Differential redox potential between the human cytosolic and mitochondrial branched-chain aminotransferase (hBCAT)

Coles, S. print, Hancock, J. T. print and Conway, M. E. print (2011) Differential redox potential between the human cytosolic and mitochondrial branched-chain aminotransferase (hBCAT). Acta Biochimica et Biophysica Sinica, 44 (2). pp. 172-176. ISSN 1745-7270

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Publisher's URL: http://dx.doi.org/10.1093/abbs/gmr103

Abstract

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
Uncontrolled Keywords:	glutathione, Nernst equation, redox potential, branched-chain aminotransferase
Faculty/Department:	Faculty of Health and Life Sciences > Department of Applied Sciences ~Pre-2012 Faculty Structure > Faculty of Health and Life Sciences > Department of Applied Sciences
ID Code:	16468
Deposited By:	C. print Foyle
Deposited On:	31 Jan 2012 10:29
Last Modified:	21 Feb 2013 09:26