University of Worcester Worcester Research and Publications

Differential Redox Potential Between the Human Cytosolic and Mitochondrial Branched-chain Aminotransferase

Coles, Steven ORCID:, Hancock, J.T. and Conway, M.E. (2012) Differential Redox Potential Between the Human Cytosolic and Mitochondrial Branched-chain Aminotransferase. Acta Biochimica et Biophysica Sinica, 44 (2). pp. 172-176. ISSN Print: 1672-9145 Online: 1745-7270

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The human branched-chain aminotransferase (hBCAT) isoenzymes are CXXC motif redox sensitive homodimers central to glutamate metabolism in the central nervous system. These proteins respond differently to oxidation by H2O2, NO, and S-glutathionylation, suggesting that the redox potential is distinct between isoenzymes. Using various reduced to oxidized glutathione ratios (GSH:GSSG) to alter the redox environment, we demonstrate that hBCATc (cytosolic) has an overall redox potential that is 30 mV lower than hBCATm (mitochondrial). Furthermore, the CXXC motif of hBCATc was estimated to be 80 mV lower, suggesting that hBCATm is more oxidizing in nature. Western blot analysis revealed close correlations between hBCAT S-glutathionylation and the redox status of the assay environment, offering the hBCAT isoenzymes as novel biomarkers for cytosolic and mitochondrial oxidative stress.

Item Type: Article
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Uncontrolled Discrete Keywords: glutathione, Nernst equation, redox potential, branched-chain aminotransferase
Subjects: Q Science > QD Chemistry
Divisions: College of Health, Life and Environmental Sciences > School of Science and the Environment
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Depositing User: Steven Coles
Date Deposited: 15 Sep 2017 08:38
Last Modified: 17 Jun 2020 17:19

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