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Lecture 6 Oxidative Phosphorylation
Lecture 6 Oxidative Phosphorylation
Lecture 6 Oxidative Phosphorylation
OXIDATIVE PHOSPHORYLATION
FUNDAMENTAL BIOCHEMISTRY
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Learning objectives
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Contents
1. INTRODUCTION
2. CHEMIOSMOTIC THEORY
3. ELECTRON TRANSPORT CHAIN
4. ATP SYNTHASE
5. CONCLUSION
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Activities
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Introduction
Living cells:
• synthesize macromolecules
• exchange substances with the environment
• move or change shape
• grow and reproduce
require energy from outside sources.
H+ H+
ADP ATP
Cytoplasm
Periplasmic space
CHEMIOSMOTIC THEORY
• NADH/FADH2 provide energy for electron
transport create an electrochemical proton
gradient
• electrochemical
proton gradient
create proton-motive
force drive ATP
synthase synthesize
ATP
Chemiosmosis can be found in photosynthesis
Electron Transport Chain
Electron Transport Chain
Complex I (NADH dehydrogenase)
Complex II (Succinate dehydrogenase)
Complex III (Cytochrome bc complex)
Complex IV (Cytochrome c oxidase)
ATP synthase
• Definition
- A kind of membrane
protein which acts as a ATP
powered pump
- Belongs to F class proton
pumps (F-type)
- Also called ATPase , F1F0
ATPase or Complex V of
which function is
transporting protons in the
form of hydrogen ions and
catalyzing the ATP synthesis
Location Bacterial plasma membrane
inner
membrane
matrix
Mitochondrion
E. coli
thylakoid
membrane
ATP
synthase
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Some images of ATPase
Structure
• F0 component (intergral
protein)
- Hydrophobic segment water-
insoluble protein
- Seemed as a stalk
- Proton channel transport
hydrogen ions
- Up to 8 different subunits (a,b,c)
• F1 component (peripheral
protein)
- Hydrophilic segment water-
soluble protein
- Seemed as a knob
- Contains catalytic subunits
catalyze ATP hydrolysis
- 5 different subunits (33)
Mechanism of rotary engine
Stator
(ab2–33)
Protons through the
channel the rotor spin
in one direction the
stator spin in opposite
direction
Rotor
(–c12)
Binding-change mechanism of ATP synthase
Binding-change mechanism of ATP synthase
- Open state: newly synthesized ATP can be released one molecule of ADP
and one molecule Pi bind to an open site
- Loose state: Passage of protons conformation change ADP + Pi bind
more firmly
- Tight state: ADP + Pi are very tightly bound ATP synthesis ATP will be
released in the next open conformation
ADP + Pi ATP
F1 3H +
matrix
Fo
intermembrane
space
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Thank you for your kindly listening
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