Schink and Pfennig 1983
Propionigenium modestum is a gram-negative, strictly anaerobic organism. It is rod-shaped and around 0.5-0.6 x 0.5-2.0μm in size. It is important in the elucidation of mechanism of ATP synthase.
The word propionigenium comes from the Latin word acidum propionicum meaning propionic acid and genre is Latin for make or produce. Modestus comes from the Latin word meaning modest, referring to an extremely modest type of metabolism.
Propionigenium modestum's current classification is Bacteria, Fusobacteria, Fusobacteria, Fusobacteriales, Fusobacteriaceae, Propionigenium, Modestum. Propionigenium modestum and Propionigenium maris, currently, are the only two species belonging to the genus Propionigenium. They both inhabit marine environments. P. modestum was found to be more closely related to Ilyobacter insuetus than it is to P. maris. P. modestum and I. insuetus share 97±4 - 98±5% 16S rRNA (ribosomal Ribonucleic Acid), while P. modestum and P. maris only share 96±5 - 96±8%. Only two species in the family Fusobacteriaceae have had their entire genomes sequenced; one being llyobacter polytropus.
P. modestum was isolated by Bernhard Schink and Norbert Pfenning in 1982. It was first isolated from black, anaerobic mud from Canale Grande in Venice, Italy, and was later isolated from human saliva. The original isolation of P. modestum was obtained through a succinate media, which was used as the primary source of energy. It was reported that for every mol of succinate that was fermented by P. modesetum, there was between 2.1 and 2.4 grams of cell dry weight isolated form the media.
P. modestum is a non-sporing and non-motile bacteria. Its growth optimum is pH of 7.1-7.7 and a temperature of 33 °C. The G+C content is 33.9%. It utilizes succinate, fumarate, malate, aspartate, oxaloacetate, and pyruvate for growth and fermentes them to propionate, (acetate), and Carbon Dioxide (CO2). This organism grows optimally in fresh and saltwater, as well as human saliva under anaerobic conditions. Propionigenium modestum converts succinate (as well as other energy sources) to propionate to generate energy. The conversion has a small free energy change so there is no electron-transport chain or substrate-linked phosphorylation.
The discovery of the ATPase in P. modestum is important because it demonstrated that the chemiosmosis theory as proposed by Peter D. Mitchell was incorrect. Mitchell proposed that the H+ was consumed in the synthesis of ATP by reacting directly with O2 converting it to H2O while producing ATP from ADP. Instead the F-type ATPase of P. modestum uses only Na+ to drive the reaction, demonstrating the production of H2O from O2 during the synthesis of ATP does not consume the H+ used by all other known F-type ATPases. Thus demonstrating that it is the H+ gradient that drives ATP synthase.
The ATPase of P. modestum acts about 6 times higher than bacterial membranes, at 6.6 units/mg of protein. The ATPase is composed of subunits a,b, and c. It has been found that subunit c is extremely stable and does not dissociate during SDS (Sodium Dodecyl Sulfate) gel electrophoresis until 120 °C.
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- Schink, Bernhard (2006). "The Genus Propionigenium". Prokaryotes. 7: 955–959.
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- Brune, Andreas; Ludwig, Wolfgang; Kaim, Georg; Schink, Bernhard; Evers, Stephan (2002). "Ilyobacter insuetus Sp. Nov., a Fermentative Bacterium Specialized in the Degradation of Hydroaromatic Compounds". International Journal of Systematic and Evolutionary Microbiology. 52.2: 429–432. doi:10.1099/00207713-52-2-429.
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Werner Laubinger and Peter Dimroth
- Kaim, Georg (2001). "The Na -translocating F1F0 ATP Synthase of Propionigenium Modestum: Mechanochemical Insights into the F0 Motor That Drives ATP Synthesis". Bioenergetics. 1505: 94–107. doi:10.1016/s0005-2728(00)00280-2.
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mitchell febs lett 43 189
- P. Dimroth (July 1992). "The ATPases of Propionigenium modestum and Bacillus alcalophilus. Strategies for ATP synthesis under low energy conditions". Biochimica et Biophysica Acta. 1101 (2): 236–239. doi:10.1016/0005-2728(92)90234-s. PMID 1385980.
- Laubinger, Werner; Dimroth, Peter (1989). "The sodium ion translocating adenosine triphosphatase of Propionigenium modestum pumps protons at low sodium ion concentrations". Biochemistry. 28 (18): 7194–7198. doi:10.1021/bi00444a010. ISSN 0006-2960.
- Dimroth, P.; Wang, H.; Grabe, M.; Oster, G. (1999). "Energy transduction in the sodium F-ATPase of Propionigenium modestum". Proceedings of the National Academy of Sciences. 96 (9): 4924–4929. doi:10.1073/pnas.96.9.4924. ISSN 0027-8424. PMC 21793.