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Delta G Atp

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The Energetic Secret of Life: Unpacking the Mystery of ΔG ATP



Ever wonder how your body builds complex molecules, contracts muscles, or even thinks? The answer, in a nutshell, lies in a tiny, ubiquitous molecule: adenosine triphosphate, or ATP. But understanding how ATP fuels these incredible processes isn't simply about knowing its structure; it's about grasping the concept of Gibbs Free Energy (ΔG) and its crucial role in ATP hydrolysis. We're not talking about dry textbook definitions here; we're diving into the energetic heart of life itself. So, buckle up, because we're about to uncover the fascinating story of ΔG ATP.

Understanding Gibbs Free Energy (ΔG)



Before we dissect ATP's energetic prowess, let's get familiar with ΔG. In simple terms, ΔG represents the energy available to do useful work in a system at constant temperature and pressure. A negative ΔG signifies an exergonic reaction – a reaction that releases energy and proceeds spontaneously. Conversely, a positive ΔG indicates an endergonic reaction, requiring energy input to occur. Think of it like this: rolling a ball downhill is exergonic (negative ΔG), while pushing it uphill is endergonic (positive ΔG).

Biological systems are constantly juggling these exergonic and endergonic reactions. Consider photosynthesis: plants absorb sunlight (energy input) to convert carbon dioxide and water into glucose (endergonic, positive ΔG). This process wouldn't be possible without the coupling of exergonic reactions that release energy. This is where ATP steps in.


ATP Hydrolysis: The Powerhouse Reaction



ATP hydrolysis is the process where ATP loses a phosphate group, forming adenosine diphosphate (ADP) and inorganic phosphate (Pi). This reaction is highly exergonic, boasting a ΔG of approximately -30.5 kJ/mol under standard conditions. This significant negative ΔG is the key to ATP's function as the cellular energy currency. The released energy isn't directly used; instead, it's coupled to endergonic reactions, making them thermodynamically feasible.

Imagine a water wheel powered by a waterfall. The waterfall's potential energy (like the energy released during ATP hydrolysis) drives the wheel (the endergonic reaction). The wheel doesn't directly use the water; it uses the energy transferred through the water's movement.


Coupling Exergonic and Endergonic Reactions: The ATP Advantage



ATP hydrolysis's negative ΔG allows it to drive numerous endergonic processes within the cell. This coupling often involves phosphorylating (adding a phosphate group) an intermediate molecule, creating a high-energy intermediate. This intermediate then participates in the endergonic reaction, making it energetically favorable.

A prime example is active transport, where cells move molecules against their concentration gradients. This requires energy. ATP hydrolysis provides this energy by phosphorylating a transport protein, causing a conformational change that allows the molecule to be transported across the membrane. Similarly, muscle contraction involves the phosphorylation and subsequent dephosphorylation of myosin, leading to the sliding of actin and myosin filaments.


Factors Affecting ΔG ATP



While -30.5 kJ/mol is a standard value, the actual ΔG of ATP hydrolysis in a cell can vary. This is influenced by several factors, including:

Concentrations of ATP, ADP, and Pi: Higher ATP concentrations reduce the ΔG (making hydrolysis less spontaneous), while higher ADP and Pi concentrations increase it (making hydrolysis more spontaneous).
Temperature and pH: These factors can affect the equilibrium constant of the reaction, influencing ΔG.
Magnesium ion concentration: Magnesium ions bind to ATP, influencing its conformation and thus the energetics of hydrolysis.


Beyond ATP: Other Energy Carriers



While ATP is the primary energy currency, other molecules, like GTP (guanosine triphosphate), also play vital roles in cellular energy transfer. These molecules have their own ΔG values for hydrolysis and are often involved in specific metabolic pathways. For example, GTP is crucial in protein synthesis and signal transduction pathways.


Conclusion:

Understanding ΔG ATP is essential for comprehending the fundamental workings of life. The highly exergonic nature of ATP hydrolysis, coupled with its ability to drive endergonic reactions, makes it the engine of cellular processes. By exploring the nuances of ΔG and its influence on ATP hydrolysis, we gain a deeper appreciation for the intricate energy management systems within living organisms. The seemingly simple act of breaking a phosphate bond unlocks a universe of biological possibilities.


Expert-Level FAQs:

1. How does the ΔG of ATP hydrolysis differ in vivo compared to standard conditions, and what are the implications? The ΔG in vivo is significantly more negative than the standard -30.5 kJ/mol due to cellular concentrations of reactants and products being far from standard state. This ensures a more efficient energy transfer.

2. Can we predict the ΔG of a coupled reaction involving ATP hydrolysis? Yes, using the individual ΔG values of both the ATP hydrolysis and the coupled reaction, and considering the stoichiometry.

3. How does the structure of ATP contribute to its high-energy phosphate bonds? Resonance stabilization of the products (ADP and Pi) is lower than that of the reactant (ATP), making the hydrolysis reaction energetically favourable.

4. What are the mechanisms of ATP regeneration? Primarily through cellular respiration (oxidative phosphorylation) and substrate-level phosphorylation in glycolysis and the citric acid cycle.

5. How is the ΔG of ATP hydrolysis influenced by enzyme catalysis? Enzymes do not affect the overall ΔG of the reaction, but they lower the activation energy, allowing the reaction to proceed faster at a given concentration of reactants.

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MITOCW | 21. Glycolysis II/Regulation - MIT OpenCourseWare And so delta G is what really matters for any individual reactions, and what's shown here on this slide is basically a approximate delta G0 change across the glycolytic pathway based on someone's approximation of the conditions found in cells.

Microsoft Word - 40B48EF9-6584-08553F.doc - cuni.cz For the hydrolysis of 1 mole of ATP to ADP at 37 ̊C, the standard free enthalpy change ∆G0 = −35 kJ . mol-1. Calculate the free enthalpy change ∆G at the ratio ATP/ADP = 100:1.

Free-energy change ( G) and entropy change ( S - chemrevise 3 Nov 2018 · The balance between entropy and enthalpy determines the feasibility of a reaction. This is given by the relationship : ∆G = ∆H - T∆Ssystem For any spontaneous change, ∆G will be negative. A reaction that has increasing entropy (+ve ∆S) and is exothermic (-ve ∆H ) will make ∆G be negative and will always be feasible

Microsoft PowerPoint - Metabolism-Basic Concepts.ppt Standard free energy change ∆Go is when reaction conditions are standard: T is 25 oC, P = 1 atm, conc of all reactants is 1M. For biochemical reactions, the pH has to be 7. The standard biochemical free energy change is designated as ∆Go’. ∆G = Gproducts – Greactants. If ∆G <0 , the forward reaction is favored relative to the reverse reaction.

Adenosine triphosphate (ATP) - KSU Rapid hydrolysis of ATP occurs only when catalyzed by an enzyme. The free energy change for ATP hydrolysis is -30,5 kJ/mol under standard conditions but the actual free energy change (ΔG) of ATP hydrolysis in living cells is very different.

AMMISSIONE5 20.ppt - unina.it ENERGIA ENZIMI La valuta energetica delle cellule: l’ATP. respirazione aerobica e fermentazione. Reazioni di ossidoriduzione nei viventi. processi energetici: fotosintesi, glicolisi,

Leccion2 - Universidad de La Laguna Supongamos una persona de 60 kg que sube una colina 100 m de alto, y que la hidrólisis de ATP se emplea con una eficacia del 60% en la producción del trabajo muscular necesario para efectuar esa subida.

Microsoft PowerPoint - Lecture 2 - Physical Foundations Recall from general chemistry lessons, that the spontaneity of a reaction is measured by the change in the Gibbs Free Energy (termed Delta G). Delta G in influenced by two different pairs of factors.

delta G - Texas Tech University Departments In a wide range of situations, we will see that understanding ∆G, ∆H and ∆S can help us understand where an equilibrium lies and often allow us to control whether the reactants or products are favored.

12-ATPase.ppt - University of Illinois Urbana-Champaign Why do we consume so much ATP? unfavorable (DG > 0). thermodynamically unfavorable reaction can be driven by a favorable one, if they are coupled. No spontaneous formation of B, …

&[Delta]G of ATP Hydrolysis and Cytosolic [ADP] Assessed at the … We recently formulated novel quantitative mathematical expressions of ∆G of ATP hydrolysis, and of the Kck as a function of total [PCr], pH and pMg, all quantities directly measurable by in vivo31P MRS (2).

CHEM 331 Biochemistry – Thermo Take Home Assignment 50 … The ΔG’o for the hydrolysis of acetyl-CoA to acetate and CoA is -32.2 kJ/mol and that for hydrolysis of ATP to AMP and PPi is -30.5 kJ/mol. Calculate ΔG’o for the ATP-dependent synthesis of acetyl-CoA.

Microsoft Word - Ejercicios_tema15.doc - unican.es a) Calcular ΔG en los eritrocitos humanos donde las concentraciones de ATP, ADP y Pi son 2.25 mM, 0.25 mM y 1.65 mM, respectivamente (suponer que el pH es 7 y la temperatura 25o C).

GTP and ATP hydrolysis in Biology - Wiley Online Library 2 May 2016 · In this special issue we focus on the comparison between catalytic mechanisms of proteins hydrolyzing ATP and GTP, putting together as many examples as suitable for one issue of the Journal.

- BIOENERGETI - JU Medicine Given the ΔG0′ values below, determine the overall ΔG0′ for the following reaction: creatine + ATP yields creatine phosphate + ADP The half reactions are ATP + H2O yields ADP + inorganic phosphate ΔG0'= −7.3 kcal/mol Creatine phosphate + H2O yields creatine + inorganic phosphate ΔG0'= −10.3 kcal/mol −3.0 kcal/mol −10.3 kcal/mol

Catabolisme glucidique - Free Phénomène à la base de tout le fonctionnement métabolique car la plupart des réactions sont couplées. C'est l'ATP qui est un agent de couplage énergétique dans la biosynthèse. Endergonique = Delta G > 0 / Exegonique = Delta G < 0. Stratégie utilisée pour la synthèse de cellules vivantes (le couplage)

Bryan Krantz: University of California, Berkeley Reading: Chs. 13 … [2] Conserve the energy stored in the original ATP molecule in the phosphoanhydride bond. [3] Increased binding energy for phosphorylated Intermediates on enzyme active sites lowering activation energy barrier, increasing enzyme specificity. Mg2+ ions are often key to this recognition process.

CHEM 332 Krebs Cycle F2023 - University of San Diego Succinate Thiokinase (STK) - Succinyl-CoA synthetase –– The GTP is easily converted to ATP by NDPK. In some tissues and specific species this is an ATP specific enzyme succinyl CoA + GDP -> succinate + GTP + CoASH substrate level phosphorylation Hydrolysis of thioester bond of succinyl CoA -delta Go’

MITOCW | 22. Glucogenesis/Carbohydrate Storage/TCA Cycle I This has a delta G 0 prime that is effectively 0. And so cells basically match their ATP to ADP ratios with any other ratios of nucleoside triphosphates and diphosphates because of this reaction.

MITOCW | 20. Bioenergetics/Intro Pathways/Glycolysis I In other words, the delta G of ATP synthesis, making ATP is going to be proportional to the log of the ratio of ATP over ADP for all the reasons I described. The delta G of using ATP, ATP hydrolysis, using ATP to drive reactions is also proportional to RT times the log, in this case, of the ADP to ATP ratio.