Glycogen, TCA Cycle and Mitochondria (Lecture 12) Flashcards
outer mitochondrial membrane
porous, ions diffuse
phospholipid synthesis
inner mitochondrial membrane
invaginations increase the surface area.
impermeable to ion transport and other molecules
ETC
oxidative phosphoryaltion
mitochondrial matrix
PDC CAC Glutamate DH FA oxidation urea cycle replication transcription/ translation
what is oxidative phosphorylation?
protein complexes take e- from NADH and FADH2. the free energy released by the e- is coupled to the transfer of protons from the matrix to the inner membrane space
H+ is pumped by complex I, III, IV complex II (succinate dehydrogenase) doesn't pump out H+ the reentry of the H+ from the inter membrane space to the matrix is coupled too the rotational torque of ATP synthase to generate energy
why is H+ pumped into the inter membrane space?
generate an electrochemical gradient, a proton motive force
the ETC transports e- form ____ to _____ potential
low potential to high potential
what is special about complex II?
does not pump protons into the matrix
it is invoiced in the CAC
what are the redox centers (prosthetic groups) to accept and release electrons? and which complexes are they associated to?
complex I and II are known as flavo proteins, because they contain flavo mono-nucleotide (FMN) and flavin adenine di-nucleotide (FAD) respectively
complex III (and 2) contain cytochromes which functions to accept and release electrons
purpose of iron sulphur (Fe-S) centres?
pass along the electrons
the sulphur in the cysteine residues will bid to iron, and Theron gains/loses electrons
what is coenzyme Q
e- carrier that is extremely hydrophobic, thus it can diffuse within the mitochondria trial membrane
both electrons form compels I and II feed into coenzyme Q
it will give the e- to complex III
what is cytochrome C
hydrophobic carrier to carry e- to complex IV
cytochrome are complexes to metals to allow for the accepting or release of e-
where does O2 get reduced?
after H+ have passed complex IV, where it is reduced to H2O
4 e-
electron path in the ETC
in complex I, NADH will reduce electrons and pass it to FMN–> Fe-S
OR
succiante carries electrons to FAD–> Fe-S –> cytochrome
coenzyme Q will travel in the mitochondrial membrane to deliver e-
in complex III, e- will be accepted and released by cytochromes coupled to Fe-S
cytochrome C will carry e-
in complex IV, e- will be accepted and released by Cooper (Cu) and cytochromes. eventually, O2 is reduced to water
proton motive force is identified by complex V (ATP synthase), which generates ATP
Complex I
NADH -Coenzyme Q reductase
main donor of e- is NADH
the e- will travel down the FMN, iron sulphur centre
e- will reduce coenzyme Q
2 functions of complex I
- catalyses the transfer of 2 e- from NADH to FMN, which then transfers e- to the Fe-S clusters 1 at a time (this oxidized NADH)
- transfer of 4 H+ into the inner membrane space (reduction of CoQ drives this)
e- transfer causes a conformational change in the transmembrane arm (perpendicular to other proteins) , which supports proton pumping . this back and forth perpendicular movement of th protein, will open/shut the H+ channel