IDENTIFICATION OF POTENTIAL INTER-DOMAIN DISULFIDES IN 3 HIGHER-PLANTMITOCHONDRIAL CITRATE SYNTHASES - PARADOXICAL DIFFERENCES IN REDOX-SENSITIVITY AS COMPARED WITH THE ANIMAL ENZYME

Authors
STEVENS FJ LI AD LATEEF SS ANDERSON LE
Citation
Fj. Stevens et al., IDENTIFICATION OF POTENTIAL INTER-DOMAIN DISULFIDES IN 3 HIGHER-PLANTMITOCHONDRIAL CITRATE SYNTHASES - PARADOXICAL DIFFERENCES IN REDOX-SENSITIVITY AS COMPARED WITH THE ANIMAL ENZYME, Photosynthesis research, 54(3), 1997, pp. 185-197
Citations number
30
Journal title
Photosynthesis research → ACNP
ISSN journal
01668595
Volume
54
Issue
3
Year of publication
1997
Pages
185 - 197
Database
ISI
SICI code
0166-8595(1997)54:3<185:IOPIDI>2.0.ZU;2-1
Abstract
The mitochondrial citrate synthases (EC 4.1.3.7) of pummelo, potato an d Arabidopsis are activated in crude extracts by dithiothreitol treatm ent and/or inactivated by the strong oxidizing agent diamide. Surprisi ngly, homology modeling reveals a potential disulfide involving two cy steine residues which are also present in the redox-insensitive model enzyme, pig heart citrate synthase. Energy minimization calculations s uggest that differences in the charge distribution enhance disulfide b ond formation in the plant mitochondrial citrate synthase and inhibit disulfide bond formation in the mammalian enzyme.