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Newton's Laws

Work, Energy, and Power

Electricity

The Chemical Bond

Functional Groups in Organic Chemistry

Chemical Thermodynamics and the Equilibrium State

Chemical Kinetics

Reactions of Organic Phosphorus Compounds

Carbohydrates

Nucleic Acids

Bioenergetics and Cellular Respiration

ATP, ADP, and AMP are nucleotides consisting of the purine base adenine, the five-sided sugar ribose, and 3,2, or 1 phosphate groups respectively.

The transfer of a phosphate group is called phosphorylation. The most common phosphorylation reaction involves the addition of an inorganic phosphate group to ADP, forming ATP, the reverse of hydrolysis.

While ATP hydrolysis is very favorable thermodynamically, the process is very slow in the absence of a catalyst. ATP is kinetically stable. Kinetic stability is essential for the capacity of a biological system to control the flow of free energy by enzyme catalysis.

ATP is the principle immediate donor of free energy in biological systems. Many endergonic biochemical processes are coupled to the exergonic cleavage of ATP. The two primary reasons for the high negative free energy change corresponding to ATP hydrolysis are electrostatic repulsion and resonance stabilization. The high negative free energy change associated with electrostatic repulsion arises due to the fact that ATP is a strong anion, with a -4 total formal charge distributed along the three phosphoryl groups. The hydrolysis of the molecule is accompanied by the separation of like charge, a decrease in electrical potential energy (internal energy, enthalpy, free energy). Picture the three phosphate groups of ATP as a compressed spring. Furthermore, the products of cleavage enjoy greater resonance stabilization than the single molecule. Keep in mind that the energy is not located in the bonds linking the phosphate groups themselves but is a property of the difference between the initial and final states of the system.




Chemical Thermodynamics and the Equilibrium State

Bioenergetics and Cellular Respiration

Because the overall free-energy change for coupled reactions equals the sum of the individual free energy changes, a thermodynamically unfavorable reaction, such as a typical biochemical processes, can be driven by a thermodynamically favorable reaction coupled to it, such as the cleavage of ATP. The activities of many protein enzymes are coupled to ATP hydrolysis. However, a few other compounds in biological systems have to capacity to carry out phosphate hydrolysis with even greater negative free energy than ATP, such as phosphoenolpyruvate, acetyl phosphate, and phosphocreatine, which means that these substances have the ability to transfer a phosphate group to ADP. ATP releases its free energy coupled to biochemical processes and recharges coupled to the hydrolysis of such molecules as phosphoenolpyruvate.







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