Energy, Life, and ATP (Nobel Lecture)

Boyer, Paul D.

doi:10.1002/(sici)1521-3773(19980918)37:17<2296::aid-anie2296>3.0.co;2-w

Cited by 177 publications

(42 citation statements)

References 54 publications

(79 reference statements)

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“…As pointed out by Smith et al [72] in structural studies of another ABC protein, the energy of ATP binding ultimately drives the overall hydrolytic cycle. This mechanism is analogous to the "binding change" mechanism of ATP synthetase proposed by Boyer [9]. These considerations are important in interpreting the influence of nucleotide interactions with CFTR on channel gating.…”

Section: Cftr As Ion Channel and Enzymementioning

confidence: 99%

CFTR (ABCC7) is a hydrolyzable-ligand-gated channel

Aleksandrov

Riordan

2006

Pflugers Arch - Eur J Physiol

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As the product of the gene mutated in cystic fibrosis, the most common genetic disease of Caucasians, CFTR is an atypical ABC protein. From an evolutionary perspective, it is apparently a relatively young member of the ABC family, present only in metazoans where it plays a critical role in epithelial salt and fluid homeostasis. Functionally, the membrane translocation process it mediates, the passive bidirectional diffusion of small inorganic anions, is simpler than the vectorial transport of larger more complex substrates ("allocrites") by most ABC transporters. However, the control of the permeation pathway which cannot go unchecked is necessarily more stringent than in the case of the transporters. There is tight regulation by the phosphorylation/dephosphorylation of the unique CFTR R domain superimposed on the basic ABC regulation mode of ATP binding and hydrolysis at the dual nucleotide binding sites. As with other ABCC subfamily members, only the second of these sites is hydrolytic in CFTR. The phosphorylation and ATP binding/hydrolysis events do not strongly influence each other; rather, R domain phosphorylation appears to enable transduction of the nucleotide binding allosteric signal to the responding channel gate. ATP hydrolysis is not required for either the opening or closing gating transitions but efficiently clears the ligand-binding site enabling a new gating cycle to be initiated.

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Section: Cftr As Ion Channel and Enzymementioning

confidence: 99%

CFTR (ABCC7) is a hydrolyzable-ligand-gated channel

Aleksandrov

Riordan

2006

Pflugers Arch - Eur J Physiol

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“…The Journal of Biological Chemistry declined to publish the Nobel Prize-winning work of Paul Boyer, as he acknowledged in an interview published in his university magazine [OLNEY, 2000] and in his Nobel lecture [BOYER, 1997]. The work awarded the 1997 Nobel Prize in Chemistry was the description of the molecular motor that creates cellular energy, and the biochemical pump that transports energy across cell membrane.…”

Section: Resultsmentioning

confidence: 99%

Rejecting and resisting Nobel class discoveries: accounts by Nobel Laureates

Campanario

2009

Scientometrics

110

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“…After decades of research [3,4], we now have a comprehensive understanding of the structure and function of the enzyme [5][6][7][8][9][10]. In E.coli, the enzyme consists of two portions (F o and F 1 ) coupled together by a central rotary asymmetric shaft (γ ) [ Fig.…”

Section: Introductionmentioning

confidence: 90%

Torque-coupled thermodynamic model for FoF1 -ATPase

Liu

2017

Phys. Rev. E

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F o F 1 -ATPase is a motor protein complex that utilizes transmembrane ion flow to drive the synthesis of adenosine triphosphate (ATP) from adenosine diphosphate (ADP) and phosphate (Pi). While many theoretical models have been proposed to account for its rotary activity, most of them focus on the F o or F 1 portions separately rather than the complex as a whole. Here, we propose a simple but new torque-coupled thermodynamic model of F o F 1 -ATPase. Solving this model at steady state, we find that the monotonic variation of each portion's efficiency becomes much more robust over a wide range of parameters when the F o and F 1 portions are coupled together, as compared to cases when they are considered separately. Furthermore, the coupled model predicts the dependence of each portion's kinetic behavior on the parameters of the other. Specifically, the power and efficiency of the F 1 portion are quite sensitive to the proton gradient across the membrane, while those of the F o portion as well as the related Michaelis constants for proton concentrations respond insensitively to concentration changes in the reactants of ATP synthesis. The physiological proton gradient across the membrane in the F o portion is also shown to be optimal for the Michaelis constants of ADP and phosphate in the F 1 portion during ATP synthesis. Together, our coupled model is able to predict key dynamic and thermodynamic features of the F o F 1 -ATPase in vivo semiquantitatively, and suggests that such coupling approach could be further applied to other biophysical systems.

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Energy, Life, and ATP (Nobel Lecture)

Cited by 177 publications

References 54 publications

CFTR (ABCC7) is a hydrolyzable-ligand-gated channel

CFTR (ABCC7) is a hydrolyzable-ligand-gated channel

Rejecting and resisting Nobel class discoveries: accounts by Nobel Laureates

Torque-coupled thermodynamic model for FoF1 -ATPase

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