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44 Cards in this Set

  • Front
  • Back

Metabolism

Either all or a specific set of chemicals reactions occurring at the cellular level.

How is cell structure maintained?

Using organic molecules as building blocks.

Factors that determine the fate of a chemical reaction:

direction


rate

kinetic energy

energy associated with motion



potential energy

energy an object possesses due to its structure or location.

First Law of Thermodynamics

energy cannot be created or destroyed, but can be transformed

Second Law of Thermodynamics

as energy is transformed, it is converted to a lower quality form. The entropy (degree of disorder) in the system is increased.

Symbol for total energy

H

Symbol for usable energy

G

Symbol for unusable energy

TS

Equation for total energy

usable energy (G) + unusable energy (TS) = total energy (H)

Symbol for change in free energy

ΔG

Determines direction of reaction

change in free energy (ΔG)



Exergonic Reaction

- negative free energy change


- spontaneous


- products have less free energy than reactants


- no additional energy needed

Endergonic reaction

- positive free energy change


- not spontaneous


- reactants have more free energy than the products


- additional energy needed



ATP



- energy-carrying molecule


- not a fuel molecule

How do exergonic and endergonic reactions work together?

energy released by exergonic reactions supplies energy for endergonic reactions.

Catalyst

speeds up chemical reaction rate

Types of catalysts

- enzymes


- ribosomes

How do enzymes catalize

- provide bonding/active sites for substrates


- provide bonding sites that stress chemical bonds



Activation energy

- energy needed to start chemical reaction


- gets reactants to active site


- more enzymes available, less activation energy needed

Active Site/Bonding Site

region of enzyme where substrates bind

Factors that alter the rates of enzyme-catalyzed reactions

- temperature


- pH


- inhibitors


- substrate concentration


- enzyme concentration


- cofactors


- coenzymes

Temperature

- enzymes are optimally active within narrow (high) temp. range



pH

- enzymes are optimally active at a pH of 2

Inhibitors

- prevent binding of substrates to enzymes


- more inhibitors means fewer products at a time

Types of Reversible Inhibitors

- Competitive inhibitors


- Noncompetitive inhibitors



Competitive inhibitors

- bind nonvalently to the active site of an enzyme.



Noncompetitive inhibitors

- bind noncovalenty to an allosteric site of an enzyme

Irreversible inhibitors

- bind covalently to the active site of an enzyme



Substrate concentration

- higher substrate concentration = higher product formation

Enzyme concentration

- higher enzyme concentration = more product formation

Cofactors

- inorganic molecules that bind temporarily to an enzyme


- help facilitate reactions

Coenzymes

- organic molecules that bind temporarily to an enzyme


- NAD and FAD

Redox Reactions

- Oxidation


- Reduction



Oxidation

Removal of electrons from an tom or molecule

Reduction

addition of electrons to an atom or molecule

Redox Reaction

when electrons are removed from one atom or molecule are immediately transferred to another atom or molecule.

Energy intermediate

molecules that store energy that may be used to drive endergonic reactions.

How do cells use NADH and FADH2?

- oxidation of these two is exergonic


- oxidation of these two can be used to make ATP

Regulation of Metabolic Pathways

- gene regulation


- cellular regulation


- biochemical regulation

Gene regulation

- enzymes encoded by genes


- turning genes on and off regulates pathways

Cellular regulation

cell-signaling molecules (like hormones) activate enzymes.

Biochemical regulation

noncovaltent bonding of inhibitors to enzymes.