PMID: 2504145Jun 1, 1989Paper

New properties of Bacillus subtilis succinate dehydrogenase altered at the active site. The apparent active site thiol of succinate oxidoreductases is dispensable for succinate oxidation

The Biochemical Journal
L Hederstedt, L O Hedén

Abstract

Mammalian and Escherichia coli succinate dehydrogenase (SDH) and E. coli fumarate reductase apparently contain an essential cysteine residue at the active site, as shown by substrate-protectable inactivation with thiol-specific reagents. Bacillus subtilis SDH was found to be resistant to this type of reagent and contains an alanine residue at the amino acid position equivalent to the only invariant cysteine in the flavoprotein subunit of E. coli succinate oxidoreductases. Substitution of this alanine, at position 252 in the flavoprotein subunit of B. subtilis SDH, by cysteine resulted in an enzyme sensitive to thiol-specific reagents and protectable by substrate. Other biochemical properties of the redesigned SDH were similar to those of the wild-type enzyme. It is concluded that the invariant cysteine in the flavoprotein of E. coli succinate oxidoreductases corresponds to the active site thiol. However, this cysteine is most likely not essential for succinate oxidation and seemingly lacks an assignable specific function. An invariant arginine in juxtaposition to Ala-252 in the flavoprotein of B. subtilis SDH, and to the invariant cysteine in the E. coli homologous enzymes, is probably essential for substrate binding.

Citations

Sep 22, 2012·Biochimica Et Biophysica Acta·T M Iverson
Feb 14, 2009·Progress in Molecular Biology and Translational Science·David H Bechhofer
Aug 27, 2005·Heredity·R Gonzàlez-Duarte, R Albalat
Apr 1, 1991·Journal of Bioenergetics and Biomembranes·D JayJ L Boldu
Feb 3, 2011·FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology·Virginie GuilletPascal Reynier
Oct 24, 1998·The International Journal of Biochemistry & Cell Biology·Y YangH M Zhou
Jun 13, 1997·Biochimica Et Biophysica Acta·C Hägerhäll
Mar 29, 1994·Biochimica Et Biophysica Acta·A A MorrisM A Birch-Machin

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