Isolation and composition of the subunits of spinach chloroplast coupling factor protein.

Binder, Andres; Jagendorf, André T.; Ngo, E K

doi:10.1016/s0021-9258(17)40807-6

Cited by 192 publications

(33 citation statements)

References 28 publications

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“…The chloroplast coupling factor CF~ was isolated by the procedure of Binder et al (10). Complete separation of CF~ from ribulose 1,5 diphosphate-carboxylase-oxygenase was achieved by two density gradient centrifugation steps ( 10-30% sucrose density gradient in 20 mM Tris HC1, 2 mM EDTA, pH 7.8).…”

Section: Isolation Of the Cfo-cf1 Atp Synthetase And The Couplingmentioning

confidence: 99%

Reconstitution of cytochrome f/b6 and CF0-CF1 ATP synthetase complexes into phospholipid and galactolipid liposomes.

Mörschel¹,

Staehelin²

1983

The Journal of Cell Biology

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Cytochrome f/b6 and ATP synthetase (CF0-CF1) complexes from spinach chloroplasts have been reconstituted into liposomes prepared from soybean phospholipids and purified spinach galactolipids. Freeze-fracture analysis revealed homogeneous populations of particles spanning the lipid bilayers with their elongated axes perpendicular to the membrane plane. The lipid composition of the liposomes had no effect on the size of the reconstituted complexes, the average diameter of cytochrome f/b6 complex measuring 8.5 nm, and of the CF0 base piece of the ATP synthetase, 9.5 nm. When reconstituted cytochrome f/b6 complexes were cross-linked by means of antibodies prepared against the whole complex, the thus aggregated particles formed either hexagonal or square arrays. In both instances the centerto-center spacing of the particles was 8.3 nm, thereby suggesting that this value could be closer to the real diameter of the complexes than the one obtained from measuring individual particles. Assuming an ellipsoidal shape for these particles, and using a measured height of 11 nm, a molecular weight of ~280,000 could be calculated for the reconstituted cytochrome f/b6 complex, consistent with a dimeric configuration. In many instances the crystalline sheets of antibody-aggregated cytochrome f/b6 complexes were found to be free in the buffer solution; apparently the antibody-induced strains caused the sheet-like aggregates to pop out of the liposomal membranes. Agglutination studies of inside-out and right-side-out thylakoid vesicles revealed the antigenic determinants of the cytochrome land cytochrome b6 polypeptides to be exposed on the inner thylakoid surface and to be present in stacked and unstacked membrane regions. The molecular weight calculated from the size of freeze-fractured CFo base pieces was over twice the value determined by x-ray scattering data. This discrepancy may be caused by significant lipid domains within the base piece, or by an unusual fracturing behavior of the base piece in reconstituted liposomes.During the last decade significant progress has been made in the isolation of functional complexes from chloroplast membranes. Efforts are underway to correlate those functional units with structural membrane components (reviewed in 22). The first enzyme and pigment-protein complexes of photosynthetic membranes to be localized and positively identified by means of immunological and electron microscopical techniques were the CF~-ATP synthetase, the ribulose 1,5 diphosphate carboxylase-oxygenase, and the phycobilisomes of red algae and cyanobacteria (9,15,34,35). While positive identification of integral membrane protein complexes has yet to be achieved, several lines of indirect evidence obtained from freeze-fracture studies of greening chloroplasts, chloroplast mutants, and reconstituted membrane systems have led to the following tentative structure-function correlations: photosystem II reaction center-bound light-harvesting complexes and 10-17-nm EF particles (5,33,53,58), photosystem Ilight-harvesti...

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Section: Isolation Of the Cfo-cf1 Atp Synthetase And The Couplingmentioning

confidence: 99%

Reconstitution of cytochrome f/b6 and CF0-CF1 ATP synthetase complexes into phospholipid and galactolipid liposomes.

Mörschel¹,

Staehelin²

1983

The Journal of Cell Biology

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“…The coupling factor CF 1 was isolated from pea chloroplasts according to Binder et al (1978) and stored in 2 M ammonium sulfate in the presence of 1 mM АТР, 1 mM EDTA, and 50 mM Tris-SO 4 , pH 7.8. Excess nucleotides and ammonium sulfate were removed by gel filtration through a Fine Sephadex G-50 column equilibrated with 50 mM Tricine-KOH, pH 7.8.…”

Section: Methodsmentioning

confidence: 99%

Viscosimetric analysis of the mechanism of ATP hydrolysis by pea chloroplast F<sub>1</sub>-ATPase

Malyan¹

2018

Photosynt.

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Dependence of ATP hydrolysis kinetics by the chloroplast coupling factor (CF 1 ) on medium viscosity was studied at varying temperatures. For samples with oxidized and reduced CF 1 -subunit, this dependence was shown to be described by Cramers' relationship k ~ (η/η o ) -n , where k is the reaction rate constant, η/η o is the medium/water viscosity ratio, and 0 < n < 1. Transition of the -subunit from its reduced to oxidized state was accompanied by increasing n value, which is indicative of increasing friction losses between certain enzyme sections and the solution. The increased medium viscosity produced no effect on the reaction activation energy which appeared to be almost the same for the both enzyme states. The molecular mechanisms responsible for CF 1 activity loss in viscous media are discussed.

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“…Preparation of CFi and the ß Polypeptide. CFi was prepared from fresh market spinach (Binder et al,1978;Lien & Racker, 1971;Hu et al, 1993) and stored as an ammonium sulfate precipitate. Prior to use CFi was desalted on a 1.5…”

Section: Methodsmentioning

confidence: 99%

ADP binding induces long-distance structural changes in the .beta. polypeptide of the chloroplast ATP synthase

Mills¹,

Seibold²,

Squier³

et al. 1995

Biochemistry

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Binding of ADP to the beta polypeptide isolated from the catalytic F1 portion (CF1) of the chloroplast ATP synthase caused an increase of 10-20% in the steady state fluorescence intensity of fluorescent maleimides attached to the cysteine residue at position 63. Fluorescence lifetime distributions indicated that the beta polypeptide switched between two conformational states depending on the presence or absence of bound ADP. The fluorescence enhancement induced by ADP binding allowed a direct calculation of the dissociation constant for ADP of 0.7 microM. ATP did not cause a fluorescence enhancement but competed with ADP for binding to the same site. An apparent dissociation constant of 2 microM was obtained for ATP binding. Fluorescence resonance energy transfer experiments indicated that Cys63 is 42 A away from the nucleotide binding site on the beta polypeptide, confirming a previous measurement [(Colvert, K.K., Mills, D.A., Richter, M.L. (1992) Biochemistry 31, 3930-3935]. Frequency domain fluorescence anisotropy measurements indicated that the beta polypeptide has an irregular, elongated shape which is in good agreement with the conformation found in the crystal structure of the beef heart mitochondrial F1 enzyme [Abrahams, J.P., Leslie, A.G.W., Lutter, R., & Walker, J.E. (1994) Nature 370, 621-628]. The rotational correlation time did not change significantly upon ADP binding, indicating that ADP did not induce a large change in the overall shape of the beta polypeptide. The results show that the nucleotide binding domain and the N-terminal domain of the beta polypeptide communicate with each other over a significant distance via conformational changes.(ABSTRACT TRUNCATED AT 250 WORDS)

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Isolation and composition of the subunits of spinach chloroplast coupling factor protein.

Cited by 192 publications

References 28 publications

Reconstitution of cytochrome f/b6 and CF0-CF1 ATP synthetase complexes into phospholipid and galactolipid liposomes.

Reconstitution of cytochrome f/b6 and CF0-CF1 ATP synthetase complexes into phospholipid and galactolipid liposomes.

Viscosimetric analysis of the mechanism of ATP hydrolysis by pea chloroplast F<sub>1</sub>-ATPase

ADP binding induces long-distance structural changes in the .beta. polypeptide of the chloroplast ATP synthase

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