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47 Cards in this Set

  • Front
  • Back
Kinetic & Potential Energy
Kinetic- energy of motion
Potential- capacity to do work owing to position or state.
KE of randomly moving particles. Can't perform work.
Heat energy
Flows from an object with a her temperature to one with a lower. This can perform work.
Entropy (S)
- Measure of disorder or randomness
- usuable energy has low (S)
- disorganized energy- high (S).
- Sum of all the chemical activities taking place in an organism.
- Consists of many intersecting series of chemical reactions or pathways
Types of metabolism
Anabolism & catabolism
-Includes the various pathways in which complex molecules are synthesized from simpler substances, such as the linking of amino acids to form proteins.
Includes the pathways in which larger molecules are broken down into smaller ones, such as the degradation of starch to form monosaccharides.
-Involves an overall release of energy, which powers anabolic pathways.
Enthalpy (H)
-Total potential energy of a system.
-Referred to as the heat content of the system.
Free Energy (G)
Amt. of energy available to do work under the conditions of a biochemist reaction.
-only energy to do cell work.
1st law of thermodynamics
Energy cannot be created or destroyed but can be transferred or converted from one form to another.
2nd law of thermodynamics
When energy is converted from one form to another, some usuable energy is converted into heat that disperses into the surrondings.
Relationship b/t enthalpy, free energy, and entropy.
<>G= <>H - T<>S
EQN= entropy increases, free energy decreases.
G= H- TS
Exergonic rcns
rcns that proceed w/o an input of energy from outside. "Downhill".negative G
Endergonic rcn
rcn where there is a gain in free energy. require an input of energy. uphill rcns. positive <>G.
Coupled rcns
the thermodynamically favorable exergonic rcn provides the energy required to frive the thermodynamically unfavorable endergonic rcn.
ATP stands for?
Adenosine triphosphate
Holds readily available energy for short periods. ATP is the energy currency of the cell.
ATP's structure
ATP is a nucleotide consisting of three parts: adenine (nitrogen base); ribose (5-C sugar); 3 phosphate groups
adenosine diphosphate. when terminal phosphate is removed.
inorganic phosphate. hi-energy of ATP.
phosphorylation rcn
phosphate group is transferred to some other compound. That compound becomes energized.
Link b/t exergonic & endergonic
ATP occupies an intermediate position. exergonic-catabolic, endergonic-anabolic.
oxidationa & reduction
oxidation-substances lose e-
reduction- substance gains e-

-both called redox rcns b/c they occur simultaneously.
-The substance that becomes oxidized, gives up electrons (energy), the substance that reduces, receives energy as it gains electrons.
electrons & free energy
an electron loses free energy as it is transferred from one acceptor to the next.
acceptor molecule. when reduced, it stores large amts. of free energy, and becomes NADH.
NUcleotides when accept H+ atoms become: NADPH & FADH2
proteins that accept e-, and not H+ atoms.
Energy of activation
(Ea) energy required to break existing bonds and begin the reaction.
enzyme & Ea
Enzymes lower Ea, but no effect on the overall free energy change. speed up rcn rates.
Enzyme substrate complex
Substrate binds to the enzyme at the active site forming an enzyme-substrate complex.
Induced fit
The binding causes a change in the enzymes's shape. The change in shape lowers Ea.
Enzyme "helpers". Nonprotein substances.
Kinds of cofactors
(1) Inorganic ions. Mg, Ca
(2) Nonpolypeptide organic molecules. Coenzymes. vitamins.
Optimal temperature
Rate of rcn is fastest at a certain temp. Hi temp denature enzymes. H+ bonds break. activity not regained when enzyme is cooled.
Optimal pH
Changes in charge affect the ionic bonds that contribute to tertiary & quartenary, thus changing shape.
Metabolic pathway
When the product of one ES complex becomes the substrate for another. A->B->C
How do cells regulate enzyme activity?
- by controlling amt. of enzyme produced
- by controlling amt. of substrate produced.
- feedback inhibiton
Feedback inhibition
The formation of a product inhibits an earlier rcn in the sequence
Allosteric enzymes
Have an allosteric site, which allosteric regulators bind to.
Reversible inhibtion
when an inhibitor forms weak chemical bonds with the enzyme. Can be competitive or non-competitive
Competitive inhibition
the inhibitor competes with the substrate for binding to the active site. Occupies the site temporarily, and doesn't damage the enzyme.
Non-competitive inhibtion
the inhibitor bindsw w/ th enzyme at a site other than the active site. This inactivates the enzyme by altering its shape.
Irreversible inhibition
an inhibitor permanetly inactivates the enzyme when it combines with one of its functional groups.
allosteric inhibtion
non-competitive inhibition
ireeversible enzyme inhibitors