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17 Cards in this Set

  • Front
  • Back
redox state of C=
=4-(2nh+nc)

h=bonds to h
c=bonds to c
4 main types of e- transfer
-directly as e-
-as H (H+ + e-) -> eg. FADH2/FADH
-as hydride (H-) -> eg. NADH/NADH+
-direct combo w/ O2
NAD (3)
(incl: what made out of)
-nicotinamide adenine dinucleotide
-most common e- carrier
-made from vita B + niacin
-hydride transfer
coenzyme Q
-e- carrier
-lipophilic (travels in hydrophobic membrane)
- Q->QH2
prosthetic group of cytochromes (including cyt c)
-heme
copper
- e- carrier
-protein cofactor
-each Cu bound to 3 his side chains
FeS clusters
- e- carrier
-protein cofactor
-each bound to 4 cys side chains
mitochondrial structure
-outer membrane
-intermembrane space
-inner membrane
-matrix
What is found in the mitochondrial matrix?
-enzymes for Krebs cycle, ox of fatty acids, pyruvate, etc
ETC overview:
main source of e-
main parts
transfer parts
final e- acceptor
(E- transport chain)
- most e-'s from NADH
-3 transfer proteins: complexes I, III, & IV
-Q and cytochrome c
-O2
stoichiometry of ETC

delta G
NADH + H+ +1/2O2 -> NAD+ + H2O

delta G = -53 kcal/mol
alternate source of e- in ETC
-FADH2 via complex II
NADH-Q reductase:
size
net rxn
H+'s moved
(complex I)
-34 polypep chains
- NADH + H+ + Q -> NAD+ + QH2
-4 H+ out of matrix
Cytochrome reductase:
size
net rxn
H+'s moved
(complex III)
-11 ppep chains
- QH2 + 2cyt c(FeIII) -> 2H+ + Q + 2 cyst c(FeII)
-2H+ out of matrix (into cytosol)
Cytochrome oxidase:
net equation
H+'s moved
dangerous biproducts
(complex IV)
-4H+ + [4e-]+O2->2H20+4H++4cytc(FeII)+O2-> 2H20+4cytc(FeIII)
-4H+
- H2O2, O2- (superoxide)
How does cytochrome oxidase avoid forming dangerous side products?
(H202, 02-)
-4cyt c feeds e- 1 at a time through CuA & heme Fe to binuclear (bimetallic) center
what is the function of the binuclear center in cytochrome oxidase?
-binds 02 and stabilizes intermediate while e- is being transfered to them