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Biochemistry Lect 5 2011 Colour 2 Slides Per Page
Biochemistry Lect 5 2011 Colour 2 Slides Per Page
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
- starvation elicits a number of cellular responses to retrieve nutrients - mitochondrial fusion enhances ATP production
Fig 5.4b Schematic representation of the link between respiration and p ATP production Step 1 Step 2
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
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
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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
ATP
MITOCHONDRIAL MATRIX
Turning of the rod activates catalytic sites in the knob that produce ATP from ADP and Pi.
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