Micro Chapter 10

Front 1

Carbon source of autotrophs

Back 1

CO2

Front 2

Carbon source of heterotrophs

Back 2

Performed organic molecules from other organisms

Front 3

Energy source of phototrophs

Back 3

light

Front 4

Energy source of chemotrophs

Back 4

Reduced inorganic or organic compounds

Front 5

Electron source of lithotrophs

Back 5

Reduced inorganic molecules

Front 6

Electron source of organotrophs

Back 6

Reduced organic molecules

Front 7

Metabolism

Back 7

total of all chemical reactions in the cell and is divided into two parts (catabolism and anabolism)

Front 8

catabolism

Back 8

break down of organic molecules

Front 9

anabolism

Back 9

synthesis of organic molecules

Front 10

energy

Back 10

capacity to do work or to cause particular changes

Front 11

chemical work

Back 11

synthesis of complex molecules

Front 12

transport work

Back 12

take up of nutrients, elimination of wastes, and maintenance of ion balances

Front 13

mechanical work

Back 13

movement of organisms or cells and movement of internal structures

Front 14

ATP

Back 14

used to transfer energy from cell's energy conserving systems to the systems that carry out cellular work

Front 15

First law of thermodynamics

Back 15

energy cannot be created nor destroyed

Front 16

Second law of thermodynamics

Back 16

energy cannot be changed from one form into another without a loss of usable energy

Front 17

Entropy

Back 17

measure of randomness or disorder

Front 18

Free energy

Back 18

the amount of energy that is free to do work after a chemical reaction

Front 19

Exergonic reaction

Back 19

energy is released

negative delta G

Front 20

Endergonic reactions

Back 20

input of energy is required

positive delta G

Front 21

Reversible reactions

Back 21

Have free energy near zero; at equilibrium

Front 22

Equilibrim

Back 22

reaction is at equilibrium when rate of forward reaction = rate of reverse reaction

Front 23

Equilibrium constant

Back 23

expresses the equilibrium concentrations of products and reactants to one another

Front 24

Standard Reduction Potential

Back 24

a measure of the tendency of the reducing agent to lose electrons

Front 25

Oxidation-reduction reactions

Back 25

electron transfers

Front 26

reductant/reducing agent

Back 26

electron donor

Front 27

oxidant/oxidizing agent

Back 27

electron acceptor

Front 28

NAD

Back 28

nicotinamide adenine dinucleotide

Front 29

NADP

Back 29

nicotinamide adenine dinucleotide phosphate

Front 30

FAD

Back 30

flavin adenine dinucleotide

Front 31

FMN

Back 31

flavin mononucleotide

Front 32

coenzyme Q (coQ)

Back 32

a quinone, also called ubiquinone

Front 33

protein catalysts

Back 33

have a great specificity for the reaction catalyzed and the molecules acted on

Front 34

catalyst

Back 34

a substance that increases the rate of a reaction without being permanently altered

Front 35

substrates

Back 35

reacting molecules

Front 36

products

Back 36

substances formed by reaction

Front 37

apoenzyme

Back 37

a protein component of an enzyme

Front 38

cofactor

Back 38

nonprotein component of an enzyme

Front 39

prosthetic group

Back 39

firmly attached

Front 40

coenzyme

Back 40

loosely attached

Front 41

holoenzyme

Back 41

apoenzyme + cofactor

Front 42

Oxidoreductase

Back 42

oxidation-reduction reactions

Front 43

Transferase

Back 43

reactions involving the transfer of groups between molecules

Front 44

Hydrolase

Back 44

hydrolysis of molecules

Front 45

lyase

Back 45

removal of groups to form double bonds or addition of groups to double bonds

Front 46

isomerase

Back 46

reactions involving isomerization

Front 47

ligase

Back 47

joining of two molecules using ATP energy

Front 48

transition-state complex

Back 48

resembles both the substrates and the products

Front 49

activation energy

Back 49

energy required to form transition state complex

Front 50

How do enzymes lower activation energy

Back 50

-by increasing concentrations of substrates at active site of enzyme

-by orienting substrates properly with respect to each other in order to form the transition-state complex

Front 51

denaturation

Back 51

loss of enzyme's structure and activity when temperature and pH rise too much above optima

Front 52

competitive inhibitor

Back 52

directly competes with binding substrate to active site

Front 53

noncompetitive inhibitor

Back 53

binds enzyme at site other than active site; changes enzyme's shape so that it becomes less active

Front 54

Cech & Altman

Back 54

discovered that some RNA molecules also can catalyze reactions

Front 55

3 mechanisms of metabolism

Back 55

-metabolic channeling

-regulation of the synthesis of a particular enzyme

-direct stimulation or inhibition of the activities of a critical enzyme

Front 56

metabolic channeling

Back 56

differential localization of enzymes and metabolites

Front 57

compartmentation

Back 57

differential distribution of enzymes and metabolites among separate cell structures or organelles

Front 58

allosteric regulation

Back 58

effector binding alters shape of active site, e

Front 59

Covalent modification

Back 59

reversible addition or removal of a chemical group that alters enzyme activity

Front 60

Feedback inhibition/ product inhibition

Back 60

inhibition of one or more critical enzymes in a pathway regulates entire pathway

Front 61

isoenzymes

Back 61

different enzymes that catalyze the same reaction