Abac Biol 1107 Campbell Chapter 8 Metabolism

Front 1

Totality of an organism's chemical processes.

Back 1

Metabolism

Front 2

Metabolic pathways which release energy by breaking down complex molecules to simpler compounds.

Back 2

Catabolic pathways

Front 3

Metabolic pathways which consume energy to build complicated molecules from simpler ones.

Back 3

Anabolic pathways

Front 4

the capacity to do work - to move matter against opposing forces.

Back 4

Energy

Front 5

Energy in the process of doing work (energy of motion).

Back 5

Kinetic energy

Front 6

Energy that matter possesses because of its location or arrangement (energy of position).

Back 6

Potential energy

Front 7

Study of energy transformations

Back 7

Thermodynamics

Front 8

Collection of matter under study which is isolated from its surroundings

Back 8

Closed system

Front 9

System in which energy can be transferred between the system and its surroundings.

Back 9

Open system

Front 10

Energy can be transferred and transformed, but it cannot be created or destroyed (energy of the universe is constant).

Back 10

First Law of Thermodynamics

Front 11

Every energy transfer or transformation makes the universe more disordered (every process increases the entropy of the universe).

Back 11

Second Law of Thermodynamics

Front 12

Quantitative measure of disorder that is proportional to randomness (designated by the letter S).

Back 12

Entropy

Front 13

Those reactions that can occur without outside help.

Back 13

Spontaneous processes

Front 14

Those reactions that can only occur if energy is added to a system.

Back 14

Nonspontaneous processes

Front 15

Portion of a system's energy available to do work; is the difference between the total energy (enthalpy) and the energy not available for doing work (TS).

Back 15

Free energy (G)

Front 16

Formula for free energy

Back 16

G = H - TS

Front 17

Formula for free energy change

Back 17

ΔG = ΔH - TΔS

Front 18

In the formula for free energy change, what is ∆G?

Back 18

change in Free energy

Front 19

In the formula for free energy change, what is ∆H?

Back 19

change in Enthalpy (total energy)

Front 20

In the formula for free energy change, what is ∆S?

Back 20

change in Entropy

Front 21

In the formula for free energy change, what is T?

Back 21

Temperature in Kelvin

Front 22

A reaction that proceeds with a net loss of free energy.

Back 22

Exergonic reaction

Front 23

An ________reaction is one that releases free energy to its surroundings.

Back 23

exergonic

Front 24

Δ G of an exergonic reaction is _____ (positive/negative)

Back 24

negative.

Front 25

Amount of energy that reactant molecules must absorb to start a reaction.

Back 25

Energy of activation

Front 26

Unstable condition of reactant molecules that have absorbed sufficient free energy to react.

Back 26

Transition state

Front 27

An energy-requiring reaction that proceeds with a net gain of free energy.

Back 27

Endergonic reaction

Front 28

An _____ reaction is one that requires free energy from its surroundings.

Back 28

endergonic

Front 29

Δ G of an endergonic reaction is ____ (positive/negative)

Back 29

positive.

Front 30

reaction in which the rates of forward and backward reactions are equal and there is no change in the concentration of products or reactants.

Back 30

Chemical Equilibrium

Front 31

The ΔG of a reaction at equilibrium is ______

Back 31

Zero

Front 32

To do work, cells manage energy resources by energy coupling, the use of an ___ process to drive an ____ one

Back 32

exergonic/endergonic

Front 33

Nucleoside triphosphate with unstable phosphate bonds that the cell hydrolyzes for energy to drive endergonic reactions.

Back 33

ATP (adenosine triphosphate)

Front 34

The bonds between the phosphate groups of ATP’s tail can be broken by ____ reactions

Back 34

hydrolysis

Front 35

List the three main kinds of work of ATP.

Back 35

1. Chemical work such as driving endergonic reactions such as the synthesis of polymers from monomers
2. Transport work such as pumping substances across membranes against the direction of spontaneous movement.
3. Mechanical work such as beating of cilia, contraction of muscle cells, and movement of chromosomes.

Front 36

Chemical agent that accelerates a reaction without being permanently changed in the process, so it can be used over and over.

Back 36

Catalyst

Front 37

Biological catalysts, which are usually proteins.

Back 37

Enzymes

Front 38

Enzymes catalyze reactions by lowering the _____

Back 38

EA barrier

Front 39

The substance an enzyme acts on and makes more reactive.

Back 39

Substrate

Front 40

Change in the shape of an enzyme's active site, which is induced by the substrate.

Back 40

Induced fit

Front 41

Restricted region of an enzyme molecule which binds to the substrate.

Back 41

Active site

Front 42

List the 4 mechanisms that enzymes use to lower activation energy and speed a reaction

Back 42

1. orients substrates
2. put stress on bonds that must be broken, making it easier to reach the transition state.
3. favorable microenvironment for a specific reaction.
4. Enzymes may even bind covalently to substrate

Front 43

List the environmental factors that can effect enzyme rate.

Back 43

1.Temperature
2.pH

Front 44

Small non-protein molecules that are required for proper enzyme catalysis.

Back 44

Cofactors

Front 45

a non-protein organic cofactor.

Back 45

Coenzyme

Front 46

The protein portion of an enzyme.

Back 46

Apoenzyme

Front 47

The apoenzyme plus its coenzyme or cofactor.

Back 47

Holoenzyme

Front 48

molecules that bind to enzymes and prevent enzymes from catalyzing reactions.

Back 48

Inhibitors

Front 49

Chemicals that resemble an enzyme's normal substrate and compete with it for the active site.

Back 49

Competitive inhibitors

Front 50

Enzyme inhibitors that do not enter the enzyme's active site, but bind to another part of the enzyme molecule

Back 50

Noncompetitive inhibitors

Front 51

Enzymes are proteins encoded by ___

Back 51

genes

Front 52

Mutations (changes) in genes lead to changes in ____ of an enzyme

Back 52

amino acid composition

Front 53

Altered amino acids in enzymes may alter their shape and affect ______.

Back 53

substrate specificity

Front 54

Specific receptor site on some part of the enzyme molecule other than the active site.

Back 54

Allosteric site

Front 55

stabilizes the active form of the enzyme

Back 55

Activators

Front 56

stabilizes the inactive form of the enzyme

Back 56

Inhibitor

Front 57

Regulation of a metabolic pathway by its end product, which inhibits an enzyme within the pathway.

Back 57

Feedback inhibition

Front 58

How can the localization of enzymes within a cell help order metabolism

Back 58

1.Metabolic pathway assembled in a multienzyme complex
2.Fixed locations within the cell as structural components of membranes
3.In solution, within an organelle with its own internal microenvironment

Front 59

Endergonic or exergonic?

Back 59

endergonic

Front 60

Endergonic or exergonic?

Back 60

exergonic

Front 61

spontaneous or non-spontaneous?

Back 61

non-spontaneous

Front 62

spontaneous or non-spontaneous?

Back 62

spontaneous

Front 63

Substrates are ___energy and products are ____ energy.

Back 63

low
high

Front 64

Substrates are ___energy and products are ____ energy.

Back 64

high
low

Front 65

negative or positive ΔG?

Back 65

positive

Front 66

negative or positive ΔG?

Back 66

negative

Front 67

Does this reaction absorb or release energy (net)?

Back 67

absorb

Front 68

Does this reaction absorb or release energy (net)?

Back 68

release

Front 69

What are the sections of the graphs labeled A-D?

Back 69

A free energy of substrate
B free energy of product
C activation energy
D free energy