218 |
A Handbook of Biology
The reduced ubiquinone
(ubiquinol or UQH ) is then
oxidized with the transfer
of electrons to cytochrome
c
via
cytochrome
bc1
complex
(complex
III).
Cytochrome c is a small
protein attached to the
outer surface of the inner
membrane. It acts as a
mobile carrier of electrons
between complex III and
IV.
Complex
IV
refers
to
cytochrome
c
oxidase
complex
containing
cytochromes a & a3, and 2
copper centers.
When the electrons pass
from one carrier to another
via complex I to IV, they are coupled to ATP synthase (complex V) for the
ATP production.
In aerobic respiration, the role of oxygen is limited to the terminal
stage. Yet, oxygen is vital since it drives the whole process by removing
hydrogen from the system. Oxygen acts as the final hydrogen acceptor.
In respiration, energy of oxidation-reduction is utilized for the
phosphorylation. So this process is called oxidative phosphorylation while
in photophosphorylation where, light energy is utilized for the production
of proton gradient for phosphorylation. Mechanism of membrane linked
ATP synthesis is explained by chemiosmotic hypothesis.
The energy released during the ETS is utilized to synthesize ATP by ATP
synthase (complex V).
ATP synthase has two major components: F1 & F0.
ADP
F0
F1
ATP
Outer
side
2H+
Pi
Matrix
Inner
mitochondrial
membrane
F0
F0
(integral
membrane
protein complex): It creates
a pathway for protons to pass
through the inner membrane.
The transport of protons is
coupled to the F1 component’s
catalytic site for ATP synthesis.
F1
F1 headpiece (peripheral
membrane
protein
complex):
Site
for
ATP
production
from
ADP
and
inorganic phosphate.
Inter-membrane
space
Inner Mitochondrial
membrane
Matrix
4H+
4H+
2H+
2H+
Electrochemical
gradient
NADH + H+
NAD+
Complex I
(NADH dehydrogenase)
Complex III
(Cytochrome bc!)
Complex II
(Succinate dehydrogenase)
Succinate
Fumarate
Cyt c
Cyt c
H2O
Complex IV
(Cytochrome c oxidase)
ADP + Pi
ATP
H+
Cu"
CuB
Cyta
Cyta#
IV
F1
F0
ATP
synthase
(Fe-s)
FAD
UQH$
UQH$
Cyt C1
Fe-S
Cyt b
e-
(Fe-S)
FMN
2e-
e-
e-
e-
e-
e-