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BIOENERGETICS : The role of ATP

Learning dynamics / energy changes reactions in biochemistry (chemical reaction


organisms in)
Biomedical importance
Biologic systems are isothermic processes and use chemical energy to power living
processes.
Free Energy is the useful energy in a system
Gibbs change in free energy (G) is the portion of the total energy change in a
system that is available for doing work and is also known a chemical potential.
1. First Law of Thermodynamics
Total energy of system, including its surroundings, remains constant.
Within the closed system, energy is neither lost nor gained during any change,
energy may be transferred into another form of energy.
For example : energy can be transfered into heat, electrical, radiant, and mechanical
energy
2. Second law of thermodynamics
Total entropy of a system must increase if a process is to occur spontaneously.

G = H - TS
G = E - TS
G (--)

: proceeds spontanously with loss of energy, called exorgenic

G (+)

: proceeds unspontanously with gain of energy, called endorgenic.


Endorgenic process must be coupled with exorgenics

G = 0
0

: at quilibrium and no net change takes place

G =0

: standard free energy changes in concentration of reactions 1 mol/L and PH 7

G >G0

: depending on the concentrations of various reactants, including the solvent,


various ions, and proteins.

Enzyme only speed up the attaintment of eqilibrium, never alters the final
concentration of the reactants.
Exorgenic process proceed by coupling to eergonic process

An endergonic can not exist independently, it must be a component of a coupled endo-exo


system

Exergonic reactions term of catabolism : breaks of oxidation of molecules


Endorgenic reactions term of anabolism : build up substance

An alternative method of coupling an exergonic to an endorgenic process is to synthesize a


compound of high-energy potential by transfered energy from exergonic to endorgenic. The
intermediate carrier is ATP.
High energy phosphates are designed by ~
Group attached to the bond on transfer to an appropriate acceptor, results in transfer of
larger quantity of free energy
ATP : ~~~
ADP : ~~
AMP : ~

3 major sources of ~ :
1. Oxydative phosphorylation
This process is the greatest quantitative source of ~ in aerobic organisms
2. Glycolysis
A net formation of two ~. Results from lactate from one molecule of glucose
generated in two reactions, pyruvate kinase and phospoglycerate kinase.
3. Citric Acid Cycle
one ~ is the cycle at the succinate thiokinase step.
"High Energy" Bonds
The structure of ATP is shown below. Anhydride bonds (in red) link the terminal
phosphates. Phosphoanhydride bonds (formed by splitting out water between two
phosphoric acids or between a carboxylic acid and a phosphoric acid) tend to have a large
negative DG of hydrolysis, and are thus said to be "high energy" bonds. It is important to
realize that the bond energy is not necessarily high, just the free energy of hydrolysis.

Energy coupling

A spontaneous reaction may drive a non-spontaneous reaction.

Free energy changes of coupled reactions are additive.

Examples of different types of coupling:


A. Some enzyme-catalyzed reactions are interpretable as two coupled half-reactions, one
spontaneous and the other non-spontaneous. At the enzyme active site, the coupled
reaction is kinetically facilitated, while the individual half-reactions are prevented. The free
energy changes of the half-reactions may be summed, to yield the free energy of the
coupled reaction.
For example, in the reaction catalyzed by the Glycolysis enzyme Hexokinase, the two halfreactions are:

ATP + H2O ADP + Pi .................. DGo' = -31 kJoules/mol

Pi + glucose glucose-6-P + H2O ... DGo' = +14 kJoules/mol

Coupled reaction: ATP + glucose ADP + glucose-6-P .. DGo' = -17 kJoules/mol


The structure of the enzyme active site, from which water is excluded, prevents the
individual hydrolytic reactions, while favoring the coupled reaction.
B. Two separate enzyme-catalyzed reactions occurring in the same cellular
compartment, one spontaneous and the other non-spontaneous, may be coupled
by a common intermediate (reactant or product).
A hypothetical, but typical, example involving pyrophosphate:

enzyme 1: A + ATP B + AMP + PPi ....DGo' = +15 kJ/mol

enzyme 2: PPi + H2O 2 Pi ....................DGo' = 33 kJ/mol

Overall: A + ATP + H2O B + AMP + 2Pi ... DGo' = 18 kJ/mol


Pyrophosphate (PPi) is often the product of a reaction that needs a driving force. Its
spontaneous hydrolysis, catalyzed by Pyrophosphatase enzyme, drives the reaction for
which PPi is a product. For an example of such a reaction, see the discussion
of cAMP formation below.