Chapter 5 - Ground Rules Of Metabolism Flashcards
(49 cards)
Energy
Capacity to do work.
Kinetic Energy
Energy of Motion
First Law of Thermodynamics
Energy cannot be created or destroyed.
Entropy
Tendency of energy to spontaneously disperse.
Increases until heat is evenly distributed throughout system.
Second Law of Thermodynamics
Entropy tends to increase.
Energy tends to spread out spontaneously.
Related to Chem. Bonding in that covalent bonds between atoms decrease movement, thus decreasing entropy.
Potential Energy
Stored Energy.
Stored in chemical bonds.
Resists entropy.
Reaction
Any process by which a chemical change occurs.
Reactants
Molecules entering a reaction.
Products
Molecules remaining at reaction’s end.
Free Energy
Amount of energy available to do work. Bond energy(energy required to break a bond)/entropy contribute to free energy.
Endergonic Reactions
Reactants have less free energy that products.
Do not proceed without an energy input.
Exergonic Reactions
Reactants have greater free energy than products.
End with net release of free energy.
Cells run these to access free energy of molecules.
Example: Aerobic Resp. (converts glucose + oxygen = CO2 and H2O for a net energy output)
Why doesn’t Earth burst into flame?
The molecules of life release energy when combined with Oxygen.
Example: Wood is cellulose (MOL). A spark initiates a reaction converting cellulose and oxygen in air to water and carbon dioxide. The reaction is exergonic, releasing enough energy to continue the same reaction with cellulose and oxygen molecules, causing a fire to keep burning following being lit.
Earth does not burst into flame because energy is required to break the bonds in any reaction.<– Activation Energy
Activation Energy
Minimum amount of energy required to start a chemical reaction.
Analagous to a hill that rewctants must climb before coasting toward the products.
Different amounts of activation energy are required to start endergonic and exergonic reactions. Amount varies with reaction.
ATP (Adenosine Triphosphate)
Functions as energy carrier by accepting energy given off by exergonic reactions and delivering it to endergonic reactions.
“Currency” of cell’s energy economy.
Nucleotide with 3 phosphate holding immense energy in their bonds. When phosphates of ATPs are transferred to each other, energy is moved along with the phosphate.<–Phosphorylation
Phosphorylation
The transfer of a phosphate group from an ATP to another molecule. This is the “net energy input” required in endergonic reactions.
ATP/ADP Cycle
Cycle of using and replenishing ATP.
When ATP loses a phosphate, ADP forms. ATP reforms when ADP binds to a phosphate in an endergonic reaction.
Catalysis
Process in which an enzyme makes a reaction run much faster than it would on its own.
Enzyme is unchanged by participating in reaction.
Most enzymes are proteins; some are RNAs. Each kind recognizes specific reactants (substrates) and alters them in a specific way.
Substrate
Specific reactants in a reaction.
Altered in a specific way by enzymes.
Enzymes are so specific because of their active sites.
Active Site
Pockets where substrates bind and reactions proceed.
Complementary in size, shape, polarity, and charge to substrate of enzyme. <–reason for specificity of enzymes relative to substrates.
Transition State
State where substrate bonds reach their breaking point and reaction runs spontaneously to product.
Lowering of Activation energy causes change bringing on transition state.
HOW TO LOWER ACTIVATION ENERGY:
Helping substrates get together by binding at active site(increases chance of substrates reacting with each other)
Orienting substrates favoring reaction (positioning bound substrates at active site aligns them for reaction)
Inducing fit between molecule and substrate(since active site isn’t perfectly complementary to substrate, interaction with substrate causes enzyme to change shape to better fit the substrate. Improved fit results in stronger bond, or bring on the transition state better/faster.
Shutting out water molecules:
Metabolism occurs in water-based fluids, but water can sometimes interfere with certain reactions, so active sites of those enzymes participating in those reactions repel water.
HOW TO LOWER ACTIVATION ENERGY:
Helping substrates get together by binding at active site(increases chance of substrates reacting with each other)
Orienting substrates favoring reaction (positioning bound substrates at active site aligns them for reaction)
Inducing fit between molecule and substrate(since active site isn’t perfectly complementary to substrate, interaction with substrate causes enzyme to change shape to better fit the substrate. Improved fit results in stronger bond, or bring on the transition state better/faster.
Shutting out water molecules:
Metabolism occurs in water-based fluids, but water can sometimes interfere with certain reactions, so active sites of those enzymes participating in those reactions repel water.
Effects of tempterature, pH, and salinity on enzymes
Temp: adding heat energy boosts free energy, bringing a reaction closer to its activation energy. More temp increases with reaction rate, but too high temp makes an enzyme denature.
pH: most enzymes in human body tolerate optimal pH between 6 and 8 (blood is 7.35). Some enzymes can tolerate harsher conditions(pepsin in stomach acid; pH 2)
Salinity: too much or too little salt disrupts H bonding holding an enzyme in 3-D shape.
Cofactors
Atoms or molecules (EXCLUDING PROTEINS) that assoc. with enzymes and are necessary for their function. Some are metal ions.
Organic molecules that are cofactors: coenzymes
Example: Catalyse (enzyme). (also an antioxidant)
Has 4 hemes. Iron atom at center of each heme is cofactor, pulling on substrate’s electrons, bringing on trans. state.