Literature DB >> 8951088

The coupling of the relative movement of the a and c subunits of the F0 to the conformational changes in the F1-ATPase.

S M Howitt1, A J Rodgers, L P Hatch, F Gibson, G B Cox.   

Abstract

F0F1-ATPase structural information gained from X-ray crystallography and electron microscopy has activated interest in a rotational mechanism for the F0F1-ATPase. Because of the subunit stoichiometry and the involvement of both a- and c-subunits in the mechanism of proton movement, it is argued that relative movement must occur between the subunits. Various options for the arrangement and structure of the subunits involved are discussed and a mechanism proposed.

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Year:  1996        PMID： 8951088     DOI： 10.1007/bf02113983

Source DB:  PubMed          Journal:  J Bioenerg Biomembr        ISSN： 0145-479X            Impact factor:   2.945


  49 in total

1.  The essential carboxyl group in subunit c of the F1F0 ATP synthase can be moved and H(+)-translocating function retained.

Authors:  M J Miller; M Oldenburg; R H Fillingame
Journal:  Proc Natl Acad Sci U S A       Date:  1990-07       Impact factor: 11.205

2.  Subunit interactions within the chloroplast ATP synthase (CF0-CF1) as deduced by specific depletion of CF0 polypeptides.

Authors:  Y Feng; R E McCarty
Journal:  J Biol Chem       Date:  1990-07-25       Impact factor: 5.157

3.  Genetic evidence for interaction between the a and b subunits of the F0 portion of the Escherichia coli proton translocating ATPase.

Authors:  C A Kumamoto; R D Simoni
Journal:  J Biol Chem       Date:  1986-08-05       Impact factor: 5.157

4.  Hypothesis. The mechanism of ATP synthase. Conformational change by rotation of the beta-subunit.

Authors:  G B Cox; D A Jans; A L Fimmel; F Gibson; L Hatch
Journal:  Biochim Biophys Acta       Date:  1984-12-17

5.  Specific binding of coupling factor 1 lacking the delta and epsilon subunits to thylakoids.

Authors:  W J Patrie; R E McCarty
Journal:  J Biol Chem       Date:  1984-09-10       Impact factor: 5.157

6.  Cross-linking and labeling of the Escherichia coli F1F0-ATP synthase reveal a compact hydrophilic portion of F0 close to an F1 catalytic subunit.

Authors:  J P Aris; R D Simoni
Journal:  J Biol Chem       Date:  1983-12-10       Impact factor: 5.157

Review 7.  The mechanism and regulation of ATP synthesis by F1-ATPases.

Authors:  R L Cross
Journal:  Annu Rev Biochem       Date:  1981       Impact factor: 23.643

8.  Model for the structure of bacteriorhodopsin based on high-resolution electron cryo-microscopy.

Authors:  R Henderson; J M Baldwin; T A Ceska; F Zemlin; E Beckmann; K H Downing
Journal:  J Mol Biol       Date:  1990-06-20       Impact factor: 5.469

9.  Topology, organization, and function of the psi subunit in the F0 sector of the H+-ATPase of Escherichia coli.

Authors:  J Hermolin; J Gallant; R H Fillingame
Journal:  J Biol Chem       Date:  1983-12-10       Impact factor: 5.157

10.  H+-ATPase activity of Escherichia coli F1F0 is blocked after reaction of dicyclohexylcarbodiimide with a single proteolipid (subunit c) of the F0 complex.

Authors:  J Hermolin; R H Fillingame
Journal:  J Biol Chem       Date:  1989-03-05       Impact factor: 5.157
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  5 in total

1.  Energy-driven subunit rotation at the interface between subunit a and the c oligomer in the F(O) sector of Escherichia coli ATP synthase.

Authors:  M L Hutcheon; T M Duncan; H Ngai; R L Cross
Journal:  Proc Natl Acad Sci U S A       Date:  2001-07-03       Impact factor: 11.205

2.  Subunit rotation in Escherichia coli FoF1-ATP synthase during oxidative phosphorylation.

Authors:  Y Zhou; T M Duncan; R L Cross
Journal:  Proc Natl Acad Sci U S A       Date:  1997-09-30       Impact factor: 11.205

Review 3.  Frontiers in ATP synthase research: understanding the relationship between subunit movements and ATP synthesis.

Authors:  P L Pedersen
Journal:  J Bioenerg Biomembr       Date:  1996-10       Impact factor: 2.945

4.  Interacting helical faces of subunits a and c in the F1Fo ATP synthase of Escherichia coli defined by disulfide cross-linking.

Authors:  W Jiang; R H Fillingame
Journal:  Proc Natl Acad Sci U S A       Date:  1998-06-09       Impact factor: 11.205

5.  Inefficient coupling between proton transport and ATP synthesis may be the pathogenic mechanism for NARP and Leigh syndrome resulting from the T8993G mutation in mtDNA.

Authors:  Gianluca Sgarbi; Alessandra Baracca; Giorgio Lenaz; Lucia M Valentino; Valerio Carelli; Giancarlo Solaini
Journal:  Biochem J       Date:  2006-05-01       Impact factor: 3.857
  5 in total

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