Item

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 N2H2ATP 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 ex-perimental temperature and pressure conditions.