biochemistry lect 5 2011 colour 2 slides per page
TRANSCRIPT
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8/13/2019 Biochemistry Lect 5 2011 Colour 2 Slides Per Page
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Fig. 4.6 Control of the
citric acid cycle
From: Biochemistry, 5th Edition,
Berg, Tymoczico and Stryer
LECTURE 5: You just cant get away from
electrons!
Key Concepts (the big picture):Key Concepts (the big picture):
the energy from the oxidation of fuels is converted to
ATP by the process of oxidative phosphorylation
oxidative phosphorylation involves the transfer of
electrons to oxygen and the synthesis of ATP
oxidative phosphorylation takes place in mitochondria
the location and number of mitochondria is correlated
with the energy demands of different tissues
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WHAT YOU NEED TO KNOW!! You shouldWHAT YOU NEED TO KNOW!! You should:
understand how the ener from the trans ort of
electrons to O2 is transformed into the high energy
phosphate bonds of ATP.
understand why the net yield of oxidative
phosphorylation is about 1.5 2.5 moles of ATP per
mole of NADH oxidized or 1.5 moles of ATP per mole of
.
be familiar with the electron transport carriers which
transfer electrons from NADH/FADH2 to O2
understand the chemiosmotic coupling hypothesis
and the role of ATP synthase
Reading: (for onReading: (for on--line testing)line testing)
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Fig. 5.1 The catabolism of various food molecules
Fig. 5.2 Free-energy change during electron transport
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Fig 5.3: Oxidative metabolism in mitochondria
Starvation and stress-induced elongation of mitochondria.
- starvation elicits a number of cellular responses to retrieve nutrients
- mitochondrial fusion enhances ATP production
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Fig. 5.4a: Essence of oxidative phosphorylation
From: Biochemistry (5th edition) Berg, Tymoczico and Stryer)
Oxidation and ATP synthesis are coupled by transmembrane proton fluxes
Fig 5.4b Schematicrepresentation of
the link between
respiration and
ATP roduction
Step 1
Step 2
Step 3
PROTON MOTIVE FORCE(CHEMI-OSMOTIC
GRADIENT)
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From Bioenergetics An Introduction to the Chemiosmotic Theory
David G. Nicholls. Academic Press London New York 1982
Animation: Chemiosmosis: How the mitochondrial membrane
couples electron transport to oxidative phosphorylation
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Animation: Chemiosmosis: How the mitochondrial membrane
couples electron transport to oxidative phosphorylation
FADH2
FAD
Fig. 5.5 Chemiosmosis
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ELECTRON TRANSFER COMPLEXES
COMPLEX 1
NADH DEHYDROGENASE contains FMN and FeS
COMPLEX 2
SUCCINATE DEHYDROGENASE- contains FAD and FeS
COMPLEX 3
CYTOCHROME bc1 contains heme and FeS
COMPLEX 4CYTOCHROME c OXIDASE- contains heme and Cu
CYTOCHROME c and CoQ
Fig. 6.5 Chemiosmosis
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Electron Micrograph of mitochondrion
showing ATP Synthase
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INTERMEMBRANE SPACE
Rotor
H+
Stator
H+ ions flowing down theirgradient enter a half channel in
a stator, which is anchored in
the membrane.
H+
ions enter binding siteswithin a rotor, changing the
shape of each subunit so that
the rotor spins within the
Fig 5.6: ATP
synthase, a
molecular
machine
Internalrod
Cata-
.
Each H+ ion makes onecomplete turn before leaving
the rotor and passing through a
second half channel in the
stator into the mitochondrial
matrix.
Spinning of the rotorcauses an internal rod to s in
lyticknob
ADP+
P ATPi
MITOCHONDRIAL MATRIX
as well. This rod extends like a
stalk into the knob below it,
which is held stationary by part
of the stator.
Turning of the rod activatescatalytic sites in the knob that
produce ATP from ADP and Pi.