Journal Article FZJ-2019-05978

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Unusual features of the c-ring of F1FO ATP synthases

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2019
Macmillan Publishers Limited, part of Springer Nature [London]

Scientific reports 9(1), 18547 () [10.1038/s41598-019-55092-z]

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Abstract: 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.

Classification:

Contributing Institute(s):
  1. Strukturbiochemie (ICS-6)
Research Program(s):
  1. 552 - Engineering Cell Function (POF3-552) (POF3-552)

Appears in the scientific report 2019
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Workflowsammlungen > Öffentliche Einträge
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ICS > ICS-6
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Open Access

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