Coupling factor ATPase complex of Rhodospirillum rubrum. Purification and properties of a reconstitutively active single subunit

Philosoph, Sonia; Binder, Andres; Gromet-Elhanan, Zippora

doi:10.1016/s0021-9258(19)75285-5

Cited by 90 publications

(25 citation statements)

References 31 publications

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“…This possibility fits with a very well established fact that for the reconstitution of soluble or membrane-bound ATPase activity from the isolated F, subunits the presence of millimolar Mg-ATP is necessary (Gromet-Elhanan & Binder, 1974;Philosoph et al, 1977;Kagawa et al, 1978;Futai & Kanazawa, 1983). More detailed investigation is necessary to establish experimental conditions for specific aggregation of 0 as well as to identify nucleotide binding site, which are involved in this process.…”

Section: Discussionsupporting

confidence: 61%

“…In the presence of Mg-ATP the isolated 0-subunit of R. rubrum aggregates to form dimers (Mt 100000) and/or trimers (Mr 150000) (Harris et al, 1985). In order to retain a reconstitutive activity of R. rubrum 0 during the long period of isolation and purification procedure, it was necessary to add 2-4 mM Mg-ATP (Mg-ADP cannot prevent inactivation of 0) to the buffer solutions (Binder & Gromet-Elhanan, 1974;Philosoph et al, 1977;Khananshvili & Gromet-Elhanan, 1982) . It is possible that the aggregated forms of 0 are more stable in solution than the monomer.…”

Section: Discussionmentioning

confidence: 99%

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Empirical estimation of interaction energies for ligands binding in the isolated .beta.-subunit of F0F1 ATP synthase from Rhodospirillum rubrum

Khananshvili¹

1988

Biochemistry

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Section: Discussionsupporting

confidence: 61%

Section: Discussionmentioning

confidence: 99%

Empirical estimation of interaction energies for ligands binding in the isolated .beta.-subunit of F0F1 ATP synthase from Rhodospirillum rubrum

Khananshvili¹

1988

Biochemistry

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“…In this work we have, therefore, also attempted to define the site responsible for the divalent cation specificity on the F,-/3 subunit, using the isolated, purified R. rubrum ß subunit, ß (Philosoph et al, 1977;Khananshvili & Gromet-Elhanan, 1982). Occupation of the cation-ATP binding site that has earlier been characterized on ß has been found to be induced by Mn2+ as well as Mg2+, but inhibited by Ca2+.…”

mentioning

confidence: 99%

Regulation of .DELTA.~.mu.H + -coupled ATP synthesis and hydrolysis: role of divalent cations and of the F0F1-.beta. subunit

Gromet-Elhanan¹,

Weiss²

1989

Biochemistry

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The divalent cation specificity of ATP-linked reactions catalyzed by the H+-translocating F0F! ATP synthase-ATPase complex has been followed in the Rhodospirillum rubrum chromatophore bound complex. In the presence of Mg2+ and Mn2+ the complex catalyzes ATP synthesis and hydrolysis as well as ATP-driven H+ translocation, but in the presence of Ca2+ it catalyzes only ATP hydrolysis, which is not coupled to H+ tanslocation. The inability of Ca2+ to maintain the coupling process is not due to opening of a proton leak in its presence nor to any release of p! from the membrane, because (a) an identical light-induced H+ translocation is observed in the absence or presence of Ca-ATP and (b) the Ca-ATPase, as well as the Mg-and Mn-ATPase activities, is blocked by specific F0 inhibitors. These results indicate that the divalent cations play an important role in the regulation of H+-coupled ATP synthesis and hydrolysis by the F0Fj complex. Further tests suggest that their site of action is located on the Fr/3 subunit. The isolated ß subunit of the R. rubrum FqF, has been reported to contain two nucleotide binding sites, a Mg-independent and a Mg-dependent site [Gromet-Elhanan, Z., & Khananshvili, D. (1984) Biochemistry 23, 1022-1028]. Addition of Mn2+ also enables the binding of 2 mol of ATP/mol of this isolated ß subunit. But under identical conditions, Ca2+ does not enable ATP binding to this cation-dependent site and inhibits its binding in the presence of Mg2+ or Mn2+. In light of these results we propose that the binding of Mg-ATP or -ATP, but not of Ca-ATP, to the R. rubrum ¥3-ß subunit forms the trigger that opens the pathway for H+ translocation through the FqF] complex during catalysis.Electron-transport coupled ATP synthesis in respiratory and photosynthetic organisms is catalyzed by a reversible prot Supported in part by grants from the Minerva Foundation, Munich, West Germany, and from the United States-Israel Binational Science Foundation (BSF), Jerusalem, Israel. ton-translocating ATP synthase-ATPase complex that is composed of two distinct structures (Senior & Wise, 1983; Merchant & Selman, 1985): a readily solubilized catalytic ATPase sector, Fb and an intrinsic membrane sector that is involved in proton fluxes, F0. The F,-ATPase from many different sources has a 3ß3• ( subunit structure and contains 0006-2960/89/0428-3645S01.50/0 © 1989 American Chemical Society

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“…Firstly, the chromatophore was prepared from the cells of Rhodopseudomonas palustris according to ref. 70, in which F o was embedded in the chromatophore, 71 whereas F 1 protruded outside (structure 0). 72 Next, the b antibody was bound to each b subunit (structure 1); then, streptavidin was connected to the b antibody (structure 2), and the H9 antibody was bound to the streptavidin in series via biotin (structure 3).…”

Section: F O F 1 -Atpase Activity Regulated By External Links On the ...mentioning

confidence: 99%

FoF1-ATPase, rotary motor and biosensor

2010

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F(o)F(1)-ATPase is an amazing molecular rotary motor at the nanoscale. Single molecule technologies have contributed much to the understanding of the motor. For example, fluorescence imaging and spectroscopy revealed the physical rotation of isolated F(1) and F(o), or F(o)F(1) holoenzyme. Magnetic tweezers were employed to manipulate the ATP synthesis/hydrolysis in F(1), and proton translation in F(o). Here, we briefly review our recent works including a systematic kinetics study of the holoenzyme, the mechanochemical coupling mechanism, reconstituting the delta-free F(o)F(1)-ATPase, direct observation of F(o) rotation at single molecule level and activity regulation through external links on the stator.

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Coupling factor ATPase complex of Rhodospirillum rubrum. Purification and properties of a reconstitutively active single subunit

Cited by 90 publications

References 31 publications

Empirical estimation of interaction energies for ligands binding in the isolated .beta.-subunit of F0F1 ATP synthase from Rhodospirillum rubrum

Empirical estimation of interaction energies for ligands binding in the isolated .beta.-subunit of F0F1 ATP synthase from Rhodospirillum rubrum

Regulation of .DELTA.~.mu.H + -coupled ATP synthesis and hydrolysis: role of divalent cations and of the F0F1-.beta. subunit

FoF1-ATPase, rotary motor and biosensor

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