Cysteine Oxidation in Proteins: Structure, Biophysics, and Simulation

Cysteine side chains can exist in distinct oxidation states depending on the pH and redox potential of the environment, and cysteine oxidation plays important yet complex regulatory roles. Compared with the effects of post-translational modifications such as phosphorylation, the effects of oxidation...

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Bibliographic Details
Published in:Biochemistry (Easton) 2022-10, Vol.61 (20), p.2165-2176
Main Authors: Garrido Ruiz, Diego, Sandoval-Perez, Angelica, Rangarajan, Amith Vikram, Gunderson, Emma L., Jacobson, Matthew P.
Format: Article
Language:English
Subjects:
Biophysics
Cysteine - chemistry
Oxidation-Reduction
Proteins - chemistry
Sulfenic Acids
Sulfonic Acids
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Summary:Cysteine side chains can exist in distinct oxidation states depending on the pH and redox potential of the environment, and cysteine oxidation plays important yet complex regulatory roles. Compared with the effects of post-translational modifications such as phosphorylation, the effects of oxidation of cysteine to sulfenic, sulfinic, and sulfonic acid on protein structure and function remain relatively poorly characterized. We present an analysis of the role of cysteine reactivity as a regulatory factor in proteins, emphasizing the interplay between electrostatics and redox potential as key determinants of the resulting oxidation state. A review of current computational approaches suggests underdeveloped areas of research for studying cysteine reactivity through molecular simulations.
ISSN:0006-2960
1520-4995
DOI:10.1021/acs.biochem.2c00349