Chapter 4 Flashcards
Thermodynamics
Study for energetics of chemical reactions.
Heat energy
movement of molecules
Potential energy
energy stored in chemical bonds
Entropy
(S) increase in disorder
Enthalpy
(H)
Gibbs free energy
ΔG = ΔH-TΔS
ΔG’s changes
ΔG increases with increasing ΔH (bond energy) and decreases with increasing entropy.
The change in Gibbs free energy of a reaction determines
whether the reaction is favorable (spontaneous, ΔG negative) or unfavorable (non spontaneous, ΔG positive)
Exergonic (ΔG)
energy exists the system
Endergonic (ΔG)
only occur if energy is added
ΔH <0
Liberates Heat; exothermic
ΔH>0
Require input of heat; endothermic
The signs of thermodynamically quantities are assigned from the point of view
of the system, not the surrounding do the universe
Spontaneous means
that a reaction may proceed without additional energy input, but is says nothing about the rate of the reaction
ΔG does not depend on
the pathway a reaction takes or the rate of the reaction; it is only a measurement of the difference in free energy between reactants and products
Chemical Kinetics
study of reaction rates
Activation Energy (Ea)
energy required to produce the transient intermediate.|This barrier prevents many reactions from proceeding even though the ΔG for the reaction may be negative
Transition State (TS)
exists for a short time either moving forward to form product or breaking back down into reactants
Catalyst
lowers the Ea of a reaction without changing the ΔG.|Lowers the Ea by stabilizing the TS, making its existence less thermodynamically favorable. (enzymes are catalysts)
Thermodynamically unfavorable reactions in the cell can be driven forward by
reaction coupling
Reaction coupling
where one very favorable reaction is used to drive an unfavorable on. Free energy changes are additive.
ATP hydrolysis
causes a conformational change in protein. Used to power energy
During ATP hydrolysis there is a transfer of phosphate
from ATP to a substrate
One reaction in a test tube
the enzyme is a catalyst with a kinetic role only. It influences the rate of the reaction, but not the outcome
Many “real life” reactions in the cell
enzyme controls outcomes by selectively promoting unfavorable reactions via reaction coupling
Enzymes are proteins that
must fold into specific three-dimensional structures to act as
catalyst
Active site
the region in the enzyme’s
three-dimensional structure that is directly involved in catalysis