Electrochemical and Structural Study of the Buried Tryptophan in Azurin: Effects of Hydration and Polarity on the Redox Potential of W48-Reference-Cited by-同舟云学术

Electrochemical and Structural Study of the Buried Tryptophan in Azurin: Effects of Hydration and Polarity on the Redox Potential of W48

Published:2022-12-21 Issue:1 Volume:127 Page:133-143
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Tyson Kristin¹,Tangtartharakul Chanin B.²,Zeug Matthias³,Findling Nathan¹,Haddy Alice⁴,Hvastkovs Eli¹^ORCID,Choe Jun-yong¹³,Kim Judy E.²^ORCID,Offenbacher Adam R.¹^ORCID

Affiliation:

1. Department of Chemistry, East Carolina University, Greenville, North Carolina 27858, United States

2. Department of Chemistry and Biochemistry, University of California at San Diego, La Jolla, California 92093, United States

3. Department of Chemistry, East Carolina Diabetes and Obesity Institute, East Carolina University, Greenville North Carolina, 27858, United States

4. Department of Chemistry and Biochemistry, University of North Carolina at Greensboro, Greensboro, North Carolina 27402, United States

Funder

Division of Integrative Organismal Systems

National Cancer Institute

National Institute of General Medical Sciences

East Carolina University

Publisher

American Chemical Society (ACS)

Subject

Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.jpcb.2c06677

Reference64 articles.

1. Proton-Coupled Electron Flow in Protein Redox Machines

2. Biochemistry and Theory of Proton-Coupled Electron Transfer

3. Protein Radicals in Enzyme Catalysis

4. Proton-Coupled Electron Transfer and Redox-Active Tyrosines: Structure and Function of the Tyrosyl Radicals in Ribonucleotide Reductase and Photosystem II

5. Hole hopping through tyrosine/tryptophan chains protects proteins from oxidative damage

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