caa a22 4500 46320834X CHVBK 20180405153132.0 cr unu---uuuuu 170326e20071201xx s 000 0 eng 10.1007/s10863-007-9110-1 doi (NATIONALLICENCE)springer-10.1007/s10863-007-9110-1 von Ballmoos Christoph Institute of Microbiology, ETH Zürich, Wolfgang-Pauli Strasse 10, CH-8093, Zürich, Switzerland aut Alternative proton binding mode in ATP synthases [Elektronische Daten] [Christoph von Ballmoos] ATP synthases are rotary engines which use the energy stored in a transmembrane electrochemical gradient of protons or sodium ions to catalyze the formation of ATP by ADP and inorganic phosphate. Current models predict that protonation/deprotonation of specific amino acids of the rotating c-ring, extracting protons from one side and delivering them to the other side of the membrane, are at the core of the proton translocation mechanism of these enzymes. In this minireview, an alternative proton binding mechanism is presented, considering hydronium ion coordination as proposed earlier. Biochemical data and structural considerations provide evidence for two different proton binding modes in the c-ring of H+-translocating ATP synthases. Recent investigations in several other proton translocating membrane proteins suggest, that hydronium ion coordination by proteins might display a general principle which was so far underestimated in ATP synthases. Springer Science+Business Media, LLC, 2007 ATP synthase nationallicence DCCD nationallicence c-ring nationallicence Hydronium ion nationallicence Proton translocation nationallicence Journal of Bioenergetics and Biomembranes Springer US; http://www.springer-ny.com 39/5-6(2007-12-01), 441-445 0145-479X 39:5-6<441 2007 39 10863 https://doi.org/10.1007/s10863-007-9110-1 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s10863-007-9110-1 text/html Onlinezugriff via DOI NATIONALLICENCE 100 1- von Ballmoos Christoph Institute of Microbiology, ETH Zürich, Wolfgang-Pauli Strasse 10, CH-8093, Zürich, Switzerland aut NATIONALLICENCE 773 0- Journal of Bioenergetics and Biomembranes Springer US; http://www.springer-ny.com 39/5-6(2007-12-01), 441-445 0145-479X 39:5-6<441 2007 39 10863 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer