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AP Biology Chapter 8 Flashcards

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7664318137Metabolismtotality of an organism's chemical reaction emergent property of life that arises from orderly interactions between molecules0
7664327609Metabolic Pathwaybegins 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 enzyme1
7664339739Metabolic pathway controlsstarting molecule and stopping molecule control flow of automobile traffic, mechanisms that regulate enzymes balance metabolic supply and demand2
7664349141Catabolic Pathwaysdegradation process some metabolic pathways release energy by breaking down complex molecules to simpler compounds "downhill"3
7664372347Catabolic Pathways releaseenergy that was stored in organic molecules. Becomes available to do work of cell4
7664381773Anabolic pathwaysconsume energy to build complicated molecules from simpler ones; sometimes called Bio synthetic pathways ex: protein synthesis "uphill"5
7664405159Bioenegeticsstudy of how energy flows through living organisms6
7664408174Energycapacity to cause change7
7664414486kinetic Energyrelative motion of object8
7664421941Heat/thermal energykinetic energy associated with random movement of atoms/molecules9
7664425800Potential energynot moving but can still possess energy due to location/structure10
7664434228Chemical Energypotential energy available for release in chemical reaction glucose increases in chemical energy11
7664441166Thermodynamicsstudy of energy transformation that occurs in a collection of matter12
7664452556Systemmatter under study13
7664455081Surroundingeverything beside system14
7664457996Isolated Systemunable to exchange energy/matter with surroundings15
7664461283open systemexchange energy/matter with surroundings16
7664472373First law Of Thermodynamics Principle of Conservationo f energyenergy can be transferred/transformed but cannot be created or destroyed17
7664483234Second Law of Thermodynamicsduring every energy transfer/transformation some energy is unavailable to do work which results in a loss of heat18
7664489981Entropya measure of disorder evident in physical disintegration increase disorder by releasing heat19
7664505531Every energy transfer/transformation increases...entropy of universe20
7664523797Bear increases entropyby eating a fish increasing disorder of surroundings by producing heat and small molecules like carbon dioxide21
7664538234If a process increases entropy it can...occur without input of energy22
7664538235Spontaneous Processoccurs without input of energy energetically favorable ex: water flowing downhill23
7664549739biological Order and Disorderliving systems increase entropy of surroundings create ordered struuter but also take ordered things and make them less ordered ex:animals eating24
7664561535Entropy of a particual system can decrease as long astotal entropy of universe increases25
7664567187Free Energy Changetells us whether a reaction occurs spontaneously or not Triangle G26
7664574751Change in Free energy equalschange in heat minus temperature and change in entropy27
7664580958If Change in Free energy is negativeit is spontaneous either change in heat is negative or temperature times change in entropy is positive (system gives up order and increases S)28
7664608305Every spontaneous process decreases...system's free energy29
7664612887When change in free energy is positive or zeroit is never spontaneous30
7664617351Triangle G equalsG final state minus G initial state31
7664623437free energymeasure of system's instability or its tendency to change to a mere stable state32
7664633540Unstable system (more free energy) tend to...change into a stable system (decrease in free energy)33
7664640417Equilibriumanother term that describes state of maximum stability free energy of mixture of reactants and products decreases34
7664664749When reaction is pushed away from Equilibrium what happens to free energyincreases35
7664675243A system at equilibrium cannotspontaneously change which means it won't work and cell will die36
7664686509A process is spontaneous and will work when...it is moving toward equilibrium37
7664689069Exergonic reaction(energy outward) proceeds with a net release of free energy loses free energy so the change inf free energy is negative38
7664708855Denaturationmisshaping enzyme over a particular temperature it denatures39
7664726385Breaking bonds needsenergy40
7664726386Endergonic reactionabsorbs free energy from surroundings stores free energy in molecules increases G (change in endergonic reaction is positive=non-spontaneous) "uphill"41
7664735614Magnitude of change in free energy is..quantity of energy required to drive reaction42
7664758806What keeps cell from reaching equilibriumconstant flow of materials key is that product cannot accumulate but becomes a reactant in the next step43
7664769010ATP powers cellular work bycoupling exergonic reactions to endergonic reactions44
76647781613 main types of work Cell performschemical, transport, mechanical45
7664781322Chemical Workpushing of endergonic reactions that wouldn't occur spontaneously46
7664797477Transport Workpumping of substanes across membranes against direction of spontaneous movemetn47
7664801601Mechanical Worksuch as beating of cilia, contraction of muscle cells movement of chromosomes during cell reproduction48
7664811510Energy couplingkey feature in way cell manages energy resources, use of exergonic process to drive endergonic one ATP responsible for mediating energy coupling49
7664825631ATP (Adenosine triphosphate)contains sugar ribose with nitrogenous base and a chain of three phosphate groups50
7664840958Bonds between phophate groups can be broken byhydrolysis51
7664843362HydrolysisBreaking down complex molecules by the chemical addition of water52
7664856083Lose of phosphate group isspontaneous53
7664860438Cell conditions are not...standard conditions54
7664865107ATP plus Water meansincrease energy compared to products change to a state of lower free energy55
7664901762Shivering usesATP hydrolysis to release heat56
7664909917generation of heat is____in cellsineffective and dangerous57
7664916139What are the conditions needed for two reactions to be coupledif the change in free energy of endergenic is less than the amount of energy released by ATP hydrolysis means overall reaction is exergonic58
7664955541Phosphorylated intermediaterecipient with phosphate group covalently bonded to it more reactive means less stable than original molecule59
7664969738Transport and Mechanical work powered byhydrolysis of ATP leads to change of protein and ability to bind to another60
7664976937ATP is what type of energy?renewable, can be regenerated by addition of phosphate to ADP61
7664979933ATP Cycleshuttling 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->ATP62
7665001406Enzymes speed up metabolic reactions bylowering energy barriers63
7665014239Enzymemacro-molecule that acts as a catalyst64
7665021505Catalystchemical agent that speeds up reaction without being consumed65
7665027596The Activation Energy Barrierchanging one molecule to another by contorting starting molecule into highly unstable state before reaction must absorb energy from surroundings to contort66
7665045713Activation Energy/free energy of activationEa 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 heat67
7665066976Transition Statewhen molecules ave absorbed enough energy for bonds to break68
7665074666Activation Energy providesbarrier that determines rate of reaction reactants must absorb enough energy to reach top of EA barrier before reaction can occur69
7665079794How Enzymes Lower Ea Barriercatalyzes reaction by lowering Ea barrier and cannot change the change of free energy for a reaction70
7665103396Substratereactant an enzyme acts on71
7665112405Enzyme substrate complexenzyme binds to its substrates72
7665120391Active Siteregion where catalysis occurs formed by only a few enzyme's amino acids73
7665126702Induced fitbrings chemical groups of active site into positions that enhance their ability to catalyze chemical reactions74
7665133004Catalysis in Enzyme's Active site75
7665163632enzyme can catalyze either fowrad or reverse depending onwhich direction has a negative change in free energy76
7665174706How do enzymes decrease Active Energy1) reactions involving two or more reactants, active site provides template on which substrates can come together in proper orientation77
7665190811Second way enzyme decreases Active Energyas active site of enzyme clutches bound substrates enzyme may stretch substrate molecules towards transition state form, stressing and bending critical chemical bounds78
7665231257Third way enzyme decreases Active Energy barrieractive site may also provide a microenivroment that is conducive to a particular type of reaction than solution itself would be without enzyme79
7665242679Fourth way enzyme decreases Active Energydirect participation of active site in chemical reaction involves brief convalent bonding between substrate and side chain of an amino acid of enzyme80
7665268069Activity of Enzymehow efficiently the enzyme functions affected by general environment factors such as temp and pH81
7665275830Optimal Conditionsfavor most active shape for enzyme molecule up to a point enzymatic reactions increase with increase of temperature82
7665293167Cofactorsnon protein helpers for catalytic activity may be bound tightly to enzyme as permanent resident or bind loosely and reversible along with substrate nonorganic83
7665298023Coenzymeif cofactor is organic molecule vitamins84
7665310756Competitive inhibitorsreduce productivity of enzymes by blocking substrates from entering active sites85
7665340059non competitive inhibitorsdo 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 effective86
7665368112regulation of enzymatic activity helps...control metabolism87
7665370548Allosteric Regulationany case in which a proteins function at one site is affected by binding of a regulatory molecule to a separate site88
7665381849binding of activator to regulatory site stabilizesshape that has functional active sites89
7665384694binding of inhibitor stabilizesinactive form of enzyme90
7665390089products of ATP balanceflow of traffic between anabolic and catabolic pathways by effecting key enzymes91
7665401548Cooperativitysubstrate 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 substrates92
7665413443Feedback inhibitormetabolic pathway switches off by inhibitory binding of its end product to enzyme that acts early on93
7665415849Specific Localization of Enzyme in cellcell compartmentalized and cell structures help bring order to metabolic pathways some enzymes assemble into multi-enzyme complex94
7665445230ways to study a chemical reactionmeasure the rate of disappearance of substrate measure rate of appearance of product95
7665451301Lab experimentafter 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 pink96
7665478975A test you could perform on gas given off to show that it is or isn't oxygenglowing stick test97
7665488160boiled catalase vs. unboiledworks faster as long as it doesn't go over temp point where it denatures98
7665502095Liver added to H2O2bubbles breaking it down with catalase99
7665512153baselinecontrol shows how much KMnO2 is used regularly to cause a color change in a known amount of H2O2100
7665524084reaction ratedecrease with time101
7665535233Less KMnO4 used equalsmore H2O2 used102
7665593846Sulfuric acid inhibits reaction bylowering pH denaturing enzyme103
7665602505Design an experimetn to test the effect on reaction rate of pH, temperature, or enzyme concentrationfirst 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 used104

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