%0 Journal Article
%A Vlasov, A. V.
%A Kovalev, K. V.
%A Marx, S.-H.
%A Round, E. S.
%A Gushchin, I. Yu.
%A Polovinkin, V. A.
%A Tsoy, N. M.
%A Okhrimenko, I. S.
%A Borshchevskiy, V. I.
%A Büldt, G. D.
%A Ryzhykau, Yu. L.
%A Rogachev, A. V.
%A Chupin, V. V.
%A Kuklin, A. I.
%A Dencher, N. A.
%A Gordeliy, V. I.
%T Unusual features of the c-ring of F1FO ATP synthases
%J Scientific reports
%V 9
%N 1
%@ 2045-2322
%C [London]
%I Macmillan Publishers Limited, part of Springer Nature
%M FZJ-2019-05978
%P 18547
%D 2019
%X Membrane integral ATP synthases produce adenosine triphosphate, the universal “energy currency” of most organisms. However, important details of proton driven energy conversion are still unknown. We present the first high-resolution structure (2.3 Å) of the in meso crystallized c-ring of 14 subunits from spinach chloroplasts. The structure reveals molecular mechanisms of intersubunit contacts in the c14-ring, and it shows additional electron densities inside the c-ring which form circles parallel to the membrane plane. Similar densities were found in all known high-resolution structures of c-rings of F1FO ATP synthases from archaea and bacteria to eukaryotes. The densities might originate from isoprenoid quinones (such as coenzyme Q in mitochondria and plastoquinone in chloroplasts) that is consistent with differential UV-Vis spectroscopy of the c-ring samples, unusually large distance between polar/apolar interfaces inside the c-ring and universality among different species. Although additional experiments are required to verify this hypothesis, coenzyme Q and its analogues known as electron carriers of bioenergetic chains may be universal cofactors of ATP synthases, stabilizing c-ring and prevent ion leakage through it.
%F PUB:(DE-HGF)16
%9 Journal Article
%$ pmid:31811229
%U <Go to ISI:>//WOS:000501745000001
%R 10.1038/s41598-019-55092-z
%U https://juser.fz-juelich.de/record/866925