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BiochemFinalLogan3
Reveiw of Biochemistry I part 3
| Question | Answer |
|---|---|
| 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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