Crystallographic studies of the binding of ligands to the dicarboxylate site of Complex II, and the identity of the ligand in the “oxaloacetate-inhibited” state-Reference-Cited by-同舟云学术

Crystallographic studies of the binding of ligands to the dicarboxylate site of Complex II, and the identity of the ligand in the “oxaloacetate-inhibited” state

Published:2006-09 Issue:9-10 Volume:1757 Page:1073-1083
ISSN:0005-2728
Container-title:Biochimica et Biophysica Acta (BBA) - Bioenergetics
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Bioenergetics

Author:

Huang Li-Shar,Shen John T.,Wang Andy C.,Berry Edward A.

Publisher

Elsevier BV

Subject

Cell Biology,Biochemistry,Biophysics

Reference22 articles.

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3. Studies on succinic dehydrogenase: IV. Activation of the beef heart enzyme;Kearney;J. Biol. Chem.,1957

4. Tightly bound oxalacetate and the activation of succinate dehydrogenase;Kearney;Biochem. Biophys. Res. Commun.,1972

5. Interaction of the membrane-bound succinate dehydrogenase with substrate and competitive inhibitors;Kotlyar;Biochim. Biophys. Acta,1984

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