The binding change mechanism for ATP synthase — Some probabilities and possibilities

Boyer, Paul D.

doi:10.1016/0005-2728(93)90063-l

Cited by 1,006 publications

(723 citation statements)

References 276 publications

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“…The F0 domain is totally membrane-embedded and involved in proton translocation while the F1 domain is extrinsically attached and provided with a set of three catalytically active nucleotide binding sites which are located at the al3-interfaces of the three circularly arranged al3-subunits. The high-resolution structure for bovine heart F1 obtained recently [6] has given strong support to the catalytic binding-change mechanism introduced by Boyer [7,8].…”

Section: Introductionmentioning

confidence: 67%

Kinetic modelling of the proton translocating CF₀CF₁‐ATP synthase from spinach

Pänke¹,

Rumberg²

1996

FEBS Letters

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Section: Introductionmentioning

confidence: 67%

Kinetic modelling of the proton translocating CF₀CF₁‐ATP synthase from spinach

Pänke¹,

Rumberg²

1996

FEBS Letters

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“…(37) Contrary to intuition, ATP hydrolysis or cleavage of the gamma phosphate bond is believed to be a step of the F 1 ATPase hydrolysis cycle that exists in equilibrium with ATP synthesis or bond formation and is therefore unlikely to cause a major structural change in the motor that produces force. (38) By contrast, binding of nucleotide in a conformation that enables it to be hydrolyzed, or release of hydrolysis products may cause large changes in The model shown in A can now be filled in with the structural elements tentatively identified as mechanical components of the kinesin motors: helix a4 is a putative spring-like element of the motor and the salt bridge between switch I (SWI) and switch II (SWII) may act like a latch to regulate release of ADP. The neck linker of conventional kinesin, possibly together with the stalk, and the stalk/neck of Ncd may act like a lever to amplify force produced by the motor.…”

Section: Motor Mechanical Elementsmentioning

confidence: 99%

Kinesin motors as molecular machines

Endow

2003

BioEssays

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SummaryMolecular motor proteins, fueled by energy from ATP hydrolysis, move along actin filaments or microtubules, performing work in the cell. The kinesin microtubule motors transport vesicles or organelles, assemble bipolar spindles or depolymerize microtubules, functioning in basic cellular processes. The mechanism by which motor proteins convert energy from ATP hydrolysis into work is likely to differ in basic ways from man-made machines. Several mechanical elements of the kinesin motors have now been tentatively identified, permitting researchers to begin to decipher the mechanism of motor function. The force-producing conformational changes of the motor and the means by which they are amplified are probably different for the plus-and minus-end kinesin motors.

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“…Structural, biochemical, and conceptual studies have shed major light on the details of this biological energy conversion process, but major issues remain have remained unresolved (Abrahams et al 1994 ;Boyer, 1993Boyer, , 1997Cherepanov et al 1999 ;Fersht, 1999 ;Wang & Oster, 1998;Weber & Senior, 1997). For example, despite the fact that the structures of several ATPases have been elucidated (e.g.…”

Section: Atpase and Energy Transduction 421 Introductionmentioning

confidence: 99%

Why nature really chose phosphate

Kamerlin

Sharma

Prasad

et al. 2013

Quart. Rev. Biophys.

319

448

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Phosphoryl transfer plays key roles in signaling, energy transduction, protein synthesis, and maintaining the integrity of the genetic material. On the surface, it would appear to be a simple nucleophile displacement reaction. However, this simplicity is deceptive, as, even in aqueous solution, the low-lying d-orbitals on the phosphorus atom allow for eight distinct mechanistic possibilities, before even introducing the complexities of the enzyme catalyzed reactions. To further complicate matters, while powerful, traditional experimental techniques such as the use of linear free-energy relationships (LFER) or measuring isotope effects cannot make unique distinctions between different potential mechanisms. A quarter of a century has passed since Westheimer wrote his seminal review, ‘Why Nature Chose Phosphate’ (Science 235 (1987), 1173), and a lot has changed in the field since then. The present review revisits this biologically crucial issue, exploring both relevant enzymatic systems as well as the corresponding chemistry in aqueous solution, and demonstrating that the only way key questions in this field are likely to be resolved is through careful theoretical studies (which of course should be able to reproduce all relevant experimental data). Finally, we demonstrate that the reason that naturereallychose phosphate is due to interplay between two counteracting effects: on the one hand, phosphates are negatively charged and the resulting charge-charge repulsion with the attacking nucleophile contributes to the very high barrier for hydrolysis, making phosphate esters among the most inert compounds known. However, biology is not only about reducing the barrier to unfavorable chemical reactions. That is, the same charge-charge repulsion that makes phosphate ester hydrolysis so unfavorable also makes it possible to regulate, by exploiting the electrostatics. This means that phosphate ester hydrolysis can not only be turned on, but also be turned off, by fine tuning the electrostatic environment and the present review demonstrates numerous examples where this is the case. Without this capacity for regulation, it would be impossible to have for instance a signaling or metabolic cascade, where the action of each participant is determined by the fine-tuned activity of the previous piece in the production line. This makes phosphate esters the ideal compounds to facilitate life as we know it.

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The binding change mechanism for ATP synthase — Some probabilities and possibilities

Cited by 1,006 publications

References 276 publications

Kinetic modelling of the proton translocating CF₀CF₁‐ATP synthase from spinach

Kinetic modelling of the proton translocating CF₀CF₁‐ATP synthase from spinach

Kinesin motors as molecular machines

Why nature really chose phosphate

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The binding change mechanism for ATP synthase — Some probabilities and possibilities

Cited by 1,006 publications

References 276 publications

Kinetic modelling of the proton translocating CF0CF1‐ATP synthase from spinach

Kinetic modelling of the proton translocating CF0CF1‐ATP synthase from spinach

Kinesin motors as molecular machines

Why nature really chose phosphate

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Kinetic modelling of the proton translocating CF₀CF₁‐ATP synthase from spinach

Kinetic modelling of the proton translocating CF₀CF₁‐ATP synthase from spinach