New Substrates, New Inhibitors and the Stereochemistry of the Succinic Dehydrogenase System

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

doi:10.1021/ja00879a017

New Substrates, New Inhibitors and the Stereochemistry of the Succinic Dehydrogenase System

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

Research output: Contribution to journal › Article › peer-review

12 Scopus citations

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-chlorosuccmate to 3-deuterio-chloro chlorofumarate. From the above facts the stereochemistry of the behavior of succinic acid in the enzyme substrate complex is deduced. K_M values and K₁ values for the new substrates under specified conditions are presented and E₀' 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 language	English (US)
Pages (from-to)	3877-3882
Number of pages	6
Journal	Journal of the American Chemical Society
Volume	84
Issue number	20
DOIs	https://doi.org/10.1021/ja00879a017
State	Published - 1962
Externally published	Yes

ASJC Scopus subject areas

Catalysis
General Chemistry
Biochemistry
Colloid and Surface Chemistry

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title = "New Substrates, New Inhibitors and the Stereochemistry of the Succinic Dehydrogenase System",

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-chlorosuccmate to 3-deuterio-chloro chlorofumarate. From the above facts the stereochemistry of the behavior of succinic acid in the enzyme substrate complex is deduced. KM values and K1 values for the new substrates under specified conditions are presented and E0' values at pH 7.3, 34° for the chlorosuccinate/chlorofumarate and methylsuccinate/mesaconate half-cells are 0.0462 volt and -0.0018 volt, respectively.",

author = "Oscar Gawron and Glaid, {Andrew J.} and Fondy, {Thomas P.} and Bechtold, {Mary M.}",

year = "1962",

doi = "10.1021/ja00879a017",

language = "English (US)",

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pages = "3877--3882",

journal = "Journal of the American Chemical Society",

issn = "0002-7863",

publisher = "American Chemical Society",

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TY - JOUR

T1 - New Substrates, New Inhibitors and the Stereochemistry of the Succinic Dehydrogenase System

AU - Gawron, Oscar

AU - Glaid, Andrew J.

AU - Fondy, Thomas P.

AU - Bechtold, Mary M.

PY - 1962

Y1 - 1962

N2 - 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-chlorosuccmate to 3-deuterio-chloro chlorofumarate. From the above facts the stereochemistry of the behavior of succinic acid in the enzyme substrate complex is deduced. KM values and K1 values for the new substrates under specified conditions are presented and E0' values at pH 7.3, 34° for the chlorosuccinate/chlorofumarate and methylsuccinate/mesaconate half-cells are 0.0462 volt and -0.0018 volt, respectively.

AB - 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-chlorosuccmate to 3-deuterio-chloro chlorofumarate. From the above facts the stereochemistry of the behavior of succinic acid in the enzyme substrate complex is deduced. KM values and K1 values for the new substrates under specified conditions are presented and E0' values at pH 7.3, 34° for the chlorosuccinate/chlorofumarate and methylsuccinate/mesaconate half-cells are 0.0462 volt and -0.0018 volt, respectively.

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DO - 10.1021/ja00879a017

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JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

IS - 20

ER -

New Substrates, New Inhibitors and the Stereochemistry of the Succinic Dehydrogenase System

Abstract

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