PMID: 9639600Jun 26, 1998Paper

Carboxin resistance in Paracoccus denitrificans conferred by a mutation in the membrane-anchor domain of succinate:quinone reductase

Archives of Microbiology
M MatssonL Hederstedt

Abstract

Succinate:quinone reductase is a membrane-bound enzyme of the citric acid cycle and the respiratory chain. Carboxin is a potent inhibitor of the enzyme of certain organisms. The bacterium Paracoccus denitrificans was found to be sensitive to carboxin in vivo, and mutants that grow in the presence of 3'-methyl carboxin were isolated. Membranes of the mutants showed resistant succinate:quinone reductase activity. The mutation conferring carboxin resistance was identified in four mutants. They contained the same missense mutation in the sdhD gene, which encodes one of two membrane-intrinsic polypeptides of the succinate:quinone reductase complex. The mutation causes an Asp to Gly replacement at position 89 in the SdhD polypeptide. P. denitrificans strains that overproduced wild-type or mutant enzymes were constructed. Enzymic properties of the purified enzymes were analyzed. The apparent Km for quinone (DPB) and the sensitivity to thenoyltrifluoroacetone was normal for the carboxin-resistant enzyme, but the succinate:quinone reductase activity was lower than for the wild-type enzyme. Mutations conferring carboxin resistance indicate the region on the enzyme where the inhibitor binds. A previously reported His to Leu replacement cl...Continue Reading

Citations

Jan 8, 2003·Proceedings of the National Academy of Sciences of the United States of America·Hiroko MiyaderaSatoshi Omura
Apr 17, 2003·Neonatal Network : NN·William L Diehl-Jones, Debbie Fraser Askin
Oct 1, 2007·Plant Disease·Herve F Avenot, Themis J Michailides
Jun 6, 2021·Biochimica Et Biophysica Acta. Proteins and Proteomics·Li-Shar HuangEdward A Berry

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