HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Ackrell, B. A. Articles by Edmondson, D. Search for Related Content PubMed PubMed Citation Articles by Ackrell, B. A. Articles by Edmondson, D. Social Bookmarking                      What's this?

JBC, Vol. 250, Issue 18, 7114-7119, Sep, 1975

Mechanism of the reductive activation of succinate dehydrogenase

B. A. Ackrell, E. B. Kearney and D. Edmondson

When succinate dehydrogenase contains oxalacetate in firmly bound form, activity cannof the enzyme results in dissociation of oxalacetate and activation of the enzyme. The course of reductive titrations appears the same whether or not the enzyme contains oxalacetate, and complete reduction as monitored by bleaching of chromophoric groups requires the incorporation of 6 to 7 reducing equivalents in either case. The stoichiometry is that expected from the non-heme iron and flavin content of the enzyme. Activation of the enzyme during reductive titrations occurs predominantly with the incorporation of the second pair of electrons, while determination of activation levels at various poised potentials shows that the group involved is reduced with the uptake of 2 H+ and 2 e-. These characteristics are consistent with titration of the flavin moiety rather than non-heme iron groups. Thus it appears that activation is concurrent with the reduction of flavin to the hydroquinone form. From the measured half-reduction potential for activation, that of the flavin in an oxalacetate-free enzyme has been estimated at -90 to -60 mv at pH 7.
CiteULike    Complore    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this?

This article has been cited by other articles:

				E. Maklashina, T. M. Iverson, Y. Sher, V. Kotlyar, J. Andrell, O. Mirza, J. M. Hudson, F. A. Armstrong, R. A. Rothery, J. H. Weiner, et al. Fumarate Reductase and Succinate Oxidase Activity of Escherichia coli Complex II Homologs Are Perturbed Differently by Mutation of the Flavin Binding Domain J. Biol. Chem., April 21, 2006; 281(16): 11357 - 11365. [Abstract] [Full Text] [PDF]

				L.-s. Huang, G. Sun, D. Cobessi, A. C. Wang, J. T. Shen, E. Y. Tung, V. E. Anderson, and E. A. Berry 3-Nitropropionic Acid Is a Suicide Inhibitor of Mitochondrial Respiration That, upon Oxidation by Complex II, Forms a Covalent Adduct with a Catalytic Base Arginine in the Active Site of the Enzyme J. Biol. Chem., March 3, 2006; 281(9): 5965 - 5972. [Abstract] [Full Text] [PDF]

				C. Affourtit, K. Krab, G. R. Leach, D. G. Whitehouse, and A. L. Moore New Insights into the Regulation of Plant Succinate Dehydrogenase. ON THE ROLE OF THE PROTONMOTIVE FORCE J. Biol. Chem., August 24, 2001; 276(35): 32567 - 32574. [Abstract] [Full Text] [PDF]