ATP hydrolysis - wikipedia ATP hydrolysis This article needs additional citations for verification. Please help improve this article by adding citations to reliable sources. Unsourced material may be challenged and removed. ( February 2015 ) This article may require cleanup to meet Wikipedia 's quality standards. The specific problem is : Grammar and word choice seem confused in places, may need a careful look by someone who knows the subject. Please help improve this article if you can. ( February 2018 ) Structure of ATP Structure of ADP Four possible resonance structures for orthophosphate ATP hydrolysis is the reaction by which chemical energy that has been stored in the high - energy phosphoanhydride bonds in adenosine triphosphate ( ATP ) is released, for example in muscles, by producing work in the form of mechanical energy. The product is adenosine diphosphate ( ADP ) and an inorganic phosphate, orthophosphate ( P ). ADP can be further hydrolyzed to give energy, adenosine monophosphate ( AMP ), and another orthophosphate ( P ). ATP hydrolysis is the final link between the energy derived from food or sunlight and useful work such as muscle contraction, the establishment of electrochemical gradients across membranes, and biosynthetic processes necessary to maintain life. The description and typical textbook labeling anhydridic bonds as `` high energy... bonds '' can be very misleading to students. These bonds are in fact relatively weak. They do involve high energy electrons but the bonds themselves are quite easy to break. As noted below, energy is released by the hydrolysis of ATP when these weak bonds are broken -- requiring a small input of energy, followed by the formation of new bonds and the release of a larger amount of energy as the total energy of the system is lowered and becomes more stable. Hydrolysis of the phosphate groups in ATP is especially exergonic, because the resulting orthophosphate group is greatly stabilized by multiple resonance structures, making the products ( ADP and P ) much lower in energy than the reactant ( ATP ). The high negative charge density associated with the three adjacent phosphate units of ATP also destabilizes the molecule, making it higher in energy. Hydrolysis relieves some of these electrostatic repulsions, liberating useful energy in the process by causing conformational changes in enzyme structure. In humans, approximately 60 percent of the energy released from the hydrolysis of one mole of ATP produces metabolic heat rather than fuel the actual reactions taking place. Due to the acid - base properties of ATP, ADP, and inorganic phosphate, the hydrolysis of ATP has the effect of lowering the pH of the reaction medium. Under certain conditions, high levels of ATP hydrolysis can contribute to lactic acidosis. How much energy ATP hydrolysis produces Hydrolysis of the terminal phosphoanhydridic bond is a highly exergonic process. The amount of released energy depends on the conditions in a particular cell. Specifically, the energy released is dependent on concentrations of ATP, ADP and P. The further the concentrations are from equilibrium the greater the absolute value of Gibbs free energy change ( ΔG ) will be. In standard conditions ( ATP, ADP and P concentrations are equal to 1M, water concentration is equal to 55M ) the value of ΔG is between - 28 to - 34 kJ / mol. The variability of the ΔG value exists, because this reaction is also dependent on the concentration of Mg cations. The cation Mg plays a role in stabilizing the ATP molecule. But the conditions in a cell are far from the standard state. In fact the ΔG in standard conditions would mean that the concentrations are close to equilibrium. And if cells were actually at equilibrium the change in Gibbs free energy would be zero. That would mean, that no energy is acquired by ATP hydrolysis, and that would have fatal consequences for the organism. Because this reaction is often coupled with thermodynamically unfavorable reactions, to give an overall negative ( spontaneous ) change in Gibbs free energy ( ΔG ) for the reaction sequence. The outcome of ATP hydrolysis is dependent not only on the studied organism, but also on the tissue or even the compartment within the cell. The current demand for energy must be taken into account as well. Variability in the ΔG are therefore to be expected. It is important to realize how far away are the actual concentrations from the standard condition concentrations. They are lower by three orders of magnitude ( standard condition values are in M and in reality they are in mM ). Because these concentrations are so low, the reaction will be energetically more favorable. To find out the ΔG in vivo in humans, the concentration of ATP, ADP and P are measured by using nuclear magnetic resonance. In a human body, in muscle, while in resting state the concentration of ATP is around 4 mM and the concentration of ADP is around 9 μmol / l. And thus the ATP hydrolysis yields the ΔG value of - 64 kJ / mol. After ischemia, when the muscle is recovering from exercise, the concentration of ATP is as low as 1 mM and the concentration of ADP is around 7 μmol / l. Therefore the absolute ΔG would be as high as - 69 kJ / mol. By comparing the standard value of ΔG and the real life value of ΔG, we can see that the worth of ATP, as measured in humans, is almost twice as much as the worth of ATP in standard conditions. See also Dephosphorylation References Syberg, F. Suveyzdis, Y., Kotting, C., Gerwert K., & Hofmann, E. Time - Resolved Fourier Transform Infrared Spectroscopy of the Nucleotide - binding Domain from the ATP - binding Cassette Transporter MsbA : ATP HYDROLYSIS ID THE RATE - LIMITING STEP IN THE CATALYTIC CYCLE. Journal of Biological Chemistry, 278 ( 28 ), 23923 - 23931 doi : 10.1074 / jbc. M112. 359208 Zharova, T.V, & Vinogradov, Proton - Translocating ATP - synthase of Paracoccus denitrificans : ATP - Hydrolytic Activity. Biochemistry ( 00062979 :, 68 ( 10 ), A.D. ( 2003 ). 1101 - 1108 Kamerlin, S.C., & Warshel, A. ( 2009 ). On the energetics of ATP hydrolysis in solution. The Journal of Physical Chemistry B, 113 ( 47 ), 15692 - 15698. Bergman, C., Kashiwaya, Y., & Veech, R.L. ( 2010 ) The effect of pH and Free Mg2+ on ATP Linked Enzymes and the Calculation of Gibbs Free Energy of ATP Hydrolysis. Journal of Physical Chemistry B, 114 ( 49 ), 16137 - 16146. Berg, J.M., Tymoczko, J.L., Stryer, L., Biochemistry, international edition. W.H. Freeman. ; New York, New York, 2011 ; p 287 Specific ^ Jump up to : Lodish, Harvey ( 2013 ). Molecular cell biology ( 7th ed. ). New York : W.H. Freeman and Co. pp. 52, 53. ISBN 9781464109812. OCLC 171110915. Jump up ^ Berne & Levy physiology. Berne, Robert M., 1918 - 2001., Koeppen, Bruce M., Stanton, Bruce A. ( 6th, updated ed. ). Philadelphia, PA : Mosby / Elsevier. 2010. ISBN 9780323073622. OCLC 435728438. Jump up ^ `` Standard Gibbs free energy of ATP hydrolysis - Generic - BNID 101989 ''. bionumbers.hms.harvard.edu. Retrieved 2018 - 01 - 25. ^ Jump up to : Philips, Ron Milo & Ron. `` '' How much energy is released in ATP hydrolysis ? ``. book.bionumbers.org. Retrieved 2018 - 01 - 25. Jump up ^ Wackerhage, H. ; Hoffmann, U. ; Essfeld, D. ; Leyk, D. ; Mueller, K. ; Zange, J. ( December 1998 ). `` Recovery of free ADP, Pi, and free energy of ATP hydrolysis in human skeletal muscle ''. Journal of Applied Physiology. 85 ( 6 ) : 2140 -- 2145. doi : 10.1152 / jappl. 1998.85. 6.2140. ISSN 8750 - 7587. PMID 9843537. Retrieved from `` https://en.wikipedia.org/w/index.php?title=ATP_hydrolysis&oldid=831577050 '' Categories : Cellular respiration Exercise physiology Hidden categories : Articles needing additional references from February 2015 All articles needing additional references Articles needing cleanup from February 2018 All pages needing cleanup Cleanup tagged articles with a reason field from February 2018 Wikipedia pages needing cleanup from February 2018 Talk About Wikipedia Add links This page was last edited on 21 March 2018, at 08 : 12. About Wikipedia

Question: what is the breakdown product formed when one phosphate group is removed from atp
Answer: adenosine diphosphate (ADP) and an inorganic phosphate, orthophosphate (Pi); adenosine diphosphate (ADP); adenosine diphosphate (ADP)