1

Electron Transport
and
Oxidative Phosphorylation
General Biochemistry
2012
Glucose Oxidation (Glycogen)
1.Phase glycolysis (glycogenolysis)
2.Phase citric acid cycle
3.Phase electron transport and
oxidative phosphorylation
2
Electron Transport
Localization: inner mitoch. membrane
Cristae the density of cristae is related to
the respiratory activity of a cell

Energy: the oxidation of NADH and
FADH
2
will produce most of the ATP
generated by the oxidation of Glc
3
Mitochondrion
4
The Electron Transport Chain
Complex I (NADH-coenzyme Q reductase)
FMN (1x)
Fe-S centers (6-7x)

Complex II (succinate-coenzyme Q reductase)
Succinate dehydrogenase (1xdimer), FAD (2x)
Fe-S centers (9x)
Cyt b
560
The Electron Transport Chain
Complex III (coenzyme Q-cyt c reductase)
Cyt b (2x)
Fe-S centers (1x)
Cyt c
1
(1x)

Complex IV (cyt c oxidase)
Cyt a
Cu (2x)
Cyt a
3
5
Complex I
The largest enzyme of inner mitochondrial membrane,
26 subunits (850 kDa)
NADH FMN Fe-S CoQ
-0,32 -0,30 +0,04
FMN
All forms are stable
Ability to accept or donate 1 or 2 e
-
6
Fe-S centers
Fe in each center forms conjugative system (+2; +3)
Coenzyme Q
7
Complex II
5 subunits = dimer of succinate dehydrogenase,
3 other small hydrophobic subunits, (127 kDa)
succinate FAD Fe-S cyt b
560
CoQ
+0,030 -0,040 -0,080 +0,045
it is not proton pump because the free-energy
change of the catalyzed reaction is too small
important for electron enter (with relatively high
potential) into the electron transport chain

FAD
8
Complex III
10 subunits, (280 kDa)
CoQ cyt b
562
cyt b
566
Fe-S cyt c
1
cyt c
+0,045 +0,030 -0,030 +0,215 +0,235
Cytochromes: Hem Proteins
9
Cytochromes: Hem Proteins
Cytochrome c
10
Complex IV
Dimer protein, 6-13 subunits, (160-200 kDa)
cyt c cyt a Cu
A
Cu
B
cyt a
3
O
2

+0,235 +0,210 +0,245 +0,340 +0,385 +0,815
4 cyt c
2+
+ 4H
+
+ O
2
4 cyt c
3+
+ 2H
2
O
Complex IV Electron Transport

Fe
II
-O-O-Cu
I
Fe
III
-O
-
-O
-
-Cu
II
Fe
II
-OH-O
-
-Cu
II
Fe
IV
=O +
-
HO-Cu
II

Fe
III
-OH
-
+
-
HO-Cu
II
2H
2
O + Fe
III
+ Cu
II

11
Q Cycle
Redox Potential Changes
12
1978 Peter D. Mitchell Nobel Prize for Chemistry
Complex V
ATP-synthase
2 subunits
Generation of a proton
gradient permits ATP
synthesis
Changes by H
+
translocation
13
ATP Synthesis
F1 unit has 3 catalytic b subunits, which are
intrinsically identical but are not functionally
equivalent at any particular moment
L=loose binds the substrates loosely and is catalycally inactive
T=tight binds them tightly and is active
O=open has very low affinity for substrates
1997 (Paul D. Boyer, John E. Walker, Jens C. Skou) Nobel Prize for Chemistry
Uncoupling of Oxidative
Phosphorylation
14
Respiratory Control
Control by substrate availability
ADP, Pi, O2, NAD+, FAD+
Cytochrome oxidase
Regulatory enzyme
Control by substrate availability reduce form of cyt c (c
2+

)
[c2+]/[c3+] = ([NADH]/[NAD+]) x ([ADP][Pi]/[ATP])
Regulation by acceptor regulaion by ATP/ADP