TY  - JOUR
AU  - Vlasov, A. V.
AU  - Kovalev, K. V.
AU  - Marx, S.-H.
AU  - Round, E. S.
AU  - Gushchin, I. Yu.
AU  - Polovinkin, V. A.
AU  - Tsoy, N. M.
AU  - Okhrimenko, I. S.
AU  - Borshchevskiy, V. I.
AU  - Büldt, G. D.
AU  - Ryzhykau, Yu. L.
AU  - Rogachev, A. V.
AU  - Chupin, V. V.
AU  - Kuklin, A. I.
AU  - Dencher, N. A.
AU  - Gordeliy, V. I.
TI  - Unusual features of the c-ring of F1FO ATP synthases
JO  - Scientific reports
VL  - 9
IS  - 1
SN  - 2045-2322
CY  - [London]
PB  - Macmillan Publishers Limited, part of Springer Nature
M1  - FZJ-2019-05978
SP  - 18547
PY  - 2019
AB  - 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.
LB  - PUB:(DE-HGF)16
C6  - pmid:31811229
UR  - <Go to ISI:>//WOS:000501745000001
DO  - DOI:10.1038/s41598-019-55092-z
UR  - https://juser.fz-juelich.de/record/866925
ER  -