Energy‐dependent release of adenine nucleotides tightly bound to chloroplast coupling factor CF<sub>1</sub>

Strotmann, Heinrich; Bickel, Susanne; Huchzermeyer, Bernhard

doi:10.1016/0014-5793(76)81036-8

Cited by 131 publications

(42 citation statements)

References 11 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The ability to perform the photolysis procedure in the absence of unbound analog and the prior determination that the analog was bound only to ADP tight binding sites ensured that no nonspecific labeling occurred. The identification of the CF, complex as the only thylakoid membrane protein photolabeled by tightly bound 2-azido-ADP confirmed previous proposals [7,301 regarding the location of the nucleotide binding sites on the membrane. The lack of photoaffinity labeling of the smaller CF, subunits also is consistent with suggestions that the only nucleotide sites on the coupling factors are on the a and p subunits [4,8,30].…”

Section: Discussionsupporting

confidence: 88%

“…This protein was found to be a component of the CF, complex (Fig.7B). This supports previous proposals that the tight nucleotide sites on the thylakoid membranes are located exclusively on the coupling factor complex [7,30]. The data in Fig.…”

Section: Photoaffinity Labeling Of Thylakoid Membranes Containing Tigsupporting

confidence: 92%

“…While indirect means have provided evidence that the tight nucleotide binding sites on the thylakoid membranes exist primarily on the CFI complex [7,301, the possibility of tight nucleotide binding sites on other membrane components has not been eliminated. Thylakoid membranes containing tightly bound 2-a~ido-[P-~'PlADP were prepared and washed to remove unbound nucleotides.…”

Section: Photoaffinity Labeling Of Thylakoid Membranes Containing Tigmentioning

confidence: 99%

“…Thylakoid membranes also contain tightly bound adenine nucleotides which are believed to be associated with the CF, complex [7,8]. The tightly bound nucleotides on the chloroplast membrane exchange with medium nucleotides only upon energization of the membranes [6-101.…”

mentioning

confidence: 99%

See 3 more Smart Citations

Localization of the tight ADP‐binding site on the membrane‐bound chloroplast coupling factor one

Czarnecki

Abbott

Selman

1983

European Journal of Biochemistry

View full text Add to dashboard Cite

The photoaffinity analog 2-azido-ADP (2-azidoadenosine 5'-diphosphate) was used as a probe of the spinach chloroplast ATP synthase. The analog acted as a substrate for photophosphorylation. Several observations suggested that 2-azido-ADP and ADP bound to the same class of tight nucleotide binding sites: (a) 2-azido-ADP competitively inhibited ADP tight binding (ZC, = 1.4 pM); (b) the concentration giving 50 % maximum binding, for analog tight binding (1 pM) was similar to that observed for ADP (2 pM); (c) nucleotide tight binding required prior membrane energization and was completely reversed by re-energization; (d) the tight binding of 2-azido-[P-"PIADP was completely prevented by ADP; (e) the analog inhibited the light-triggered ATPase activity at micromolar concentrations.Ultraviolet irradiation of washed thylakoid membranes containing tightly bound 2-a~ido-[P-~'PlADP resulted in the covalent incorporation of the label into the membranes. Denaturing polyacrylamide gel electrophoresis of the labeled membranes demonstrated that the j subunit of the coupling factor one complex was the only polypeptide in the thylakoid membranes which was labeled. These results identify the fi subunit of the coupling factor as the location of the tightly bound ADP on the thylakoid membranes.

show abstract

Section: Discussionsupporting

confidence: 88%

Section: Photoaffinity Labeling Of Thylakoid Membranes Containing Tigsupporting

confidence: 92%

Section: Photoaffinity Labeling Of Thylakoid Membranes Containing Tigmentioning

confidence: 99%

mentioning

confidence: 99%

See 2 more Smart Citations

Localization of the tight ADP‐binding site on the membrane‐bound chloroplast coupling factor one

Czarnecki

Abbott

Selman

1983

European Journal of Biochemistry

View full text Add to dashboard Cite

show abstract

“…Chloroplast thylakoids containing tightly-bound [2-3H] ADP were prepared by illuminating washed, osmotically shocked chloroplasts in the presence of label followed by removal of medium nucleotides by several centrifugation and washing steps [27,28]. By definition, this ADP occupies tight, adenine-nucleotide-specific regulatory sites on CF, .…”

Section: Materials a N D Methodsmentioning

confidence: 99%

Activation of ATPase of spinach coupling factor 1. Release of tightly bound ADP from the soluble enzyme

Sherman

Wimmer

1984

Eur J Biochem

View full text Add to dashboard Cite

Several seemingly unrelated procedures used to elicit the latent ATPase activity of soluble spinach coupling factor 1 can be correlated to the release of tightly-bound ADP from the uncoupled enzyme. This ADP release is further enhanced by the presence of medium nucleotides, especially substrate ATP, and may or may not involve release from the catalytic site itself. Similarly, the light/dithiothreitol activation of membrane-bound CF, ATPase is reported to be accompanied by energy-dependent ADP dissociation. Further indication that ADP release is involved in the ATPase activation mechanism is the observation that a pyruvate kinase phosphoenolpyruvate trap for ADP released during light/dithiothreitol treatment greatly retards the decay of membrane-bound ATPase activity that occurs in the dark, presumably by preventing reassociation of ADP. The time course of CF, reactivation by light, after light/dithiothreitol activation followed by dark decay, allows a distinction to be made between the apparently rate-limiting dithiol modification and the more rapid dissociation of tightly bound ADP.Osmotically shocked spinach chloroplasts (outer membrane ruptured and stroma removed) catalyze the synthesis of ATP when energized in the presence of ADP and Pi. These

show abstract

Mitochondrial ATPase

Penefsky¹

1979

Advances in Enzymology - And Related Areas of Molecular Biology

View full text Add to dashboard Cite

Energy‐dependent release of adenine nucleotides tightly bound to chloroplast coupling factor CF₁

Cited by 131 publications

References 11 publications

Localization of the tight ADP‐binding site on the membrane‐bound chloroplast coupling factor one

Localization of the tight ADP‐binding site on the membrane‐bound chloroplast coupling factor one

Activation of ATPase of spinach coupling factor 1. Release of tightly bound ADP from the soluble enzyme

Mitochondrial ATPase

Contact Info

Product

Resources

About

Energy‐dependent release of adenine nucleotides tightly bound to chloroplast coupling factor CF1

Cited by 131 publications

References 11 publications

Localization of the tight ADP‐binding site on the membrane‐bound chloroplast coupling factor one

Localization of the tight ADP‐binding site on the membrane‐bound chloroplast coupling factor one

Activation of ATPase of spinach coupling factor 1. Release of tightly bound ADP from the soluble enzyme

Mitochondrial ATPase

Contact Info

Product

Resources

About

Energy‐dependent release of adenine nucleotides tightly bound to chloroplast coupling factor CF₁