Identification of potential inter-domain disulfides in three higher plant mitochondrial citrate synthases: Paradoxical differences in redox-sensitivity as compared with the animal enzyme |
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| Authors: | Stevens Fred J Dong Li Alex Salman Lateef S Anderson Louise E |
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| Institution: | (1) Center for Mechanistic Biology and Biotechnology, Argonne National Laboratory, Argonne, IL 60439-4833, USA;(2) Department of Biological Sciences, University of Illinois at Chicago, Chicago, IL 60607-7060, USA |
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| Abstract: | The mitochondrial citrate synthases (EC 4.1.3.7) of pummelo, potato and Arabidopsis are activated in crude extracts by dithiothreitol treatment and/or inactivated by the strong oxidizing agent diamide. Surprisingly, homology modeling reveals a potential disulfide involving two cysteine residues which are also present in the redox-insensitive model enzyme, pig heart citrate synthase. Energy minimization calculations suggest that differences in the charge distribution enhance disulfide bond formation in the plant mitochondrial citrate synthase and inhibit disulfide bond formation in the mammalian enzyme. |
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| Keywords: | redox-sensitive cysteines redox-regulation reductive activation regulatory disulfides |
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