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Complex cooperativity of ATP hydrolysis in the F1-ATPase molecular motor

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Ming S. Liu, B. D. Todd, Richard J. Sadus

Genomics · Submitted 21 Jan 2004

abstract compiled · 2026-09-23 · no language-model review

The authors' main claim The quantitative analysis and modeling suggest the existence of complex cooperative hydrolysis between three different catalysis sites of F1-ATPase.

how it is stated · hedged possibility 0.98 read the record →

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arXiv IDq-bio/0401027 (version 1)
Pith IDMCH7IZ2C, Pith's permanent record of this paper and its review
CitationB. D. Todd, Ming S. Liu, Richard J. Sadus. "Complex cooperativity of ATP hydrolysis in the F1-ATPase molecular motor." arXiv:q-bio/0401027 (2004). https://pith.science/paper/MCH7IZ2C
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The compiled record

The paper's own sentences, arranged. Each label is drawn from a closed vocabulary; the number beside it is the probability the classifier gave that label. Numbers in the tables are the authors', checked by code. No sentence in this record was written by a model.

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Compiled by classifier-1.13.0 via TypeSafe API, question bank abstract-p1-20260923, 2026-09-23: 1 request, 4,826 input tokens.

What the abstract itself states, as probabilities: claims first 0.04 · states limitation 0.11 · human participants 0.02 · controlled comparison 0.05 · randomized assignment 0.01 · states quantitative result 0.08 · compares with prior results 0.48 · mentions code or data availability 0.02.

The abstract, sentence by sentence

arXiv listing abstract v1. Results and the main claim are underlined; .

F1-ATPase catalyses ATP hydrolysis and converts the cellular chemical energy into mechanical rotation. The hydrolysis reaction in F1-ATPase does not follow the widely believed Michaelis-Menten mechanism. Instead, the hydrolysis mechanism behaves in an ATP-dependent manner. We develop a model for enzyme kinetics and hydrolysis cooperativity of F1-ATPase which involves the binding-state changes to the coupling catalytic reactions. The quantitative analysis and modeling suggest the existence of complex cooperative hydrolysis between three different catalysis sites of F1-ATPase. This complexity may be taken into account to resolve the arguments on the bindingchange mechanism in F1-ATPase.

background contribution method result interpretation main claim

What the classifier reports for each sentence. The number is the probability it gave the label.
#sentencerolethe authors' own workstates the main conclusionstrength
s0 F1-ATPase catalyses ATP hydrolysis and converts the cellular chemical energy into mechanical rotation. background 1.00 0.07 0.03 asserted 1.00
s1 The hydrolysis reaction in F1-ATPase does not follow the widely believed Michaelis-Menten mechanism. result 0.50 0.33 0.20 asserted 1.00
s2 Instead, the hydrolysis mechanism behaves in an ATP-dependent manner. result 0.85 0.46 0.09 asserted 1.00
s3 We develop a model for enzyme kinetics and hydrolysis cooperativity of F1-ATPase which involves the binding-state changes to the coupling catalytic reactions. method 0.65 0.93 0.11 asserted 0.98
s4 The quantitative analysis and modeling suggest the existence of complex cooperative hydrolysis between three different catalysis sites of F1-ATPase. result 1.00 0.92 0.81 hedged possibility 0.98
s5 This complexity may be taken into account to resolve the arguments on the bindingchange mechanism in F1-ATPase. interpretation 0.99 0.18 0.13 hedged possibility 1.00

What kind of paper the classifier reports this is: theoretical result 1.00 · evidence from simulation or computation 0.75.

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  • C citations
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Every quoted sentence on this record is the authors'. Every label is from Pith's closed vocabulary, with the probability shown beside it. Every number in the measurements table is the authors', checked by code. Record as JSON

The paper
Original abstract

F1-ATPase catalyses ATP hydrolysis and converts the cellular chemical energy into mechanical rotation. The hydrolysis reaction in F1-ATPase does not follow the widely believed Michaelis-Menten mechanism. Instead, the hydrolysis mechanism behaves in an ATP-dependent manner. We develop a model for enzyme kinetics and hydrolysis cooperativity of F1-ATPase which involves the binding-state changes to the coupling catalytic reactions. The quantitative analysis and modeling suggest the existence of complex cooperative hydrolysis between three different catalysis sites of F1-ATPase. This complexity may be taken into account to resolve the arguments on the bindingchange mechanism in F1-ATPase.

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