Disease relevance of frdB

• We have examined the role of the quinone-binding (Q(P)) site of Escherichia coli succinate:ubiquinone oxidoreductase (succinate dehydrogenase) in heme reduction and reoxidation during enzyme turnover [1].
• Flavin fluorescence of succinate dehydrogenase (SucDH, complex II of the respiratory chain) of rat liver inner mitochondrial membranes correlated with the immunoreactivity of a representative anti-M7 myocarditis serum [2].

High impact information on frdB

• The Iron-Sulfur Clusters in Escherichia coli Succinate Dehydrogenase Direct Electron Flow [3].
• Succinate dehydrogenase is an indispensable enzyme involved in the Krebs cycle as well as energy coupling in the mitochondria and certain prokaryotes [3].
• These observations were made both with wild-type envelopes and with envelopes of a mutant which lacks the enzymes succinate dehydrogenase and fumarase, indicating that the switching-promoting activity of the analogues was not caused by their conversion to fumarate [4].
• Similar to succinate dehydrogenase, it is part of both the electron transfer chain and the citric acid cycle [5].
• During growth on glucose, but not on glycerol, activities of succinate dehydrogenase and of 2-oxoglutarate dehydrogenase were missing nearly completely [6].

Biological context of frdB

• Relieving transcriptional control of the sdhCDAB-b0725-sucABCD operon by chromosomal promoter exchange mutagenesis yielded a strain with increased specific activities of the TCA cycle enzymes succinate dehydrogenase, alpha-ketoglutarate dehydrogenase and succinyl-CoA synthetase, which are encoded by this operon [7].

References