Mechanics of coupling proton movements toc-ring rotation in ATP synthase

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36 degrees step size of proton-driven c-ring rotation in FoF1-ATP synthase.

Synthesis of adenosine triphosphate ATP, the 'biological energy currency', is accomplished by F(o)F(1)-ATP synthase. In the plasma membrane of Escherichia coli, proton-driven rotation of a ring of 10 c subunits in the F(o) motor powers catalysis in the F(1) motor. Although F(1) uses 120 degrees stepping during ATP synthesis, models of F(o) predict either an incremental rotation of c subunits in...

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36 1 step size of proton - driven c - ring rotation in FoF 1 - ATP synthase

Synthesis of adenosine triphosphate ATP, the ‘biological energy currency’, is accomplished by FoF1-ATP synthase. In the plasma membrane of Escherichia coli, proton-driven rotation of a ring of 10 c subunits in the Fo motor powers catalysis in the F1 motor. Although F1 uses 1201 stepping during ATP synthesis, models of Fo predict either an incremental rotation of c subunits in 361 steps or large...

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step size of proton - driven c - ring rotation in FoF 1 - ATP synthase

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F(0) of ATP synthase is a rotary proton channel. Obligatory coupling of proton translocation with rotation of c-subunit ring.

Coupling of proton flow and rotation in the F(0) motor of ATP synthase was investigated using the thermophilic Bacillus PS3 enzyme expressed functionally in Escherichia coli cells. Cysteine residues introduced into the N-terminal regions of subunits b and c of ATP synthase (bL2C/cS2C) were readily oxidized by treating the expressing cells with CuCl(2) to form predominantly a b-c cross-link with...

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Obstruction of transmembrane helical movements in subunit a blocks proton pumping by F1Fo ATP synthase.

Subunit a plays a key role in promoting H(+) transport-coupled rotary motion of the subunit c ring in F1Fo ATP synthase. H(+) binding and release occur at Asp-61 in the middle of the second transmembrane helix (TMH) of Fo subunit c. H(+) are thought to reach cAsp61 via aqueous half-channels formed by TMHs 2-5 of subunit a. Movements of TMH4 and TMH5 have been proposed to facilitate protonation ...

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ژورنال

عنوان ژورنال: FEBS Letters

سال: 2003

ISSN: 0014-5793

DOI: 10.1016/s0014-5793(03)01101-3