Database of in-situ Raman spectra from Na2H2ATP solutions at 80,100 and 120 °C and up to 1666 MPa for determination of the rate constant of the ATP hydrolysis
Cite as:
Moeller, Christoph; Schmidt, Christian; Testemale, Denis; Guyot, François; Kokh, Maria; Wilke, Max (2023): Database of in-situ Raman spectra from Na2H2ATP solutions at 80,100 and 120 °C and up to 1666 MPa for determination of the rate constant of the ATP hydrolysis. GFZ Data Services. https://doi.org/10.5880/fidgeo.2023.031
Status
I N R E V I E W : Moeller, Christoph; Schmidt, Christian; Testemale, Denis; Guyot, François; Kokh, Maria; Wilke, Max (2023): Database of in-situ Raman spectra from Na2H2ATP solutions at 80,100 and 120 °C and up to 1666 MPa for determination of the rate constant of the ATP hydrolysis. GFZ Data Services. https://doi.org/10.5880/fidgeo.2023.031
Abstract
In biochemical systems, enzymes catalyze the endergonic phosphorylation of adenosine diphos-phate (ADP) to adenosine triphosphate (ATP) by different pathways, e.g., oxidative phosphoryla-tion catalyzed by membrane bound ATP synthase or substrate-level phosphorylation. The stored energy is released by the enzymatically controlled exergonic hydrolysis of ATP to power other vital endergonic reactions; therefore, ATP is widely known as the universal energy currency. Rapid abiotic ATP hydrolysis kinetics thus means higher maintenance energy costs for cells, and it has been suggested that this is an important factor in setting the limits to the functioning of living organisms (Bains et al. 2015). In order to evaluate the running conditions of the in-situ procedure by Moeller et al. (2022) using Raman spectroscopy opened up an efficient way of obtaining further insights to the effects of P-T- ionic composition on the kinetics of ATP-ADP hy-drolysis. Raman spectroscopy can be combined with a hydrothermal diamond anvil cell, which provides an isochoric system for measurements up to pressures of 2000 MPa. Another system for in-situ Raman spectroscopy at elevated pressures and temperatures is based on an autoclave fitted with optical high-pressure windows, as shown by Louvel et al. (2015) and works up to 200 MPa. In this system, pressure and temperature can be controlled independently, so that isobaric temperature series are possible.
This data publication compromises all Raman spectra measured in-situ of Na2H2ATP solutions at 80, 100 and 120 °C and up to 1666 MPa to determine the rate constants of the hydrolysis of adenosine triphosphate (ATP) to adenosine diphosphate (ADP) at 48 different P-T conditions. Furthermore, an assignment of peaks in the fitted range, the initial fit parameters and the fit-results are provided. Besides the kinetic data, the pH of the ATP solutions was calculated at experimental temperature and pressure conditions.
Authors
Moeller, Christoph;Institute of Geosciences, University of Potsdam, Potsdam, Germany
Schmidt, Christian;GFZ German Research Centre for Geosciences, Potsdam, Germany
Testemale, Denis;Néel Institute, Univ. Grenoble Alpes, Grenoble, France
Guyot, François;IMPMC Muséum National d'Histoire Naturelle, Paris, France
Kokh, Maria;Institut für Geowissenschaften, Potsdam, Germany; Institut für Mineralogie, Münster, Germany
Wilke, Max;Institute of Geosciences, University of Potsdam, Potsdam, Germany
Contact
Moeller, Christoph
(Doctoral student); Institute of Geosciences, Potsdam, Germany;
Contributors
Hydrothermal Diamond-Anvil Cell Laboratory; Laboratory Of Fundamental Research In Condensed Matter Physics
Keywords
ATP, adenosine triphosphate, ADP, adenosine diphosphate, AMP, adenosine monophosphate, In-situ Raman spectroscopy, Autoclave, Hydrothermal diamond anvil cell, HDAC, Hydrolysis, Kinetics, biosphere > biological process > animal life > metabolism > metabolite, chemical process > chemical reaction > reaction kinetics
affiliation: Institute of Geosciences, University of Potsdam, Potsdam, Germany
titles
title: Database of in-situ Raman spectra from Na2H2ATP solutions at 80,100 and 120 °C and up to 1666 MPa for determination of the rate constant of the ATP hydrolysis
publisher: GFZ Data Services
publicationYear: 2023
subjects
subject: ATP
subject: adenosine triphosphate
subject: ADP
subject: adenosine diphosphate
subject: AMP
subject: adenosine monophosphate
subject: In-situ Raman spectroscopy
subject: Autoclave
subject: Hydrothermal diamond anvil cell
subject: HDAC
subject: Hydrolysis
subject: Kinetics
subject (subjectScheme=GEMET - INSPIRE themes, version 1.0): biosphere > biological process > animal life > metabolism > metabolite
subject (subjectScheme=GEMET - INSPIRE themes, version 1.0): chemical process > chemical reaction > reaction kinetics
CharacterString: Database of in-situ Raman spectra from Na2H2ATP solutions at 80,100 and 120 °C and up to 1666 MPa for determination of the rate constant of the ATP hydrolysis
CharacterString: In biochemical systems, enzymes catalyze the endergonic phosphorylation of adenosine diphos-phate (ADP) to adenosine triphosphate (ATP) by different pathways, e.g., oxidative phosphoryla-tion catalyzed by membrane bound ATP synthase or substrate-level phosphorylation. The stored energy is released by the enzymatically controlled exergonic hydrolysis of ATP to power other vital endergonic reactions; therefore, ATP is widely known as the universal energy currency. Rapid abiotic ATP hydrolysis kinetics thus means higher maintenance energy costs for cells, and it has been suggested that this is an important factor in setting the limits to the functioning of living organisms (Bains et al. 2015). In order to evaluate the running conditions of the in-situ procedure by Moeller et al. (2022) using Raman spectroscopy opened up an efficient way of obtaining further insights to the effects of P-T- ionic composition on the kinetics of ATP-ADP hy-drolysis. Raman spectroscopy can be combined with a hydrothermal diamond anvil cell, which provides an isochoric system for measurements up to pressures of 2000 MPa. Another system for in-situ Raman spectroscopy at elevated pressures and temperatures is based on an autoclave fitted with optical high-pressure windows, as shown by Louvel et al. (2015) and works up to 200 MPa. In this system, pressure and temperature can be controlled independently, so that isobaric temperature series are possible.
This data publication compromises all Raman spectra measured in-situ of Na2H2ATP solutions at 80, 100 and 120 °C and up to 1666 MPa to determine the rate constants of the hydrolysis of adenosine triphosphate (ATP) to adenosine diphosphate (ADP) at 48 different P-T conditions. Furthermore, an assignment of peaks in the fitted range, the initial fit parameters and the fit-results are provided. Besides the kinetic data, the pH of the ATP solutions was calculated at experimental temperature and pressure conditions.
pointOfContact
CI_ResponsibleParty
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CharacterString: Moeller, Christoph
organisationName
CharacterString: Institute of Geosciences, Potsdam, Germany
CI_OnLineFunctionCode (codeList=http://www.isotc211.org/2005/resources/Codelist/gmxCodelists.xml#CI_OnLineFunctionCode codeListValue=http://www.isotc211.org/2005/resources/Codelist/gmxCodelists.xml#CI_OnLineFunctionCode_information): information
Released
Dataset
Abstract
;Institute of Geosciences, University of Potsdam, Potsdam, Germany
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