Temperature effect on water dynamics in tetramer phosphofructokinase matrix and the super-arrhenius respiration rate

Abstract Advances in understanding the temperature effect on water dynamics in cellular respiration are important for the modeling of integrated energy processes and metabolic rates. For more than half a century, experimental studies have contributed to the understanding of the catalytic role of wat...

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Autores principales:	Hsiao-Ching Yang, Yung-Chi Ge, Kuan-Hsuan Su, Chia-Cheng Chang, King-Chuen Lin, Vincenzo Aquilanti, Toshio Kasai
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/e7a7b4737c7a4d3384f1296f688d9793
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spelling	oai:doaj.org-article:e7a7b4737c7a4d3384f1296f688d97932021-12-02T14:01:36ZTemperature effect on water dynamics in tetramer phosphofructokinase matrix and the super-arrhenius respiration rate10.1038/s41598-020-79271-52045-2322https://doaj.org/article/e7a7b4737c7a4d3384f1296f688d97932021-01-01T00:00:00Zhttps://doi.org/10.1038/s41598-020-79271-5https://doaj.org/toc/2045-2322Abstract Advances in understanding the temperature effect on water dynamics in cellular respiration are important for the modeling of integrated energy processes and metabolic rates. For more than half a century, experimental studies have contributed to the understanding of the catalytic role of water in respiration combustion, yet the detailed water dynamics remains elusive. We combine a super-Arrhenius model that links the temperature-dependent exponential growth rate of a population of plant cells to respiration, and an experiment on isotope labeled 18O2 uptake to H2 18O transport role and to a rate-limiting step of cellular respiration. We use Phosphofructokinase (PFK-1) as a prototype because this enzyme is known to be a pacemaker (a rate-limiting enzyme) in the glycolysis process of respiration. The characterization shows that PFK-1 water matrix dynamics are crucial for examining how respiration (PFK-1 tetramer complex breathing) rates respond to temperature change through a water and nano-channel network created by the enzyme folding surfaces, at both short and long (evolutionary) timescales. We not only reveal the nano-channel water network of PFK-1 tetramer hydration topography but also clarify how temperature drives the underlying respiration rates by mapping the channels of water diffusion with distinct dynamics in space and time. The results show that the PFK-1 assembly tetramer possesses a sustainable capacity in the regulation of the water network toward metabolic rates. The implications and limitations of the reciprocal-activation–reciprocal-temperature relationship for interpreting PFK-1 tetramer mechanisms are briefly discussed.Hsiao-Ching YangYung-Chi GeKuan-Hsuan SuChia-Cheng ChangKing-Chuen LinVincenzo AquilantiToshio KasaiNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 11, Iss 1, Pp 1-14 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Hsiao-Ching Yang Yung-Chi Ge Kuan-Hsuan Su Chia-Cheng Chang King-Chuen Lin Vincenzo Aquilanti Toshio Kasai Temperature effect on water dynamics in tetramer phosphofructokinase matrix and the super-arrhenius respiration rate
description	Abstract Advances in understanding the temperature effect on water dynamics in cellular respiration are important for the modeling of integrated energy processes and metabolic rates. For more than half a century, experimental studies have contributed to the understanding of the catalytic role of water in respiration combustion, yet the detailed water dynamics remains elusive. We combine a super-Arrhenius model that links the temperature-dependent exponential growth rate of a population of plant cells to respiration, and an experiment on isotope labeled 18O2 uptake to H2 18O transport role and to a rate-limiting step of cellular respiration. We use Phosphofructokinase (PFK-1) as a prototype because this enzyme is known to be a pacemaker (a rate-limiting enzyme) in the glycolysis process of respiration. The characterization shows that PFK-1 water matrix dynamics are crucial for examining how respiration (PFK-1 tetramer complex breathing) rates respond to temperature change through a water and nano-channel network created by the enzyme folding surfaces, at both short and long (evolutionary) timescales. We not only reveal the nano-channel water network of PFK-1 tetramer hydration topography but also clarify how temperature drives the underlying respiration rates by mapping the channels of water diffusion with distinct dynamics in space and time. The results show that the PFK-1 assembly tetramer possesses a sustainable capacity in the regulation of the water network toward metabolic rates. The implications and limitations of the reciprocal-activation–reciprocal-temperature relationship for interpreting PFK-1 tetramer mechanisms are briefly discussed.
format	article
author	Hsiao-Ching Yang Yung-Chi Ge Kuan-Hsuan Su Chia-Cheng Chang King-Chuen Lin Vincenzo Aquilanti Toshio Kasai
author_facet	Hsiao-Ching Yang Yung-Chi Ge Kuan-Hsuan Su Chia-Cheng Chang King-Chuen Lin Vincenzo Aquilanti Toshio Kasai
author_sort	Hsiao-Ching Yang
title	Temperature effect on water dynamics in tetramer phosphofructokinase matrix and the super-arrhenius respiration rate
title_short	Temperature effect on water dynamics in tetramer phosphofructokinase matrix and the super-arrhenius respiration rate
title_full	Temperature effect on water dynamics in tetramer phosphofructokinase matrix and the super-arrhenius respiration rate
title_fullStr	Temperature effect on water dynamics in tetramer phosphofructokinase matrix and the super-arrhenius respiration rate
title_full_unstemmed	Temperature effect on water dynamics in tetramer phosphofructokinase matrix and the super-arrhenius respiration rate
title_sort	temperature effect on water dynamics in tetramer phosphofructokinase matrix and the super-arrhenius respiration rate
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/e7a7b4737c7a4d3384f1296f688d9793
work_keys_str_mv	AT hsiaochingyang temperatureeffectonwaterdynamicsintetramerphosphofructokinasematrixandthesuperarrheniusrespirationrate AT yungchige temperatureeffectonwaterdynamicsintetramerphosphofructokinasematrixandthesuperarrheniusrespirationrate AT kuanhsuansu temperatureeffectonwaterdynamicsintetramerphosphofructokinasematrixandthesuperarrheniusrespirationrate AT chiachengchang temperatureeffectonwaterdynamicsintetramerphosphofructokinasematrixandthesuperarrheniusrespirationrate AT kingchuenlin temperatureeffectonwaterdynamicsintetramerphosphofructokinasematrixandthesuperarrheniusrespirationrate AT vincenzoaquilanti temperatureeffectonwaterdynamicsintetramerphosphofructokinasematrixandthesuperarrheniusrespirationrate AT toshiokasai temperatureeffectonwaterdynamicsintetramerphosphofructokinasematrixandthesuperarrheniusrespirationrate
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Temperature effect on water dynamics in tetramer phosphofructokinase matrix and the super-arrhenius respiration rate

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