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Sulfur K-Edge XAS Studies of the Effect of DNA Binding on the [Fe_4S_4] Site in EndoIII and MutY

Ha, Yang and Arnold, Anna R. and Nuñez, Nicole N. and Bartels, Phillip L. and Zhou, Andy and David, Sheila S. and Barton, Jacqueline K. and Hedman, Britt and Hodgson, Keith O. and Solomon, Edward I. (2017) Sulfur K-Edge XAS Studies of the Effect of DNA Binding on the [Fe_4S_4] Site in EndoIII and MutY. Journal of the American Chemical Society, 139 (33). pp. 11434-11442. ISSN 0002-7863. PMCID PMC5568943. doi:10.1021/jacs.7b03966. https://resolver.caltech.edu/CaltechAUTHORS:20170719-101916396

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Abstract

S K-edge X-ray absorption spectroscopy (XAS) was used to study the [Fe_4S_4] clusters in the DNA repair glycosylases EndoIII and MutY to evaluate the effects of DNA binding and solvation on Fe–S bond covalencies (i.e., the amount of S 3p character mixed into the Fe 3d valence orbitals). Increased covalencies in both iron–thiolate and iron–sulfide bonds would stabilize the oxidized state of the [Fe_4S_4] clusters. The results are compared to those on previously studied [Fe_4S_4] model complexes, ferredoxin (Fd), and to new data on high-potential iron–sulfur protein (HiPIP). A limited decrease in covalency is observed upon removal of solvent water from EndoIII and MutY, opposite to the significant increase observed for Fd, where the [Fe_4S_4] cluster is solvent exposed. Importantly, in EndoIII and MutY, a large increase in covalency is observed upon DNA binding, which is due to the effect of its negative charge on the iron–sulfur bonds. In EndoIII, this change in covalency can be quantified and makes a significant contribution to the observed decrease in reduction potential found experimentally in DNA repair proteins, enabling their HiPIP-like redox behavior.


Item Type:Article
Related URLs:
URLURL TypeDescription
http://dx.doi.org/10.1021/jacs.7b03966DOIArticle
http://pubs.acs.org/doi/abs/10.1021/jacs.7b03966PublisherArticle
http://pubs.acs.org/doi/suppl/10.1021/jacs.7b03966PublisherSupporting Information
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5568943PubMed CentralArticle
ORCID:
AuthorORCID
David, Sheila S.0000-0001-5873-7935
Barton, Jacqueline K.0000-0001-9883-1600
Solomon, Edward I.0000-0003-0291-3199
Alternate Title:S K-edge XAS Studies of the Effect of DNA Binding on the [Fe_4S_4] Site in EndoIII and MutY
Additional Information:© 2017 American Chemical Society. Received: April 19, 2017. Published: July 18, 2017. This work was supported by NIH grants (GM040392, E.I.S.; GM103393, K.O.H.; GM120087 J.K.B.; CA069875 S.S.D.). J.K.B. also thanks the Moore Foundation. A.R.A. was supported by the National Institute of Aging of the NIH on a predoctoral NRSA (F31AG040954). Portions of this research were carried out at the Stanford Synchrotron Radiation Lightsource (SSRL), a Directorate of SLAC National Accelerator Laboratory and an Office of Science User Facility operated for the U.S. Department of Energy (DOE) Office of Science by Stanford University. The SSRL Structural Molecular Biology Program is supported by the DOE Office of Biological and Environmental Research and by the National Institutes of Health, National Institute of General Medical Sciences (P41GM103393). The authors declare no competing financial interest.
Funders:
Funding AgencyGrant Number
NIHGM040392
NIHGM103393
NIHGM120087
NIHCA069875
Gordon and Betty Moore FoundationUNSPECIFIED
NIH Predoctoral FellowshipF31AG040954
National Institute on AgingUNSPECIFIED
Department of Energy (DOE)UNSPECIFIED
NIHP41GM103393
Issue or Number:33
PubMed Central ID:PMC5568943
DOI:10.1021/jacs.7b03966
Record Number:CaltechAUTHORS:20170719-101916396
Persistent URL:https://resolver.caltech.edu/CaltechAUTHORS:20170719-101916396
Official Citation:Sulfur K-Edge XAS Studies of the Effect of DNA Binding on the [Fe4S4] Site in EndoIII and MutY Yang Ha, Anna R. Arnold, Nicole N. Nuñez, Phillip L. Bartels, Andy Zhou, Sheila S. David, Jacqueline K. Barton, Britt Hedman, Keith O. Hodgson, and Edward I. Solomon Journal of the American Chemical Society 2017 139 (33), 11434-11442 DOI: 10.1021/jacs.7b03966
Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:79202
Collection:CaltechAUTHORS
Deposited By: Ruth Sustaita
Deposited On:19 Jul 2017 18:21
Last Modified:15 Nov 2021 17:46

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