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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): 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

WHAT YOU NEED TO KNOW!! You should: should

understand how the energy gy from the transport p 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 FADH2 oxidized. oxidized 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 onon-line testing)

Fig. 5.1 The catabolism of various food molecules

Fig. 5.2 Free-energy change during electron transport

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

Fig. 5.4a: Essence of oxidative phosphorylation

Oxidation and ATP synthesis are coupled by transmembrane proton fluxes

From: Biochemistry (5th edition) Berg, Tymoczico and Stryer)

Fig 5.4b Schematic representation of the link between respiration and p ATP production Step 1 Step 2

PROTON MOTIVE FORCE (CHEMI-OSMOTIC GRADIENT) Step 3

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

Animation: Chemiosmosis: How the mitochondrial membrane couples electron transport to oxidative phosphorylation

FAD FADH2

Fig. 5.5 Chemiosmosis

Oxidized and reduced form of Coenzyme Q/Ubiquinone

Succinate Dehydrogenase

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 4 CYTOCHROME c OXIDASE- contains heme and Cu

CYTOCHROME c and CoQ

Fig. 6.5 Chemiosmosis

Electron Micrograph of mitochondrion showing ATP Synthase

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Fig 5.6: ATP synthase, a molecular machine

INTERMEMBRANE SPACE

H+ Rotor

H+ ions flowing down their gradient enter a half channel in a stator, which is anchored in the membrane. H+ ions enter binding sites within a rotor, changing the shape of each subunit so that the rotor spins within the membrane membrane. Each H+ ion makes one complete turn before leaving the rotor and passing through a second half channel in the stator into the mitochondrial matrix. Spinning of the rotor causes an internal rod to spin as well. This rod extends like a stalk into the knob below it, which is held stationary by part of the stator.

Stator

Internal rod Catalytic knob ADP + P


i

ATP

MITOCHONDRIAL MATRIX

Turning of the rod activates catalytic sites in the knob that produce ATP from ADP and Pi.

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