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Microbe Profile: Paracoccus denitrificans - a versatile model
This article is part of the Microbe Profiles collection.
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Stephen Spiro1 and David J. Richardson2
Graphical Abstract
Electron transfer pathways of Paracoccus denitrificans. Enzymes and electron carriers are coloured according to location: orange (membrane bound) and blue (periplasmic). Electron transfer reactions are coloured black, blue and orange to indicate that they occur predominantly in the presence or absence of oxygen, or both, respectively. Note that pseudoazurin is expressed under anaerobic growth conditions and donates electrons to the nitrite, NO and N2O reductases. Abbreviations: ETF, electron transfer flavoprotein; NAR, membrane-bound nitrate reductase; NAP, periplasmic nitrate reductase; MDH, methanol dehydrogenase; MaDH, methylamine dehydrogenase; AMI, amicyanin; SOX, sulphur oxidation system; ASD, aldose sugar dehydrogenase; UQ, ubiquinone; UQH2, ubiquinol.
Abstract
Paracoccus denitrificans is a metabolically versatile alphaproteobacterium first isolated in 1910 by Martinus Beijerinck. Similarities between the aerobic respiratory chain and membrane composition of P. denitrificans and those of eukaryotic mitochondria have stimulated the use of P. denitrificans as a model for oxidative phosphorylation. The organism has also been used extensively as a model for studies of denitrification, cytochrome c biogenesis, lithotrophy using thiosulphate as a source of energy, methylotrophy, and carbon metabolism more broadly. Through the application of structural biology and modern genome-based approaches, work on P. denitrificans continues to make significant contributions across multiple areas of microbiology.
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Keyword(s):
denitrification
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methylotrophy
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oxidative phosphorylation
and
Paracoccus denitrificans