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| Boxma, B.; Ricard, G.; van Hoek, A. H.; Severing, E.; Moon-van der Staay, S.Y.; van der Staay, G.W.M.; van Alen, T.A.; de Graaf, R.M.; Cremers, G.; Kwantes, M.; McEwan, N.R.; Newbold, C.J.; Jouany, J.P.; Michalowski, T.; Pristas, P.; Huynen, M.A.; Hackstein, J.H.P.. |
| Background: The hydrogenosomes of the anaerobic ciliate Nyctotherus ovalis show how mitochondria can evolve into hydrogenosomes because they possess a mitochondrial genome and parts of an electron-transport chain on the one hand, and a hydrogenase on the other hand. The hydrogenase permits direct reoxidation of NADH because it consists of a [ FeFe] hydrogenase module that is fused to two modules, which are homologous to the 24 kDa and the 51 kDa subunits of a mitochondrial complex I.Results: The [ FeFe] hydrogenase belongs to a clade of hydrogenases that are different from well-known eukaryotic hydrogenases. The 24 kDa and the 51 kDa modules are most closely related to homologous modules that function in bacterial [ NiFe] hydrogenases. Paralogous,... |
| Tipo: Journal Article |
Palavras-chave: MITOCHONDRIE; CILIE; HYDROGENASE MULTIPLE SEQUENCE ALIGNMENT; COMPLEX-I; PHYLOGENETIC ANALYSIS; EUKARYOTIC EVOLUTION; IRON HYDROGENASES; LIFE-STYLE; HYDROGENOSOMES; MITOCHONDRIA; PROTEIN; MODELS. |
| Ano: 2007 |
URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD2008786cfe28&uri=/notices/prodinra1/2009/10/ |
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