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Biology 181 Module 2 > Energy > Flashcards

Energy Flashcards

1
Q

Cell Requirements

A
  • A way to encode/transmit info (DNA)
  • Membrane separating inside from out
  • ENERGY
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2
Q

ATP

A

TRIphosphate
contains NRG in CHEMICAL BONDS
In all polyers (lipids, DNA, carbohydrates…)

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3
Q

Phototrophs

A 
Energy from sun
photons
vascular palnts
cyanonobacteria
CO2 are carbon source, make more complex moelcs from it
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4
Q

Autotrophs (Photo)

A

CO2 is carbon source, make more complex moelcs from it

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5
Q

Heterotrophs (Photo)

A

carbon from other organic compounds
not taking CO2 and making it more complex,
heliobacter
sulfer bacteria
get NRG from sunlight in molecs that let them make hydrogen ion gradeint, but it is not used to make CO2 more complex

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6
Q

Chemotrophs

A

Energy from chemical compounds

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7
Q

Autotrophs (C)

A

Live in harsh environments
Redox rxns
Most bacteria
Sulfer and magnesium e- transfer fixes carbon

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8
Q

Heterotrophs (C)

A

Humans!

Get carbon from eating other organic compounds

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9
Q

Autotrophs

A

self feeders, make own organic source carbon

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10
Q

Heterotrophs

A

“other feeders” rely on other organsms for organic sources of carbon

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11
Q

Metabolism

A

Building and breaking down of carbon sources to harness or releases energy
sum of reactions to harness or release energy
always happening!

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12
Q

Catabolism

A

Marcromolecues: broken down into subunits
release of energy
released enrgy can be coupled with ATP production (ADP+Pi)

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13
Q

Anabolism

A

Make larger units out of polymers
energy dependent
couple to reactions that USE ATP and break it down (ADP and Pi from ATP)

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14
Q

Kinetic energy

A

NRG of motion. (thermal, light, electric)

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15
Q

Potential energy

A

released when a change in structure or position occurs.

Stored energy tht is ready to use

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16
Q

What needs energy?

A

active transport!

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17
Q

thermal energy

A

molecules moving

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18
Q

light energy

A

movement of photons

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19
Q

Electrons in chemical energy

A

electron further from nucleus: Greater PE
movement to lower orbital: NRG release, kinetic NRG
High PE to low PE: more distant shell to closer shell

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20
Q

Covalent bonds

A

result of shared electrons
when electrons far from both nuclie, lots of PE in bond
closer= lower PE in bond
Longer polymer with lots of bonds means MORE PE
(More when electronegitivity)

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21
Q

ATP structure

A 
Sugar: Ribose (OH GROUP!)
connect to adenine base
3 phosphate groups attached
(AMP, 1 phosphate)
(ADP, 2 phosphates)
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22
Q

Phosphates in ATP

A

negatively charged
repelling eachother
so HIGH PE
when released, KE, does work

23
Q

First Law Thermodynamics

A

NRG neither created nor destroyed

24
Q

Second Law

A

Entropy increases, so only part of the energy originally WILL BE LOST to entropy, given off as heat

25
Free Energy: Delta G: GIbbs free energy
amount of energy avaliable to do work (NOT THE PART LOST TO ENTROPY)
26
Endergonic
Requires NRG, non spontaneous | products higher than reactants
27
Exergonic
does not require NRG, spontaneous | products lower than reactants
28
Gibbs free energy equation
DELTA G= DELTA H- T DELTA S
29
H
Enthalpy, total energy avaliable
30
S
entropy, degrees of disorder
31
T
temp in kelvin. Higher temperature means higher S (entropy) | increase increases disorder, makes S bigger
32
decrease disorder
(-DS) increase chemical energy in bonds (+DH)
33
increase disorder
decrease chemical energy in bonds (-DH)
34
Breaking bonds (low energy state
Negative Delta G
35
High energy state (making bonds):
Postiive Delta G
36
ATP Hydrolysis
ATP and Water break water, add hydroxyl, release phospate. ATP--> ADP +Pi Lots of energy release with phosophate bond breaking NEGATIVE Delta G!!!! Entropy INCREASED
37
Reaction Coupling
Overall total is used to determine exergonic or endergonic Overall negative--> exergonic rxn product of first reaction is a reactant in the next See notes/lecture!
38
ATP has intermediate Delta G
-7 Because intermediate, can use Pi as input to drive second reaction. can be used to go to ATP or ADP Reactions with more neative delta G donate phospate group Reactions with more psotive delta G recieve phosphate group ATP NRG provider ADP NRG acceptor
39
Enzymes
Peak is unstable transition state uncatalyzed has higher Ea catalysts lower Ea DELTA G IS ALWAYS THE SAME (from reactants to products)
40
Ea
activation enrgy | reactants to transition state
41
Enzyme catalyzed RXN
``` Substrate+ enzyme(E) → ES→ EP→ E+P enzyme not consumed ES: complex of substrate and enxyme reactions catalyzed EP: complex of enzyme and product STABALIZE TRANSITION STATE (this is what lowers Ea) ```
42
Enzymes
highly specific. Only a specific molecule, or a small family | can only catalyze one or a very few reactions
43
Competitive Inhibition (reversible)
bind to active site of the enzyme and prevent the substrate from binding. Compete with substrate for active site 2 similar molecs compete for active site. Depending on amount of inhibitor or substrate, either Inhibiting because competeing for binding site Many drugs work this way
44
Non competitive Inhibition (reversible)
Inhibitors bind to site different from active site a couple of sites on enzyme that can bind molecules (not just the main active site) The noncompetitive slow down rxn that would be catalyzed by enzyme Slows it so that very little product is made (if any) NOT COMPETEING FOR SAME ACTIVE SITE Can cause conf. change in enzyme, like pocket where substrate would normally bind
45
Enzymes do not
HAVE ENERGY! | they just get the molecules right so that its easier
46
Beta galactosidase
Attacking molecs (more than one type) • Semipermeable membrane, put substrate on one side and let it diffuse across membrane o Substrate radioactively labled • Found radioactive activity equal on both halves membrabe • Put enzyme on one side (enzyme can’t pass through, s still can) o Found more substrate on one side (the one with enzyme) because enzyme and substrate interacting. Substrate gets stuck there
47
Active site
Binds to substrate, causes rxn to occur | weak, just stabalizing Tstate, lowering Ea
48
Irreversible Inhibitors
usually come from covalent bonds with enzymes and irreversibly inactivate them. enzyme can't work
49
Reversible Inhibitors
Form weak bonds with enzyme and easily dissociate from them
50
H2O2 experiment
shine light where rxn occuring. Enzyme and H2O2 have different spectra. BUT at some point in the middle, the spectra become one. Then progresses back
51
Do all enzymes form an enzyme-substrate complex? Beta galactosidase
Semi permeable membrane. Substrate on 1 side, can pass through membrane until equilibrium. THEN added enzyme to one side, it cant pass through membrane, but sub still can. More on the side without the enzyme because substrate stuck with enzyme.
52
Allosteric Regulation (inhibition and activation)
Non competitive inhibition used to control enzymatic pathways shape change to enzyme End products often used as indicators of whether pathway should be running Good to shut down at begining if shut down needs to happen.
53
Cofactors
small inorganic molec in cell (vitamins) | to gen substrates to bind well to enzyme tht will act on them
54
Coenzymes
small ORGANIC molec in cell | to gen substrates to bind well to enzyme tht will act on them

Biology 181 Module 2 (6 decks)

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