Literature DB >> 15254387

Notes on the mechanism of ATP synthesis.

M A Bianchet1, P L Pedersen, L M Amzel.   

Abstract

The most commonly quoted mechanism of the coupling between the electrochemical proton gradient and the formation of ATP from ADP and P(i) assumes that all states of the F(1) portion of the ATP synthase have beta subunits in "tight," "loose," and "open" conformations. Models based on this assumption are inconsistent with some of the available experimental evidence. A mechanism that includes an additional beta subunit conformation, "closed," observed in the rat liver structure overcomes these difficulties.

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Year:  2000        PMID： 15254387     DOI： 10.1023/a:1005673209883

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


  11 in total

1.  Structural features of the gamma subunit of the Escherichia coli F(1) ATPase revealed by a 4.4-A resolution map obtained by x-ray crystallography.

Authors:  A C Hausrath; G Grüber; B W Matthews; R A Capaldi
Journal:  Proc Natl Acad Sci U S A       Date:  1999-11-23       Impact factor: 11.205

2.  The 2.8-A structure of rat liver F1-ATPase: configuration of a critical intermediate in ATP synthesis/hydrolysis.

Authors:  M A Bianchet; J Hullihen; P L Pedersen; L M Amzel
Journal:  Proc Natl Acad Sci U S A       Date:  1998-09-15       Impact factor: 11.205

3.  F1-ATPase is a highly efficient molecular motor that rotates with discrete 120 degree steps.

Authors:  R Yasuda; H Noji; K Kinosita; M Yoshida
Journal:  Cell       Date:  1998-06-26       Impact factor: 41.582

4.  Direct observation of the rotation of F1-ATPase.

Authors:  H Noji; R Yasuda; M Yoshida; K Kinosita
Journal:  Nature       Date:  1997-03-20       Impact factor: 49.962

Review 5.  The ATP synthase--a splendid molecular machine.

Authors:  P D Boyer
Journal:  Annu Rev Biochem       Date:  1997       Impact factor: 23.643

6.  Specific placement of tryptophan in the catalytic sites of Escherichia coli F1-ATPase provides a direct probe of nucleotide binding: maximal ATP hydrolysis occurs with three sites occupied.

Authors:  J Weber; S Wilke-Mounts; R S Lee; E Grell; A E Senior
Journal:  J Biol Chem       Date:  1993-09-25       Impact factor: 5.157

7.  Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria.

Authors:  J P Abrahams; A G Leslie; R Lutter; J E Walker
Journal:  Nature       Date:  1994-08-25       Impact factor: 49.962

8.  Nucleotide occupancy of F1-ATPase catalytic sites under crystallization conditions.

Authors:  S Löbau; J Weber; A E Senior
Journal:  FEBS Lett       Date:  1997-03-03       Impact factor: 4.124

9.  Rotation of subunits during catalysis by Escherichia coli F1-ATPase.

Authors:  T M Duncan; V V Bulygin; Y Zhou; M L Hutcheon; R L Cross
Journal:  Proc Natl Acad Sci U S A       Date:  1995-11-21       Impact factor: 11.205

10.  Catalytic site nucleotide binding and hydrolysis in F1F0-ATP synthase.

Authors:  S Löbau; J Weber; A E Senior
Journal:  Biochemistry       Date:  1998-07-28       Impact factor: 3.162
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  3 in total

1.  Charge displacements during ATP-hydrolysis and synthesis of the Na+-transporting FoF1-ATPase of Ilyobacter tartaricus.

Authors:  Christiane Burzik; Georg Kaim; Peter Dimroth; Ernst Bamberg; Klaus Fendler
Journal:  Biophys J       Date:  2003-09       Impact factor: 4.033

2.  TCDD decreases ATP levels and increases reactive oxygen production through changes in mitochondrial F(0)F(1)-ATP synthase and ubiquinone.

Authors:  Howard G Shertzer; Mary Beth Genter; Dongxiao Shen; Daniel W Nebert; Ying Chen; Timothy P Dalton
Journal:  Toxicol Appl Pharmacol       Date:  2006-10-04       Impact factor: 4.219

Review 3.  ATP synthases in the year 2000: defining the different levels of mechanism and getting a grip on each.

Authors:  P L Pedersen; Y H Ko; S Hong
Journal:  J Bioenerg Biomembr       Date:  2000-10       Impact factor: 2.945
  3 in total

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