PMID: 12694200Apr 16, 2003

Complex II from phototrophic purple bacterium Rhodoferax fermentans displays rhodoquinol-fumarate reductase activity

European Journal of Biochemistry
Hiroko MiyaderaKiyoshi Kita

Abstract

It has long been accepted that bacterial quinol-fumarate reductase (QFR) generally uses a low-redox-potential naphthoquinone, menaquinone (MK), as the electron donor, whereas mitochondrial QFR from facultative and anaerobic eukaryotes uses a low-redox-potential benzoquinone, rhodoquinone (RQ), as the substrate. In the present study, we purified novel complex II from the RQ-containing phototrophic purple bacterium, Rhodoferax fermentans that exhibited high rhodoquinol-fumarate reductase activity in addition to succinate-ubiquinone reductase activity. SDS/PAGE indicated that the purified R. fermentans complex II comprises four subunits of 64.0, 28.6, 18.7 and 17.5 kDa and contains 1.3 nmol heme per mg protein. Phylogenetic analysis and comparison of the deduced amino acid sequences of R. fermentans complex II with pro/eukaryotic complex II indicate that the structure and the evolutional origins of R. fermentans complex II are closer to bacterial SQR than to mitochondrial rhodoquinol-fumarate reductase. The results strongly indicate that R. fermentans complex II and mitochondrial QFR might have evolved independently, although they both utilize RQ for fumarate reduction.

References

Nov 13, 2003·Proceedings of the National Academy of Sciences of the United States of America·James RegeimbalJames C A Bardwell
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Citations

Jan 15, 1990·Biochemical and Biophysical Research Communications·K KitaM Kasahara
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Related Concepts

Rhodoquinone
Conserved Sequence
Benzoquinone
Succinate Dehydrogenase
Oxidase
Chromatography, DEAE-Cellulose
Fumarate Reductase Activity
Homologous Sequences, Amino Acid
Phylogeny
Fumarate

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