In biochemical systems, enzymes facilitate the endergonic reaction of adenosine diphosphate (ADP) to adenosine triphosphate (ATP) via pathways such as oxidative phosphorylation by mem-brane-bound ATP synthase or substrate-level phosphorylation. The energy stored in ATP is re-leased through enzymatic control of exergonic hydrolysis, which powers other essential ender-gonic reactions, thus earning ATP the name as the universal energy currency. The non-enzymatic hydrolysis of ATP to ADP in the absence of biological processes increases and counteracts this biological process. It is believed that this is a key factor in defining the operational limits of liv-ing organisms (Bains et al., 2015). The in-situ procedure developed by Moeller et al. (2022, 2024), which employs Raman spec-troscopy, has facilitated the exploration of the effects of pressure, temperature, and ionic com-position on the kinetics of ATP-ADP hydrolysis in an effective manner. Raman spectroscopy can be combined with a hydrothermal diamond anvil cell, thereby enabling measurements in an isochoric system at pressures up to 2000 MPa (Moeller et al., 2024). Another configuration for in-situ Raman spectroscopy at elevated pressures and temperatures employs an autoclave with optical high-pressure windows, as demonstrated by Louvel et al. (2015). This system is capable of operating at pressures up to 200 MPa, with independent control of pressure and temperature, allowing for isobaric temperature series to be conducted. In living organisms, ATP is activated by complexation with Mg2+. The objective of this study was to provide new kinetic data on ATP hy-drolysis and offer further insights into this key metabolite under extreme conditions, thus ex-tending the datasets of Moeller et al. ([dataset] 2024A, B). This data publication presents the complete set of Raman spectra obtained in situ for Na2H2ATP solutions with MgCl2, CaCl2, and NaCl at temperatures of 80 °C, 100 °C, and 120 °C under vapor saturation or at 20 MPa. The data were employed to ascertain the rate constants for ATP hydro-lysis to ADP across eight distinct chemical compositions. An elaborative thermodynamic model was used to mimic the chemical system at experimental conditions. The results are a compre-hensive database of ATP species concentrations at 80 °C, 100 °C, and 120 °C, which is provided herewith.
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.