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Cited by 42Biochemical and Molecular Researchthermodynamics and calorimetric analysesChemical Reaction Mechanisms

The Effect of pH and Free Mg2+ on ATP Linked Enzymes and the Calculation of Gibbs Free Energy of ATP Hydrolysis

Bergman, Christian, Kashiwaya, Yoshihiro, Veech, Richard L.·2010·The Journal of Physical Chemistry B
DOI 10.1021/jp105723r
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Abstract

The apparent equilibrium constants, K′, of biochemical reactions containing substrates which bind [Mg2+] unequally can be significantly altered by changes in free intracellular [Mg2+]. Intracellular free [Mg2+] can be estimated by measurements of [citrate]/[isocitrate], a ratio known to vary with tissue free [Mg2+]. The combined equilibrium constant for glyceraldehyde-3-phosphate dehydrogenase, phosphoglycerate kinase, and triose phosphate isomerase for the three reactions (K(GG-TPI)′) was corrected using new binding constants for dihydroxyacetone-phosphate and 3-phosphoglycerate. The result of this calculation is demonstrated in the calculation of the free energy of ATP hydrolysis. In addition, the dependence of the equilibrium constant for the glutamine synthetase reaction on pH and free [Mg2+] was demonstrated. Furthermore, a theory linking the ΔG′ value of mitochondrial complex I−II and the cytosolic ΔG′ value of ATP hydrolysis is discussed with evidence from previous publications.

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  • Hydrolyzing peptides inside the cell might allow the bacterium to capture the energy released by the hydrolysis, and for longer peptides this might result in a net gain of energy.

    “Hydrolyzing peptides inside the cell might allow the bacterium to capture the energy released by the hydrolysis, and for the longer peptides, this might result in a net gain of energy as the energy released can exceed the energy required to re-phosphorylate two moles of ATP (Martin, 1998; Bergman et al., 2010).”

    From Modeled Structure of the Cell Envelope Proteinase of Lactococcus lactis (2020) · cites this paper as Bergman et al., 2010

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Authors
Bergman, C., Kashiwaya, Y., & Veech, R. L.
Affiliations
National Institutes of Health (US)
Corresponding author
Veech, Richard L.
ORCID
Venue
The Journal of Physical Chemistry B
Publisher
American Chemical Society (ACS)
Published
2010-09-27
Volume
114
Issue
49
Pages
16137-16146
ISSN
  • 1520-5207 (ISSN-L)
  • 1520-6106
DOI
10.1021/jp105723r
OpenAlex
W2331049753
Cited by
42
References
53
Citations by year
2026: 3 · 2025: 3 · 2024: 6 · 2023: 1 · 2022: 2 · 2021: 2 · 2020: 3 · 2019: 2 · 2018: 3 · 2017: 4 · 2016: 5 · 2015: 3 · 2014: 2 · 2012: 3
FWCI
0.39
Type
journal article
Language
en
Open access
closed
Locations
  • The Journal of Physical Chemistry B (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
  • Physical Sciences › Chemistry › Physical and Theoretical Chemistry › thermodynamics and calorimetric analyses
  • Physical Sciences › Chemistry › Organic Chemistry › Chemical Reaction Mechanisms
Keywords
ATP hydrolysis, Gibbs free energy, pH dependence, apparent equilibrium constant, glyceraldehyde-3-phosphate dehydrogenase, phosphoglycerate kinase, triosephosphate isomerase, glutamine synthetase, coupled reactions, intracellular magnesium
MeSH terms
Adenosine Triphosphate, Enzymes, Hydrogen-Ion Concentration, Hydrolysis, Magnesium, Thermodynamics, Electron Transport Complex I

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