Asymmetric enzyme kinetics of F1-ATPase induced by rotation-assisted substrate binding
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arXiv
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| Autores principales: | , |
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| Formato: | Preprint |
| Publicado: |
2024
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| _version_ | 1866908389888491520 |
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| author | Nakayama, Yohei Toyabe, Shoichi |
| author_facet | Nakayama, Yohei Toyabe, Shoichi |
| contents | We demonstrate asymmetric enzyme kinetics of a biomolecular motor F1-ATPase between synthesis and hydrolysis of adenosine triphosphate (ATP). Our experiments show that ATP hydrolysis follows Michaelis-Menten kinetics, but ATP synthesis, which is an F1-ATPase's primary biological role, deviates from it. Specifically, the synthesis rate is sustained even at low substrate concentrations. Analysis of a theoretical model consistent with the experimental results reveals that ATP synthesis implements a rotation-assisted mechanism, in which a limited binding rate at low substrate concentration is partially compensated for by rotation to an angle where the binding rate is high. The results may imply that F1-ATPase implements a regulatory mechanism of enhancing substrate binding for ATP synthesis. |
| format | Preprint |
| id |
arxiv_https___arxiv_org_abs_2402_17326 |
| institution | arXiv |
| publishDate | 2024 |
| record_format | arxiv |
| spellingShingle | Asymmetric enzyme kinetics of F1-ATPase induced by rotation-assisted substrate binding Nakayama, Yohei Toyabe, Shoichi Biological Physics We demonstrate asymmetric enzyme kinetics of a biomolecular motor F1-ATPase between synthesis and hydrolysis of adenosine triphosphate (ATP). Our experiments show that ATP hydrolysis follows Michaelis-Menten kinetics, but ATP synthesis, which is an F1-ATPase's primary biological role, deviates from it. Specifically, the synthesis rate is sustained even at low substrate concentrations. Analysis of a theoretical model consistent with the experimental results reveals that ATP synthesis implements a rotation-assisted mechanism, in which a limited binding rate at low substrate concentration is partially compensated for by rotation to an angle where the binding rate is high. The results may imply that F1-ATPase implements a regulatory mechanism of enhancing substrate binding for ATP synthesis. |
| title | Asymmetric enzyme kinetics of F1-ATPase induced by rotation-assisted substrate binding |
| topic | Biological Physics |
| url | https://arxiv.org/abs/2402.17326 |