caa a22 4500 445821280 CHVBK 20180317145245.0 cr unu---uuuuu 170323e20110601xx s 000 0 eng 10.1007/s00239-011-9447-2 doi (NATIONALLICENCE)springer-10.1007/s00239-011-9447-2 The Evolution of Respiratory Chain Complex I from a Smaller Last Common Ancestor Consisting of 11 Protein Subunits [Elektronische Daten] [Vamsi Moparthi, Cecilia Hägerhäll] The NADH:quinone oxidoreductase (complex I) has evolved from a combination of smaller functional building blocks. Chloroplasts and cyanobacteria contain a complex I-like enzyme having only 11 subunits. This enzyme lacks the N-module which harbors the NADH binding site and the flavin and iron-sulfur cluster prosthetic groups. A complex I-homologous enzyme found in some archaea contains an F420 dehydrogenase subunit denoted as FpoF rather than the N-module. In the present study, all currently available whole genome sequences were used to survey the occurrence of the different types of complex I in the different kingdoms of life. Notably, the 11-subunit version of complex I was found to be widely distributed, both in the archaeal and in the eubacterial kingdoms, whereas the 14-subunit classical complex I was found only in certain eubacterial phyla. The FpoF-containing complex I was present in Euryarchaeota but not in Crenarchaeota, which contained the 11-subunit complex I. The 11-subunit enzymes showed a primary sequence variability as great or greater than the full-size 14-subunit complex I, but differed distinctly from the membrane-bound hydrogenases. We conclude that this type of compact 11-subunit complex I is ancestral to all present-day complex I enzymes. No designated partner protein, acting as an electron delivery device, could be found for the compact version of complex I. We propose that the primordial complex I, and many of the present-day 11-subunit versions of it, operate without a designated partner protein but are capable of interaction with several different electron donor or acceptor proteins. The Author(s), 2011 NADH:quinone oxidoreductase nationallicence NiFe-hydrogenase nationallicence Formate:hydrogen lyase nationallicence Protein phylogeny nationallicence Functional modules nationallicence Antiporter nationallicence Moparthi Vamsi Department of Biochemistry and Structural Biology, Center for Molecular Protein Science, Lund University, Box 124, 22100, Lund, Sweden aut Hägerhäll Cecilia Department of Biochemistry and Structural Biology, Center for Molecular Protein Science, Lund University, Box 124, 22100, Lund, Sweden aut Journal of Molecular Evolution Springer-Verlag 72/5-6(2011-06-01), 484-497 0022-2844 72:5-6<484 2011 72 239 https://doi.org/10.1007/s00239-011-9447-2 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s00239-011-9447-2 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Moparthi Vamsi Department of Biochemistry and Structural Biology, Center for Molecular Protein Science, Lund University, Box 124, 22100, Lund, Sweden aut NATIONALLICENCE 700 1- Hägerhäll Cecilia Department of Biochemistry and Structural Biology, Center for Molecular Protein Science, Lund University, Box 124, 22100, Lund, Sweden aut NATIONALLICENCE 773 0- Journal of Molecular Evolution Springer-Verlag 72/5-6(2011-06-01), 484-497 0022-2844 72:5-6<484 2011 72 239 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer