New substrates, new inhibitors and the stereochemistry of the succinic dehydrogenase system

Oscar Gawron, Andrew J. Glaid, Thomas P Fondy, Mary M. Bechtold

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Abstract

L-Chlorosuccinate and L-methylsuccinate are substrates for succinic dehydrogenase, chlorofumarate and mesaconate being produced, respectively, by enzyme catalyzed dehydrogenation. The respective enantiomorphs, D-chlorosuccinate and L-methylsuccinate, are inhibitors of the enzyme and the stereospecificity of succinic dehydrogenase is thereby established. The enzyme exhibits a trans stereoselectivity, dehydrogenating erythro-3-deuterio-L-chlorosuccinate to 3-deuterio-chlorofumarate. From the above facts the stereochemistry of the behavior of succinic acid in the enzyme substrate complex is deduced. K M values and K I values for the new substrates under specified conditions are presented and E 0′ values at pH 7.3, 34° for the chlorosuccinate/chlorofumarate and methylsuccinate/mesaconate half-cells are 0.0462 volt and -0.0018 volt, respectively.

Original languageEnglish (US)
Pages (from-to)3877-3882
Number of pages6
JournalJournal of the American Chemical Society
Volume84
Issue number20
StatePublished - 1952
Externally publishedYes

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ASJC Scopus subject areas

  • Chemistry(all)

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