The unusual enzymology of ATP synthase

Boyer, Paul D.

doi:10.1021/bi00400a001

Cited by 98 publications

(28 citation statements)

References 42 publications

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“…However, for metal ions like Zn 2+ or Cd 2+ , which have a pronounced affinity toward hydrogen donors, the situation is more complicated [22,23]. In these instances, the self-association is much larger and there is evidence that relatively stable dimeric stacks, like [Zn(ATP)] 2 4-, are formed, which then may also further associate to larger aggregates [22,23]. The occurrence of these dimers is explained [22,23,28] by the formation of an intermolecular metal ion bridge by coordination of Zn 2+ or Cd 2+ to the phosphate moiety of one nucleotide and to N7 of the other [16,28].…”

Section: Self-association Of Atpmentioning

confidence: 99%

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Adenosine 5'-triphosphate (ATP4-): Aspects of the coordination chemistry of a multitalented biological substrate

Sigel

2004

Pure and Applied Chemistry

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Firstly, the self-stacking properties of ATP 4-and the effects of metal ions and protons on these properties are described. Some examples involving macrochelate formation between phosphate-coordinated metal ions (M 2+ ) and N7 of the adenine residue in M(ATP) 2-are discussed, and this is followed by considerations on mixed ligand complexes consisting of ATP 4-, M 2+ , and amino acid anions with side chains that allow either aromatic-ring stacking or hydrophobic interactions with the adenine moiety; this gives rise to selectivity. Next, the properties of diphosphorylated 9-[2-(phosphonomethoxy)ethyl]adenine (PMEA 2-; Adefovir), i.e., of PMEApp 4-, are compared with those of (2′-deoxy)ATP 4-with regard to their metal ion-binding qualities, and in this way it can be explained why PMEApp 2-is initially an excellent substrate for nucleic acid polymerases. Of course, after incorporation of the PMEA residue into the growing nucleic acid chain, this is terminated and this is how PMEA exerts its antiviral properties [its bis(pivaloyloxymethyl)ester, Adefovir dipivoxil, was recently approved for use in hepatitis B therapy]. Finally, the change in free energy connected with (macro)chelate formation or intramolecular stacking interactions and the effect of a reduced dielectric constant of the solvent on the stability of complexes and their structures in solution is considered.

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Section: Self-association Of Atpmentioning

confidence: 99%

“…In fact, Boyer [2] has estimated that ATP and adenosine 5′-diphosphate (ADP 3-) and inorganic phosphate (P i ), from which it is formed, participate in more chemical reactions than any other compound on the Earth's surface except water.…”

Section: Introductionmentioning

confidence: 99%

Adenosine 5'-triphosphate (ATP4-): Aspects of the coordination chemistry of a multitalented biological substrate

Sigel

2004

Pure and Applied Chemistry

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“…This cooperativity of both ATP synthesis and ATP hydrolysis is currently best described by the alternating site model (18). In this model at any time during functioning, one catalytic site is involved in the bond cleavage reaction and is essentially closed; a second is opening to release the tightly bound product, and the third is closing to trap the substrate.…”

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confidence: 99%

Rotation of a γ-ε Subunit Domain in the Escherichia coli F1F0-ATP Synthase Complex

Aggeler

Ogilvie

Capaldi

1997

Journal of Biological Chemistry

110

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A triple mutant of Escherichia coli F 1 F 0 -ATP synthase, ␣Q2C/␣S411C/⑀S108C, has been generated for studying movements of the ␥ and ⑀ subunits during functioning of the enzyme. It includes mutations that allow disulfide bond formation between the Cys at ␣411 and both Cys-87 of ␥ and Cys-108 of ⑀, two covalent cross-links that block enzyme function (Aggeler, R., and Capaldi, R. A. (1996) J. Biol. Chem. 271, 13888 -13891). A cross-link is also generated between the Cys at ␣2 and Cys-140 of the ␦ subunit, which has no effect on functioning (Ogilvie, I., Aggeler, R., and Capaldi, R. A. (1997) J. Biol. Chem. 272, 16652-16656). CuCl 2 treatment of the mutant ␣Q2C/ ␣S411C/⑀S108C generated five major cross-linked products. These are ␣-␥-␦, ␣-␥, ␣-␦-⑀, ␣-␦, and ␣-⑀. The ratio of ␣-␥-␦ to the ␣-␥ product was close to 1:2, i.e. in one-third of the ECF 1 F 0 molecules the ␥ subunit was attached to the ␣ subunit at which the ␦ subunit is bound. Also, 20% of the ⑀ subunit was present as a ␣-␦-⑀ product. With regard to the ␦ subunit, 30% was in the ␣-␥-␦, 20% in the ␣-␦-⑀, and 50% in the ␣-␦ products when the cross-linking was done after incubation in ATP ؉ MgCl 2 . The amounts of these three products were 40, 22, and 38%, respectively, in experiments where Cu 2؉ was added after preincubation in ATP ؉ Mg 2؉ ؉ azide. The ␦ subunit is fixed to, and therefore identifies, one specific ␣ subunit (␣ ␦ ). A distribution of the ␥ and ⑀ subunits, which is essentially random with respect to the ␣ subunits, can only be explained by rotation of ␥-⑀ relative to the ␣ 3 ␤ 3 domain in ECF 1 F 0 .F 1 F 0 -type ATPases are found in the plasma membrane of bacteria, the inner membrane of mitochondria, and the thylakoid membrane of chloroplasts. These enzymes can both use a proton gradient to synthesize ATP and in the reverse direction hydrolyze ATP to establish a proton gradient for subsequent substrate and ion transport processes (1-3). The F 1 part of the enzyme from Escherichia coli, ECF 1 F 0 , is composed of ␣, ␤, ␥, ␦, and ⑀ subunits in the stoichiometry 3:3:1:1:1. This part is linked by a narrow stalk to the F 0 part that is composed of a, b, and c subunits in the stoichiometry 1:2:9 -12 (3-6). The stalk contains a part of the ␥ and ⑀ subunits (6, 7). Two other subunits, ␦ and b, are required for linkage of the F 1 and F 0 parts. These two subunits may provide a second separate connection (8, 9).Electron microscopy (10) and, more recently, a high resolution structure of the mitochondrial F 1 (11) have shown that the ␣ and ␤ subunits alternate in a hexagonal arrangement around a central cavity. These two large subunits have a similar fold, each with three domains, an N-terminal ␤ barrel domain on top and away from the F 0 , a middle nucleotide-binding domain, and a C-terminal ␣-helical domain (11). Three catalytic sites are present and located predominantly on ␤ subunits. The other three nucleotide binding sites on the ␣ subunits appear to have mostly a structural role. A part of the ␥ subunit is found within the ␣ 3 ␤ 3 barrel and organ...

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“…With respect to F, function, it has been proposed that during steady-state hydrolysis, the three catalytic sites work through the binding change mechanism of Boyer et al (Kayalar et al, 1977;Hackney and Boyer, 1978;Hutton and Boyer, 1979;Boyer, 1987Boyer, , 1989Boyer, , 1993. This hypothesis proposes that the catalytic sites exist in three different conformations that alternate upon binding and release of substrates and products.…”

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Acceleration of Unisite Catalysis of Mitochondrial F₁‐Adenosinetriphosphatase by ATP, ADP and Pyrophosphate

Garcia¹,

Gómez‐Puyou

Maldonado

et al. 1997

European Journal of Biochemistry

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The effect of ATP, ADP and pyrophosphate (PP,) on hydrolysis and release of [y-'*P]ATP bound to the high-affinity catalytic site of soluble F, from bovine heart mitochondria under unisite conditions [Grubmeyer, C., Cross, R. L. & Penefsky, H. S. (1982) J. B i d . Chem. 257, 12092-121001 was studied. In accord with the previous data, it was observed that millimolar concentrations of ATP or ADP added to F, undergoing unisite hydrolysis of [y-"PIATP accelerated its hydrolysis. PP, also produced a hydrolytic burst of a fraction of the previously bound [y-izP]ATP; kinetic data suggested that for production of optimal hydrolysis by PP, of the bound [y-'*P]ATP, two binding sites with apparent Kd of 27 pM and 240 pM must be filled. The extent of the hydrolytic burst induced by MgPP, was lower than that induced by ADP and ATP. In F, in which PP, had produced a hydrolytic burst of the bound [y-3zP]ATP, the addition of ATP induced a second burst of hydrolysis. By filtration experiments and enzyme trapping, it was also studied whether ATP, ADP and PP, produce release of the tightly bound [y-'*P]ATP. At millimolar concentrations, ATP and ADP brought about release of about 25 % of the previously bound [y-"PIATP. At micromolar concentrations, ADP accelerated the hydrolysis of the previously bound [Y-~'P]ATP but not its release. Hence, the hydrolytic and release reactions could be separated, indicating that the two reactions require the occupancy of different sites in F,. With PP,, no release of the tightly bound [y-?'P]ATP was observed. The ADP induced hydrolysis and release of the F,-bound [y-'*P]ATP were inhibited by sodium azide to the same extent (60%). Since release of ATP from a high-affinity catalytic site of F, represents the terminal step of oxidative phosphorylation, the data illustrate that the binding energy of substrates to F, is critical to the ejection of ATP into the media. The failure of PP, to induce release of [y-"P]ATP bound to F, under unisite conditions is probably due to its lower binding energy.

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The unusual enzymology of ATP synthase

Cited by 98 publications

References 42 publications

Adenosine 5'-triphosphate (ATP4-): Aspects of the coordination chemistry of a multitalented biological substrate

Adenosine 5'-triphosphate (ATP4-): Aspects of the coordination chemistry of a multitalented biological substrate

Rotation of a γ-ε Subunit Domain in the Escherichia coli F1F0-ATP Synthase Complex

Acceleration of Unisite Catalysis of Mitochondrial F₁‐Adenosinetriphosphatase by ATP, ADP and Pyrophosphate

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The unusual enzymology of ATP synthase

Cited by 98 publications

References 42 publications

Adenosine 5'-triphosphate (ATP4-): Aspects of the coordination chemistry of a multitalented biological substrate

Adenosine 5'-triphosphate (ATP4-): Aspects of the coordination chemistry of a multitalented biological substrate

Rotation of a γ-ε Subunit Domain in the Escherichia coli F1F0-ATP Synthase Complex

Acceleration of Unisite Catalysis of Mitochondrial F1‐Adenosinetriphosphatase by ATP, ADP and Pyrophosphate

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Acceleration of Unisite Catalysis of Mitochondrial F₁‐Adenosinetriphosphatase by ATP, ADP and Pyrophosphate