Identification of potential inter-domain disulfides in three higher plant mitochondrial citrate synthases: Paradoxical differences in redox-sensitivity as compared with the animal enzyme

@article{Stevens2004IdentificationOP,
  title={Identification of potential inter-domain disulfides in three higher plant mitochondrial citrate synthases: Paradoxical differences in redox-sensitivity as compared with the animal enzyme},
  author={F. Stevens and Alex Dong Li and S. Salman Lateef and L. Anderson},
  journal={Photosynthesis Research},
  year={2004},
  volume={54},
  pages={185-197}
}
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… Expand
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Mass Spectrometric Evidence for an Alternate Disulfide Bond in Chloroplast Fructose Bisphosphatase
Thioredoxin Network in Plant Mitochondria: Cysteine S-Posttranslational Modifications and Stress Conditions
Regulation of the mitochondrial tricarboxylic acid cycle.
Interaction between photosynthesis and respiration in illuminated leaves.
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