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13 Cards in this Set

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draw the picture of what would happen if a cell used glucose?
p
why is oxidation of hydrocarbons so lucrative?
1)oxidation of hydrocarbons to reduce oxygen and form h20 to form water releases a lot of free energy: -56 kcal

2) if cellular metabolism can strip H atoms from hydrocarbons and combine them with oxygen, a lot of energy can be generated that can do useful work: drive ion gradients, make atp
during glycolysis and the krebs cycle, what happens to H atoms?
-they are stripped away from carbohydrates
-next, they are transferred to NAD+ and FADH to make NADH and FADH2
-the equation then proceeds as follows
NADH + ½ O2 + H+ <> H2O+ NAD+

delta g = -52 kcal/mole
is the oxidation of NADH from oxygen practical?
no because it would require a lot of energy
is the oxidation of NADH coupled to atp synthesis?
it couples it inderectly by allowing small packets of energy to be released at a time
does oxygen have a high or low electron affinity?
high
E’o is a measure of
ΔG’o for the reaction
ΔG’o =
- nFE’o

n=transfer of electrons
a very high electron affinity indicates what?

give one example
a very positive “standard redox potential”, E’o - +0.816 V
Clearly if E’o is very positive
the molecule will have a high electron affinity and will want to accept electrons
why is it bad for NADH to be directly oxidized by oxogyn?

what happens instead?
oxygen has a very high electron affinity and will release too much energy

instead, NADH is oxidized by a molecule with a much lower electron affinity (close to NADH): coenzyme Q (aka. Ubiquinone, UQ or Q)...coenzyme q is the first in a chain of electron carriers

this event is catalyzed by NADH dehydrogenase

the process up to oxygen is sort of like a ladder: electrons are transferred to molecules with higher and higher electron affinities until they reach oxygen

each time electrons are transferred they release energy
NADH dehydrogenase
complex 1

an integral membrane protein found in the mitochondrial matrix

catalyzes the transfer of electrons from NADH and coenzyme Q
describe the carriers of the electron transport chain?
at least 5 types

The carriers of the electron transport chain are of five types (at least) – most are small molecules or atoms imbedded in prosthetic groups within proteins

Flavoproteins – a protein that binds a prosthetic group FAD or FMN (derived from vitamin B2)

Cytochromes – proteins that contain the heme prosthetic group – use the Fe2+/Fe3+ transformation.

Three copper atoms within the mitochondrial membrane. Cu2+/Cu+

Ubiquinone – a small molecule that exists in a pool in the lipid bilayer

Iron-sulfur protein complexes - Fe and S atoms embedded in protein
the electron transport chain can go "fuc ic"