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Altered coordination in a blue copper protein upon association with redox partner revealed by carbon-deuterium vibrational probes.
Mammoser, Claire C; Agh, Ryan E; Garcia, Nicholas M; Wang, Yiqi; Thielges, Megan C.
Affiliation
  • Mammoser CC; Department of Chemistry, Indiana University, Bloomington, IN 47405, USA. thielges@iu.edu.
  • Agh RE; Department of Chemistry, Indiana University, Bloomington, IN 47405, USA. thielges@iu.edu.
  • Garcia NM; Department of Chemistry, Indiana University, Bloomington, IN 47405, USA. thielges@iu.edu.
  • Wang Y; Department of Chemistry, Indiana University, Bloomington, IN 47405, USA. thielges@iu.edu.
  • Thielges MC; Department of Chemistry, Indiana University, Bloomington, IN 47405, USA. thielges@iu.edu.
Phys Chem Chem Phys ; 24(36): 21588-21592, 2022 Sep 21.
Article in En | MEDLINE | ID: mdl-36069424
ABSTRACT
Proteins tune the reactivity of metal sites; less understood is the impact of association with a redox partner. We demonstrate the utility of carbon-deuterium labels for selective analysis of delicate metal sites. Introduced into plastocyanin, they reveal substantial strengthening of the key Cu-Cys89 bond upon association with cytochrome f.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Plastocyanin / Copper Type of study: Risk_factors_studies Language: En Journal: Phys Chem Chem Phys Journal subject: BIOFISICA / QUIMICA Year: 2022 Document type: Article Affiliation country: Estados Unidos
Fulltext
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Plastocyanin / Copper Type of study: Risk_factors_studies Language: En Journal: Phys Chem Chem Phys Journal subject: BIOFISICA / QUIMICA Year: 2022 Document type: Article Affiliation country: Estados Unidos