / Q000378:metabolism*
chemical_list: D000255:Adenosine Triphosphate; D004247:DNA; D051759:Xeroderma Pigmentosum Group D Protein