7664318137 | Metabolism | totality of an organism's chemical reaction emergent property of life that arises from orderly interactions between molecules | 0 | |
7664327609 | Metabolic Pathway | begins with specific molecule which is then altered into a series of defined steps, resulting in a certain product. Each step is catalyzed by a specific enzyme | ![]() | 1 |
7664339739 | Metabolic pathway controls | starting molecule and stopping molecule control flow of automobile traffic, mechanisms that regulate enzymes balance metabolic supply and demand | 2 | |
7664349141 | Catabolic Pathways | degradation process some metabolic pathways release energy by breaking down complex molecules to simpler compounds "downhill" | ![]() | 3 |
7664372347 | Catabolic Pathways release | energy that was stored in organic molecules. Becomes available to do work of cell | 4 | |
7664381773 | Anabolic pathways | consume energy to build complicated molecules from simpler ones; sometimes called Bio synthetic pathways ex: protein synthesis "uphill" | ![]() | 5 |
7664405159 | Bioenegetics | study of how energy flows through living organisms | 6 | |
7664408174 | Energy | capacity to cause change | 7 | |
7664414486 | kinetic Energy | relative motion of object | 8 | |
7664421941 | Heat/thermal energy | kinetic energy associated with random movement of atoms/molecules | 9 | |
7664425800 | Potential energy | not moving but can still possess energy due to location/structure | ![]() | 10 |
7664434228 | Chemical Energy | potential energy available for release in chemical reaction glucose increases in chemical energy | 11 | |
7664441166 | Thermodynamics | study of energy transformation that occurs in a collection of matter | 12 | |
7664452556 | System | matter under study | 13 | |
7664455081 | Surrounding | everything beside system | 14 | |
7664457996 | Isolated System | unable to exchange energy/matter with surroundings | 15 | |
7664461283 | open system | exchange energy/matter with surroundings | 16 | |
7664472373 | First law Of Thermodynamics Principle of Conservationo f energy | energy can be transferred/transformed but cannot be created or destroyed | 17 | |
7664483234 | Second Law of Thermodynamics | during every energy transfer/transformation some energy is unavailable to do work which results in a loss of heat | 18 | |
7664489981 | Entropy | a measure of disorder evident in physical disintegration increase disorder by releasing heat | 19 | |
7664505531 | Every energy transfer/transformation increases... | entropy of universe | 20 | |
7664523797 | Bear increases entropy | by eating a fish increasing disorder of surroundings by producing heat and small molecules like carbon dioxide | 21 | |
7664538234 | If a process increases entropy it can... | occur without input of energy | 22 | |
7664538235 | Spontaneous Process | occurs without input of energy energetically favorable ex: water flowing downhill | 23 | |
7664549739 | biological Order and Disorder | living systems increase entropy of surroundings create ordered struuter but also take ordered things and make them less ordered ex:animals eating | 24 | |
7664561535 | Entropy of a particual system can decrease as long as | total entropy of universe increases | 25 | |
7664567187 | Free Energy Change | tells us whether a reaction occurs spontaneously or not Triangle G | 26 | |
7664574751 | Change in Free energy equals | change in heat minus temperature and change in entropy | 27 | |
7664580958 | If Change in Free energy is negative | it is spontaneous either change in heat is negative or temperature times change in entropy is positive (system gives up order and increases S) | 28 | |
7664608305 | Every spontaneous process decreases... | system's free energy | 29 | |
7664612887 | When change in free energy is positive or zero | it is never spontaneous | 30 | |
7664617351 | Triangle G equals | G final state minus G initial state | 31 | |
7664623437 | free energy | measure of system's instability or its tendency to change to a mere stable state | 32 | |
7664633540 | Unstable system (more free energy) tend to... | change into a stable system (decrease in free energy) | 33 | |
7664640417 | Equilibrium | another term that describes state of maximum stability free energy of mixture of reactants and products decreases | 34 | |
7664664749 | When reaction is pushed away from Equilibrium what happens to free energy | increases | 35 | |
7664675243 | A system at equilibrium cannot | spontaneously change which means it won't work and cell will die | 36 | |
7664686509 | A process is spontaneous and will work when... | it is moving toward equilibrium | 37 | |
7664689069 | Exergonic reaction | (energy outward) proceeds with a net release of free energy loses free energy so the change inf free energy is negative | ![]() | 38 |
7664708855 | Denaturation | misshaping enzyme over a particular temperature it denatures | 39 | |
7664726385 | Breaking bonds needs | energy | 40 | |
7664726386 | Endergonic reaction | absorbs free energy from surroundings stores free energy in molecules increases G (change in endergonic reaction is positive=non-spontaneous) "uphill" | ![]() | 41 |
7664735614 | Magnitude of change in free energy is.. | quantity of energy required to drive reaction | 42 | |
7664758806 | What keeps cell from reaching equilibrium | constant flow of materials key is that product cannot accumulate but becomes a reactant in the next step | 43 | |
7664769010 | ATP powers cellular work by | coupling exergonic reactions to endergonic reactions | 44 | |
7664778161 | 3 main types of work Cell performs | chemical, transport, mechanical | 45 | |
7664781322 | Chemical Work | pushing of endergonic reactions that wouldn't occur spontaneously | 46 | |
7664797477 | Transport Work | pumping of substanes across membranes against direction of spontaneous movemetn | 47 | |
7664801601 | Mechanical Work | such as beating of cilia, contraction of muscle cells movement of chromosomes during cell reproduction | 48 | |
7664811510 | Energy coupling | key feature in way cell manages energy resources, use of exergonic process to drive endergonic one ATP responsible for mediating energy coupling | 49 | |
7664825631 | ATP (Adenosine triphosphate) | contains sugar ribose with nitrogenous base and a chain of three phosphate groups | ![]() | 50 |
7664840958 | Bonds between phophate groups can be broken by | hydrolysis | 51 | |
7664843362 | Hydrolysis | Breaking down complex molecules by the chemical addition of water | 52 | |
7664856083 | Lose of phosphate group is | spontaneous | 53 | |
7664860438 | Cell conditions are not... | standard conditions | 54 | |
7664865107 | ATP plus Water means | increase energy compared to products change to a state of lower free energy | 55 | |
7664901762 | Shivering uses | ATP hydrolysis to release heat | 56 | |
7664909917 | generation of heat is____in cells | ineffective and dangerous | 57 | |
7664916139 | What are the conditions needed for two reactions to be coupled | if the change in free energy of endergenic is less than the amount of energy released by ATP hydrolysis means overall reaction is exergonic | 58 | |
7664955541 | Phosphorylated intermediate | recipient with phosphate group covalently bonded to it more reactive means less stable than original molecule | 59 | |
7664969738 | Transport and Mechanical work powered by | hydrolysis of ATP leads to change of protein and ability to bind to another | 60 | |
7664976937 | ATP is what type of energy? | renewable, can be regenerated by addition of phosphate to ADP | 61 | |
7664979933 | ATP Cycle | shuttling of inorganic phosphate and energy couples cell's energy yielding exergonic breakdown reactions in cell ATP-> releases energy-> ADP+P-> energy required from exergonic run->ATP | 62 | |
7665001406 | Enzymes speed up metabolic reactions by | lowering energy barriers | 63 | |
7665014239 | Enzyme | macro-molecule that acts as a catalyst | 64 | |
7665021505 | Catalyst | chemical agent that speeds up reaction without being consumed | 65 | |
7665027596 | The Activation Energy Barrier | changing one molecule to another by contorting starting molecule into highly unstable state before reaction must absorb energy from surroundings to contort | 66 | |
7665045713 | Activation Energy/free energy of activation | Ea initial investment of energy for starting reaction by contorting reactant molecules so bond can break amount of energy needed to push reactions to top of energy barrier so downhill can begin often supplied in form of heat | 67 | |
7665066976 | Transition State | when molecules ave absorbed enough energy for bonds to break | 68 | |
7665074666 | Activation Energy provides | barrier that determines rate of reaction reactants must absorb enough energy to reach top of EA barrier before reaction can occur | 69 | |
7665079794 | How Enzymes Lower Ea Barrier | catalyzes reaction by lowering Ea barrier and cannot change the change of free energy for a reaction | 70 | |
7665103396 | Substrate | reactant an enzyme acts on | 71 | |
7665112405 | Enzyme substrate complex | enzyme binds to its substrates | ![]() | 72 |
7665120391 | Active Site | region where catalysis occurs formed by only a few enzyme's amino acids | 73 | |
7665126702 | Induced fit | brings chemical groups of active site into positions that enhance their ability to catalyze chemical reactions | 74 | |
7665133004 | Catalysis in Enzyme's Active site | ![]() | 75 | |
7665163632 | enzyme can catalyze either fowrad or reverse depending on | which direction has a negative change in free energy | 76 | |
7665174706 | How do enzymes decrease Active Energy | 1) reactions involving two or more reactants, active site provides template on which substrates can come together in proper orientation | 77 | |
7665190811 | Second way enzyme decreases Active Energy | as active site of enzyme clutches bound substrates enzyme may stretch substrate molecules towards transition state form, stressing and bending critical chemical bounds | 78 | |
7665231257 | Third way enzyme decreases Active Energy barrier | active site may also provide a microenivroment that is conducive to a particular type of reaction than solution itself would be without enzyme | 79 | |
7665242679 | Fourth way enzyme decreases Active Energy | direct participation of active site in chemical reaction involves brief convalent bonding between substrate and side chain of an amino acid of enzyme | 80 | |
7665268069 | Activity of Enzyme | how efficiently the enzyme functions affected by general environment factors such as temp and pH | 81 | |
7665275830 | Optimal Conditions | favor most active shape for enzyme molecule up to a point enzymatic reactions increase with increase of temperature | 82 | |
7665293167 | Cofactors | non protein helpers for catalytic activity may be bound tightly to enzyme as permanent resident or bind loosely and reversible along with substrate nonorganic | 83 | |
7665298023 | Coenzyme | if cofactor is organic molecule vitamins | 84 | |
7665310756 | Competitive inhibitors | reduce productivity of enzymes by blocking substrates from entering active sites | ![]() | 85 |
7665340059 | non competitive inhibitors | do not directly compete with substrate to bind to enzyme at active site impede enzymatic reactions by binding to another part of the enzyme causes enzyme to change shape in such a way that the active site becomes less effective | ![]() | 86 |
7665368112 | regulation of enzymatic activity helps... | control metabolism | 87 | |
7665370548 | Allosteric Regulation | any case in which a proteins function at one site is affected by binding of a regulatory molecule to a separate site | ![]() | 88 |
7665381849 | binding of activator to regulatory site stabilizes | shape that has functional active sites | 89 | |
7665384694 | binding of inhibitor stabilizes | inactive form of enzyme | 90 | |
7665390089 | products of ATP balance | flow of traffic between anabolic and catabolic pathways by effecting key enzymes | 91 | |
7665401548 | Cooperativity | substrate binds to one active site in a multisubunit enzyme triggering a shape change in all sub-units increasing catalytic activity amplifies response of enzymes to substrates | ![]() | 92 |
7665413443 | Feedback inhibitor | metabolic pathway switches off by inhibitory binding of its end product to enzyme that acts early on | 93 | |
7665415849 | Specific Localization of Enzyme in cell | cell compartmentalized and cell structures help bring order to metabolic pathways some enzymes assemble into multi-enzyme complex | 94 | |
7665445230 | ways to study a chemical reaction | measure the rate of disappearance of substrate measure rate of appearance of product | 95 | |
7665451301 | Lab experiment | after adding sulfuric acid test amount of substrate (hydrogen peroxide) remaining by titrating with potassium permanganate once all the left over H2O2 has reacted additional KMN04 will be in excess and will not be decomposed causing solution to turn pink | 96 | |
7665478975 | A test you could perform on gas given off to show that it is or isn't oxygen | glowing stick test | 97 | |
7665488160 | boiled catalase vs. unboiled | works faster as long as it doesn't go over temp point where it denatures | 98 | |
7665502095 | Liver added to H2O2 | bubbles breaking it down with catalase | 99 | |
7665512153 | baseline | control shows how much KMnO2 is used regularly to cause a color change in a known amount of H2O2 | 100 | |
7665524084 | reaction rate | decrease with time | 101 | |
7665535233 | Less KMnO4 used equals | more H2O2 used | 102 | |
7665593846 | Sulfuric acid inhibits reaction by | lowering pH denaturing enzyme | 103 | |
7665602505 | Design an experimetn to test the effect on reaction rate of pH, temperature, or enzyme concentration | first start out with control by mixing hydrogen peroxide and distilled water then titrate 5 mL sample to determine baseline then add 5 mL of catalse with hydrogen peroxide mix for ten seconds and then pour sulfuric acid in and titrate do this again for concentrations of 10 mL 15 mL 20 mL 25 mL and 30 mL of catalse to see how enzyme concentration affects how much hydogen peroxide is used | 104 |
AP Biology Chapter 8 Flashcards
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