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Reveiw of Biochemistry I part 3

Bond dissociation Energy The energy required to break or make a chemical bond.
Activation Energy The minimum energy required by reacting molecules.
Spontaneous reactions Exothermic, ∆H is greater than the Ea
Non-spontaneous reactions Endothermic, ∆H is less than the Ea
If Ea is increased what happens to the number of particles? The number decrease
If Ea is increased what happens to the reaction rate? The rate decreases
If the Ea is decreased, what happens to the reaction rate? The rate is increased!
Is the effect of a change in Ea on the reaction rate a linear or exponential change? Exponential!
Catalysts Lower the Ea, speeds up reaction, can be used to regulate kinetics.
Vmax The maximum concentration of a substrate where it will have an effect on the velocity.
Steady State Approximation The ES Complex tends to decay as fast as it forms.
Michaelis- Menten Constant Utilized as a measure of the affinity of an enzyme for its substrate. Predicts how velocity is related to [S] if [enzyme] is held constant.
If you have a smaller Km, what can you tell abou the enzyme, and reaction rate? More effective enzyme, faster reaction rate.
Enzyme Biological catalysts.
Lineweaver-Burke Equation A linear presentation of the kinetic response for an enzyme catalyzed process.
Competitive inhibition A molecule (inhibitor) chemically resembles the substrate, so the enzyme gets “confused.” This slows down the rate of reaction because less enzyme is reacting with the substrate.
Why is it called competitive inhibition? The inhibitor is occupying the catalytic sites, therefore there is competition for the catalytic sites.
What do you do to reverse competitive inhibition Increase [S], causing a shift to the right towards the ES complex.
Non-Competitive Inhibition A molecule (inhibitor) reacts with an area remote from the catalytic site. This permanently reduces Vmax.
What is a characteristic of a NC inhibitor? Heavy metal ions.
Where does the NC inhibitor bind to? Non-catalytic sites.
How can you reverse NC inhibition? Add Chelating Agents
If there is a change in Vmax, what sort of inhibition is the process? Non Competitive
Irreversible Inhibition A rapid process that is deleterious to the gross organism.
Adenisine Tri Phosphate (ATP) A nucleotide, that contains an N - base, a pentose and phosphate groups.
ATP + Water = ? ADP and Inorganic phosphate
What is the ∆G of hydrolysis of ATP? -31 KJ
What is Gibbs Free Energy (∆G) A measure of the maximum magnitude of the net useful work that can be obtained from a reaction.
What does it mean of ∆G is negative? Spontaneous reaction/ product favored
What does it mean if ∆G is positive? Non-spontaneous reaction/ reactant favored.
1st law of thermodynamics The energy change of a process is equated to the heat evolved and the work done by that process. ∆E = Q + W
2nd law of thermodynamics To order a random system, work must be done. The universe tends towards disorder.
Entropy (∆S) The measure of randomness or disorder in a system.
What is the relationship between entropy and probability of a system? the more random = the more probable (and the more spontaneous)
Free energy change of a process ∆G = ∆H - T∆S
Cellular Energy Conversions The conversion of reducing power to phosphate power (ATP)
Outer Membrane of mitochondria Mostly permeable
Inner Membrane of mitochondria Difficult to permeate, defines matrix, uses pumps and gates.
Pyridine- Linked Dehydrogenase An enzyme (therefore, a protein), NADH or NADPH (dinucleotide active forms of Niacin)
Flavin-Linked Dehydrogenase An enzyme (protein), FAD or FMN – co factors, Manifestations of Riboflavin
Cytochromes Organo-metallic containing polypeptides. Chelating Agents.
What is the typical structure of a cytochrome? Heme structure - a ring with coordinate covalent bonding.
Non- Heme Iron Proteins • A polypeptide with iron, but no organic substructure (heme) • The iron is locked in by coordinate covalent bonds
Co-Enzyme Q • Not a polypeptide • Can be a redox • Found in all aerobic organisms
NADH + H+ + ½ O2 → NAD+ + H2O Electron Transport
What is the gibbs free energy of electron transport? -220 kJ
What is the ultimate electron acceptor? OXYGEN!!!
Chemiosmotic Hypothesis For oxidative phosphorylation to occur, the mitochondrial membrane must be continuous and it must have a matrix or it cannot create a gradient!
What is the effect of uncouplers? make the mitochondrial membrane porous to protons → continue to burn fuel, but produce no ATP (increased inefficiency)
If you run out of ATP and O2 consumption stops, what can you add to restart O2 consumption? ADP
What happens if you add rotenone to the system? O2 is no longer being consumed.
What can you add to reverse the effects of rotenone? Succinate
What does oligomycin do to the system? Stops consumption of O2
What can be done to reverse the effects of oligomycin? 2,4 DNP
What is the most permanent way to stop consumption of oxygen? add Cyanide.
Created by: eane220

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