Biology Ch. 6

Front 1

a cell needs?

Back 1

a way to encode/transmit info

a membrane separating inside & out

energy

Front 2

What is ATP & what's it's purpose?

Back 2

The universal currency of all cells.

It provides energy in a form ALL cells can readily use to perform work

It contains energy in its chemical bonds

Packaged energy in a chemical form that's accessible to the cell

Front 3

Metabolic classification

Back 3

organisms harvest energy from environment & 2 sources of carbon

Front 4

the 2 carbon sources from metabolic classification

Back 4

sun & chemical compounds

Front 5

phototroph

Back 5

obtains energy from the sun (plants)

takes in carbon dioxide and water &

creates sugar & oxygen

Front 6

chemotroph

Back 6

obtains energy from chemical compounds (animals)

takes in organic compounds from ingesting organisms

creates carbon dioxide & water

Front 7

autotrophs

Back 7

able to convert CO2 into glucose from their own organic sources of carbon

Front 8

heterotrophs

Back 8

don't have the ability to convert CO2 into carbon source; must ingest other organisms/molecules to obtain carbon

Front 9

metabolism

Back 9

the building up/ breaking down of carbon sources to harness/release energy

forms two branches

Front 10

catabolism

Back 10

the breakdown of molecules into smaller units, producing ATP

Front 11

anabolism

Back 11

the building of molecules from smaller units, requiring an input of energy, ATP

Front 12

energy of a system

Back 12

the system's ability to do work ie.

synthesizing DNA, RNA & protiens

moving vesicles in a cell

pumping substances across membranes

Front 13

kinetic energy

Back 13

energy of motion

associated w/ any form of movement

include light/electricity/thermal energy

Front 14

potential energy

Back 14

energy not associated w/ movement but rather is stored energy

depends on the structure of an object/ position w/ surroundings & the energy is released when the structure of an object/ position w/ surroundings is changed

the further the electron from the nucleus, the more potential energy present

Front 15

chemical energy

Back 15

possible due to the position of electrons around the nucleus of an atom

Front 16

1st Law of Thermodynamics

Back 16

energy is neither created nor destroyed, & only changes forms

Front 17

2nd Law of Thermodynamics

Back 17

energy changes form,

the total amount of energy remains constant, the energy available to do work decreases

there is a loss of energy to do work when transforming energy amount of disorder(entropy) increases when energy is transformed

Front 18

Chemical Reactions

Back 18

atoms keep their identity but the bonds linking them change the making & breaking of bonds

Front 19

Gibbs Free Energy ∆G

Back 19

the amount of energy in a system available to do work

Front 20

∆G

Back 20

the difference in Gibbs free energy between reactants/products of a chemical reaction

Front 21

∆G+

Back 21

if the product of a reaction has more free energy

require an input of energy & are endogonic

Front 22

∆G-

Back 22

if the reactants have more free energy than products

release energy & exergonic occur spontaneously

Front 23

∆G = ∆H - T∆S

Back 23

the energy available (G) = enthalpy [total energy](H) - absolute temp in Kº (T) & entropy [degree of disorder] (S)

Front 24

what influences the movement of molecules & adds to the degree of disorder present?

Back 24

temperature

Front 25

∆G in anabolic reactions

Back 25

have ∆G+ & require energy input, in ATP form

Front 26

∆G in catabolic reactions

Back 26

have ∆G- & require energy in ATP form

Front 27

ATP Hydrolysis

Back 27

ATP w/ H2O is exergonic(spontaneous) releases energy (-∆G)

Front 28

Energetic Coupling

Back 28

reaction 1: A -> B ∆G>0(energy consumed)

reaction 2: B -> C ∆G<0(energy released)

Front 29

Intermediate ∆G

Back 29

ATP- energy provider

ADP- energy acceptor

Front 30

enzymes

Back 30

chemical reactions in cell that are catalyzed by proteins

able to reduce the activation energy by stabilizing the transition state. the rate of the reaction increases because the activation energy is reduced

Front 31

what happens when a new compound forms?

Back 31

there's a brief transition state where bonds are breaking/forming & is unstable & has a large amount of free energy

when activation energy is low, the reaction is faster

Front 32

enzyme catalyzed reactions

Back 32

substrate(S) -> product(P)

S+enzyme(E) -> ES -> EP -> E+P

the substrate forms a complex w/ the enzyme; the substrate is converted into product while still part of a complex w/ enzyme & the complex dissociates releasing E & P.

Front 33

enzyme shape

Back 33

have a 3D structure that brings together amino acids to form active sites

binds the substrate & converts it to the product (enzyme active site)

Front 34

substrate & active site interactions

Back 34

weak-noncovalent interactions/transient covalent bonds that stabilize the transition state & decrease the activation energy required for reaction

Front 35

active site formation

Back 35

an enzyme's active site is very small compared to the enzyme

the active site amino acids may be spaced far apart in the primary sequence of the enzyme, but when the protien is folded together it forms the active site

Front 36

Svante Arrhenius

Back 36

first demonstration of the enzyme-substrate complex

a Swedish chemist who in 1888 proposed an idea that enzymes form complexes w/ substrates to catalyze a chemical reaction

Front 37

Kurt Stern

Back 37

an American chemist who carried out one of the earliest experimental demonstrations that supported Arrhenius' hypothesis & used spectral analysis.

analyzed the absorption peak patterns & determined if an intermediate complex was formed or not

Front 38

spectral analysis

Back 38

different molecules absorb different wavelengths of light

Front 39

absorption peak

Back 39

the wavelength of maximum absorption for a particular molecule

Front 40

second demontstration of the enzyme/substrate complex

Back 40

enzyme ß-galactosidase catalyzes cleavage of glycosidic bond that links galactose-glucose in a disaccharide lactose

Front 41

how to show formation of enzyme/substrate complex

Back 41

a beaker named ß thiogalactoside added to compartment 1 & its movement is followed by measuring the radioactivity in the two compartments. overtime radioactivity become the same

Front 42

inhibitors

Back 42

decrease the activity of an enzyme

competitive

noncompetitive

Front 43

activators

Back 43

increase activity of an enzyme

Front 44

competitive inhibitors

Back 44

bind to active site of the enzyme & prevent substrate from binding. they compete w/ the substrate for the active site

Front 45

noncompetitive inhibitors

Back 45

bind to a site other than the active. slow down the reaction normally catalyzed by the enzyme by altering the enzyme shape