Altered coordination in a blue copper protein upon association with redox partner revealed by carbon–deuterium vibrational probes-Reference-Cited by-同舟云学术

Altered coordination in a blue copper protein upon association with redox partner revealed by carbon–deuterium vibrational probes

Published:2022 Issue:36 Volume:24 Page:21588-21592
ISSN:1463-9076
Container-title:Physical Chemistry Chemical Physics
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Mammoser Claire C.¹,Agh Ryan E.¹,Garcia Nicholas M.¹^ORCID,Wang Yiqi¹,Thielges Megan C.¹^ORCID

Affiliation:

1. Department of Chemistry, Indiana University, Bloomington, IN 47405, USA

Abstract

IR spectroscopy of a carbon–deuterium vibrational probe reveals that binding of the redox partner induces significant strengthening of the Cu-Cys89 bond in plastocyanin.

Funder

U.S. Department of Energy

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Link

http://pubs.rsc.org/en/content/articlepdf/2022/CP/D2CP03314C

Reference51 articles.

1. S. J.Lippard and J. M.Berg , Principles of Bioinorganic Chemistry , University Science Books , Mill Valley, CA , 1994

2. D. S.Bendall , Protein Electron Transfer , BIOS Scientific Publishers Limited , Oxford, UK , 1996

3. J.McCleverty , Chemistry of the First-row Transition Metals , Oxford University Press , Oxford, UK , 1999

4. Recent advances in understanding blue copper proteins

5. Inner- and outer-sphere metal coordination in blue copper proteins

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