Reveiw of Biochemistry I part 3
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| Bond dissociation Energy | The energy required to break or make a chemical bond.
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| Activation Energy | The minimum energy required by reacting molecules.
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| Spontaneous reactions | Exothermic, ∆H is greater than the Ea
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| Non-spontaneous reactions | Endothermic, ∆H is less than the Ea
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| If Ea is increased what happens to the number of particles? | The number decrease
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| If Ea is increased what happens to the reaction rate? | The rate decreases
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| If the Ea is decreased, what happens to the reaction rate? | The rate is increased!
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| Is the effect of a change in Ea on the reaction rate a linear or exponential change? | Exponential!
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| Catalysts | Lower the Ea, speeds up reaction, can be used to regulate kinetics.
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| Vmax | The maximum concentration of a substrate where it will have an effect on the velocity.
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| Steady State Approximation | The ES Complex tends to decay as fast as it forms.
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| 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.
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| If you have a smaller Km, what can you tell abou the enzyme, and reaction rate? | More effective enzyme, faster reaction rate.
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| Enzyme | Biological catalysts.
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| Lineweaver-Burke Equation | A linear presentation of the kinetic response for an enzyme catalyzed process.
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| 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.
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| Why is it called competitive inhibition? | The inhibitor is occupying the catalytic sites, therefore there is competition for the catalytic sites.
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| What do you do to reverse competitive inhibition | Increase [S], causing a shift to the right towards the ES complex.
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| Non-Competitive Inhibition | A molecule (inhibitor) reacts with an area remote from the catalytic site. This permanently reduces Vmax.
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| What is a characteristic of a NC inhibitor? | Heavy metal ions.
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| Where does the NC inhibitor bind to? | Non-catalytic sites.
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| How can you reverse NC inhibition? | Add Chelating Agents
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| If there is a change in Vmax, what sort of inhibition is the process? | Non Competitive
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| Irreversible Inhibition | A rapid process that is deleterious to the gross organism.
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| Adenisine Tri Phosphate (ATP) | A nucleotide, that contains an N - base, a pentose and phosphate groups.
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| ATP + Water = ? | ADP and Inorganic phosphate
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| What is the ∆G of hydrolysis of ATP? | -31 KJ
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| What is Gibbs Free Energy (∆G) | A measure of the maximum magnitude of the net useful work that can be obtained from a reaction.
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| What does it mean of ∆G is negative? | Spontaneous reaction/ product favored
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| What does it mean if ∆G is positive? | Non-spontaneous reaction/ reactant favored.
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| 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
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| 2nd law of thermodynamics | To order a random system, work must be done. The universe tends towards disorder.
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| Entropy (∆S) | The measure of randomness or disorder in a system.
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| What is the relationship between entropy and probability of a system? | the more random = the more probable (and the more spontaneous)
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| Free energy change of a process | ∆G = ∆H - T∆S
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| Cellular Energy Conversions | The conversion of reducing power to phosphate power (ATP)
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| Outer Membrane of mitochondria | Mostly permeable
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| Inner Membrane of mitochondria | Difficult to permeate, defines matrix, uses pumps and gates.
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| Pyridine- Linked Dehydrogenase | An enzyme (therefore, a protein), NADH or NADPH (dinucleotide active forms of Niacin)
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| Flavin-Linked Dehydrogenase | An enzyme (protein), FAD or FMN – co factors, Manifestations of Riboflavin
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| Cytochromes | Organo-metallic containing polypeptides. Chelating Agents.
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| What is the typical structure of a cytochrome? | Heme structure - a ring with coordinate covalent bonding.
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| Non- Heme Iron Proteins | • A polypeptide with iron, but no organic substructure (heme)
• The iron is locked in by coordinate covalent bonds
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| Co-Enzyme Q | • Not a polypeptide
• Can be a redox
• Found in all aerobic organisms
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| NADH + H+ + ½ O2 → NAD+ + H2O | Electron Transport
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| What is the gibbs free energy of electron transport? | -220 kJ
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| What is the ultimate electron acceptor? | OXYGEN!!!
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| 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!
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| What is the effect of uncouplers? | make the mitochondrial membrane porous to protons → continue to burn fuel, but produce no ATP (increased inefficiency)
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| If you run out of ATP and O2 consumption stops, what can you add to restart O2 consumption? | ADP
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| What happens if you add rotenone to the system? | O2 is no longer being consumed.
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| What can you add to reverse the effects of rotenone? | Succinate
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| What does oligomycin do to the system? | Stops consumption of O2
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| What can be done to reverse the effects of oligomycin? | 2,4 DNP
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| What is the most permanent way to stop consumption of oxygen? | add Cyanide.
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