The nucleotide binding site of F1‐ATPase which carries out uni‐site catalysis is one of the alternating active sites of the enzyme

  title={The nucleotide binding site of F1‐ATPase which carries out uni‐site catalysis is one of the alternating active sites of the enzyme},
  author={I. Kozlov and Y. Milgrom and M. Murataliev and E. N. Vulfson},
  journal={FEBS Letters},
Nucleotide‐depleted mitochondrial F1‐ATPase binds 3'‐(2')‐O‐(2‐nitro‐4‐azidobenzoyl)‐derivatives of ATP (NAB‐ATP) and GTP (NAB‐GTP) when these nucleotide analogues are added to the enzyme in equimolar quantities in the presence of Mg2+ (uni‐site catalysis conditions). The binding of NAB‐ATP is accompanied by its hydrolysis and inorganic phosphate dissociation from the enzyme; NAB‐ADP remains bound to F1‐ATPase. The F1‐ATPase·NAB‐ADP complex has no ATPase activity and its reactivation in the… Expand
Properties of chloroplast F1-ATPase partially modified by 2-azido adenine nucleotides, including demonstration of three catalytic pathways.
The CF1 is derivatized more extensively, the original catalytic pathway is lost, and two catalytic pathways that do not show modulation by ATP concentration are found, and the remaining beta subunits now have weak but independent catalytic capacity. Expand
The properties of hybrid F1-ATPase enzymes suggest that a cyclical catalytic mechanism involving three catalytic sites occurs.
Maximal rates of ATP hydrolysis catalyzed by F1-ATPase enzymes are known to involve strong positive catalytic site cooperativity. There are three potential catalytic nucleotide-binding sites on F1.Expand
Kinetic studies of ATP synthase: The case for the positional change mechanism
This review summarizes recent isotopic and kinetic evidence in favour of the concept, originally proposed by Boyer and coworkers, that energy from the proton gradient is exerted not directly for the reaction at the catalytic site, but rather to release product from a single catalysttic site. Expand
The number of functional catalytic sites on F1-ATPases and the effects of quaternary structural asymmetry on their properties
  • R. L. Cross
  • Chemistry, Medicine
  • Journal of bioenergetics and biomembranes
  • 1988
It is concluded that at least two and probably all three of the catalytic sites on F1 are functionally equivalent despite permanent structural asymmetry in the soluble enzyme. Expand
ATP Synthase and the Actions of Inhibitors Utilized To Study Its Roles in Human Health, Disease, and Other Scientific Areas
The rich source of ATP synthase inhibitors and their known or purported sites of action presented in this review should provide valuable insights into their applications as potential scaffolds for new therapeutics for human and animal diseases as well as for the discovery of new pesticides and herbicides to help protect the world's food supply. Expand
The binding change mechanism for ATP synthase--some probabilities and possibilities.
  • P. Boyer
  • Chemistry, Medicine
  • Biochimica et biophysica acta
  • 1993
Conformational changes and catalysis, the uniqueness of the ATP synthase structure and the role of unfolded protein structure in mechanism are discussed. Expand
Symmetry in F1-type ATPases.
La symetrie de l'enzyme F0F1-ATPase a ete etudiee grâce a la diffraction des RX, a la microscopie electronique, les modeles de structure tridimensionnelle, et les relations structure fonction ont eteExpand


Tightly bound adenosine diphosphate, which inhibits the activity of mitochondrial F1‐ATPase, is located at the catalytic site of the enzyme
It is proposed that ATP‐dependent dissociation of the F1‐ATPase‐GDP complex occurs more rapidly, than that of the MgADP‐Pi complex, because of the higher rate of ATP hydrolysis. Expand
The non-catalytic nucleotide-binding site of mitochondrial ATPase is localised on the alpha-subunit(s) of factor F1.
The results obtained testify to the fact that the non-catalytic site of mitochondrial ATP ase located on the alpha-subunit(s) of factor F1 may participate in the mechanism of ATP hydrolysis by membrane-bound ATPase. Expand
Exploring the adenine nucleotide binding sites on mitochondrial F1-ATPase with a new photoaffinity probe, 3'-O-(4-benzoyl)benzoyl adenosine 5'-triphosphate.
A mechanism of enzyme action for the Fl-ATPase suggests that a catalytic site resides on the p subunit and is closely associated, both topologically and hnctionally, with a specific ADP binding site situated on an immediately apposing a subunit. Expand
Assessment of the rate of bound substrate interconversion and of ATP acceleration of product release during catalysis by mitochondrial adenosine triphosphatase.
The estimated rate of reversal of hydrolysis of F1-ATPase-bound ATP to bound ADP + Pi varies only about 5-fold with ATP concentration, which adds to evidence that energy input or membrane components are not required for bound ATP synthesis. Expand
Interactions between the mitochondrial adenosinetriphosphatase and periodate-oxidized adenosine 5'-triphosphate, an affinity label for adenosine 5'-triphosphate binding sites.
Periodate-oxidized ATP (o-ATP) was prepared as an affinity label of nucleotide binding sites on the chloroform-released ox heart mitochondrial ATPase. In the presence of MgSO4, o-ATP is a substrateExpand
Localisation of adenine nucleotide-binding sites on beef-heart mitochondrial ATPase by photolabelling with 8-azido-ADP and 8-azido-ATP.
In contrast to the uncoupled ATPase activity, where the two ATP-binding sites do not interact, cooperation between the two sites is required for ATP hydrolysis coupled to reduction of NAD+ by succinate. Expand
Interaction of adenine nucleotides with multiple binding sites on beef heart mitochondrial adenosine triphosphatase.
Reconstitution of F1 with ADP or with almost 5 mol of AMP-P(NH)P resulted in preparations that exhibited an undiminished capacity to restore oxidative phosphorylation in F1-deficient submitochondrial particles. Expand
Azidonaphthoyl-ADP: a specific photolabel for the high-affinity nucleotide-binding sites of F1-ATPase.
This observation is discussed in terms of a stochastic model requiring a minimum of two interacting catalytic domains out of three in order to commence catalysis. Expand
On the subunit stoichiometry of the F1-ATPase and the sites in it that react specifically with p-fluorosulfonylbenzoyl-5'-adenosine.
It has been shown that the ATPase inactivated with FSBA retains the capacity to bind up to 2.2 mol of [14C]ADP/350,000 g of enzyme. Expand
An active-site-directed adenosine triphosphate analogue binds to the beta-subunits of factor F1 mitochondrial adenosine triphosphatase with its triphosphate moiety.
The results suggest that ATP may also bind to the beta-subunit of the adenosine triph phosphatase with its triphosphate moiety. Expand