Chapter 8 Flashcards

(55 cards)

1
Q

Metabolism

A

-totality of an organisms chemical reactions
-emergent property of life that arises from interactions between molecules within the cell
-subject to laws of thermodynamics
-never in equilibrium

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2
Q

Metabolic pathway

A

-beings with specific molecule
-ends with product
-each step catalyzed by specific enzyme

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3
Q

Catabolic pathways

A

-release energy by breaking down complex molecules into simpler compounds
ex cellular respiration
-releases free energy in series of reactions

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4
Q

Anabolic pathways

A

-consume energy to build complex molecules from simpler ones
ex synthesis of protein from amino acids

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5
Q

Bioenergetics

A

study of how organisms manage their energy resources

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6
Q

Energy

A

-capacity to cause change
-exists in various forms, some can perform work (move matter against forces or rearrange matter)
-can be converted from one form to another

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7
Q

Kinetic energy

A

-energy associated with motion
-heat (thermal energy)- kinetic energy associated with random movement of atoms or molecules
-light-photosynthesis

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8
Q

Potential energy

A

-energy that matter possesses because of its location or structure
-chemical energy-potential energy available for release in a chemical reaction

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9
Q

Thermodynamics

A

-study of energy transformations that occur in a collection of matter

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10
Q

System

A

matter under study

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11
Q

Surroundings

A

-the rest of the universe
-everything outside the system

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12
Q

Isolated system

A

-does not exchange energy and matter with surroundings

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13
Q

Open system

A

-exchange energy and matter
-all organisms

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14
Q

First law of thermodynamics

A

-principle of conservation of energy
-the energy of the universe is constant
-energy can be transferred and transformed but cannot be created or destroyed

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15
Q

Second law of thermodynamics

A

-energy transfer or transformation increases the entropy (disorder) of the universe
-some energy is unusable and lost as heat during transfer

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16
Q

Spontaneous processes

A

occur without energy input
-must increase the entropy of the universe

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17
Q

Nonspontaneous processes

A

-require input of energy

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18
Q

Typical energy flow

A

energy flows into most ecosystems as light and exits in form of heat to increase entropy

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19
Q

Systems free energy

A

-the energy that can do work when temperature and pressure are uniform
change in G= change in H-tchange in S
H=enthalpy, total energy
S=change in entropy
T=in Kelvin

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20
Q

Negative delta G

A

spontaneous
-decreases systems total energy or increases the entropy

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21
Q

Positive or zero delta G

A

never spontaneous

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22
Q

Change in G

A

G final-G initial
-system in final state is more stable

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23
Q

Free energy

A

measure of systems instability
-its tendency to change to a more stable state

24
Q

Spontaneous

A

-free energy decreases
-stability of system increases

25
Equilibrium
-state of maximum stability -no further net change in concentration of product or reactants -lowest value of G -change in G =0
26
Move out of equilibrium
G increase, change in G positive, reaction is non spontaneous
27
Spontaneous and can perform work when
it is moving towards equilibrium
28
Exergonic reaction
-proceeds with net release of free energy -spontaneous
29
Endergonic reaction
-absorbs free energy -nonspontaneous
29
Energy coupling
-how cells manage energy resources to do work -use of an exergonic process to drive an endergonic one -most mediated by atp
30
3 kinds of work cell does
-chemical- synthesis of polymers -transport- nak pump -mechanical-segregation of chromosomes
31
ATP
-cells energy shuttle -composed of ribose (sugar), adenine (nitrogenous base) and 3 phosphate groups -bonds between phosphate groups of atp tail can be broken by hydrolysis -energy related when last phosphate bond is broken
32
Phosphorylation
-how atp drives endergonic reactions -transferring a phosphate group to some other molecule
33
Phosphorylated intermediate
-recipient molecule in phosphorylation -more reactive, less stable than original molecule
34
ATP
-reneweable resource -regenerated by addition of P group to ADP
35
Enzyme
catalytic protein -catalyze reactions by lowering activation energy barrier -do not affect the change in free energy -speed up reactions that would occur eventually -selective, determine which chemical processes occur at any time
36
Catalyst
chemical agent that speeds up a reaction without being consumed by the reaction
37
Free energy of activation/free energy
initial energy needed to start a chemical reaction -often in form of thermal energy that reactant molecules absorb from surroundings
38
Substrate
reactant that enzyme acts on
39
Enzyme substrate complex
enzyme binds to its substrate
40
Active site
region on enzyme where substrate binds -can lower activation energy barrier by orienting substrates correctly, straining substrate bonds, providing favorable microenvironment, covalently bonding to substrate
41
Induced fit
-of a substrate -brings chemical groups of active site into positions that enhance their ability to catalyze reactions
42
Enzyme activity impacted by
-environmental factors -temp and pH (optimal) -optimal conditions favor most active shape for enzyme molecule
43
Cofactors
-nonprotein helpers required by enzymes for catalytic activity -bind permanently or reversibly to enzyme
44
Organic cofactors
-coenzymes -ex vitamins
45
Competitive inhibitors
-bind to active site of enzyme -compete with substrate
46
Noncompetitive inhibitors
-bind to another part of enzyme -causes enzyme to change shape and makes active site less effective
47
Evolution of enzymes
-enzymes-proteins encoded by genes -mutations in genes lead to changes in amino acid composition of enzyme -altered amino acids in enzymes may alter substrate specificity
48
How does cell regulate enzyme activity
-switching on or off genes that encode specific enzymes -regulates activity of enzymes
49
Allosteric regulation
-either inhibit or stimulate enzyme activity -regulatory molecule binds to protein at one site and affects proteins function at another site -made from polypeptide subunits
50
Binding of activator
stabilizes the active form -ADP for catabolic enzymes
51
Bindings of inhibitor
-stabilizes the inactive form -ATP for catabolic enzymes
52
Cooperativity
-a form of allosteric regulation that can amplify enzyme activity -one substrate molecule primes an enzyme to act on additional substrate molecules more readily -binding by a substrate to one active site affects catalysis in a different active site
53
Caspases
-inhibition of proteolytic enzymes -help management of inappropriate inflammatory responses
54
End product of metabolic pathway
-shuts down the pathway -prevents cell from wasting chemical resources by synthesizing more product than needed