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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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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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Stevens, F.J., Dong Li, A., Salman Lateef, S. et al. Identification of potential inter-domain disulfides in three higher plant mitochondrial citrate synthases: Paradoxical differences in redox-sensitivity as compared with the animal enzyme. Photosynthesis Research 54, 185–197 (1997). https://doi.org/10.1023/A:1005991423503

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