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Transport Electron

Final step for making ATP


through oxydative
phosphorylation

Donald John Calvien H


Outline

 Basic molecules for ox. Phosphorylation and location


 Membrane and components
 Mitochondria and electron transfer
 Electron transport chain
 Principles of energy conservation in membrane
(photon gradient and chemical osmosis)
 ATP synthesis
Overview
Membrane and cell
organization
Intracellular is protected from external
environment by membrane
Membrane is selective (Selective for
substrate; eg. glucose and amino acid
transport proteins.
Comprises of two parts:
 Phospholipid bi-layer
 Embedded proteins (tansmembrane)
Phospholipid bi-layer
 Basis: diacylglycerol, third OH
glycerol bound to polar "head
group" derivative of phosphate
ester .
 Acyl group; long hydrocarbon non
polar
 Phospholipids are joined via
hydrophobic interactions
between “tail” and polar
interactions between “heads” and
H2O.
 Hydrocarbon tails located away
from H2O; bi-layer, sandwich in
2-D.
Embedded proteins
(transmembrane)

• Spans bi-layer, bundle of alpha helix, beta-barrels


• Peripheral membrane proteins located on membrane
surface, structural function.
Ubiquinone : non-protein
for electron transport

Consists of outer and inner


membrane.
Transport electron
for ATP producion
• Mitochondria : Oxidative Phosphorylation
• Chloroplast : Photosynthetic
phosphorylation
Nobel Prize in Chemistry 1978 Peter Mitchell (1920-1992)
Glynn research Laboratories, United Kingdom

electron transport + ATP synthase = oxidative phosphorylation system.

Chemiosmotic :

• Electron transport system releases


energy which allows certain carriers
in the chain to transport H+ or
protons) across a membrane.
• The energized state as a result of
charge separation is called proton
motive force or PMF.
Generation of ATP occurs as
protons cross membrane and re-
Slide Title enter either the bacterial
cytoplasm or stroma (Cloroplast)
or matrix mitochondria.

As protons move down


concentration gradient through
the ATP synthase, the energy
released causes the rotor (F0) and
stalk of ATP synthase to rotate

The mechanical energy from the rotation is converted into


chemical energy as P is added to ADP to form ATP in the
catalytic head (F1 domain).
NADH and FADH2
oxidation
• NADH oxidation to NAD+ • FADH oxidation to FAD+ by
by O2 O2
 1/2 O2 + NADH+ H+ → H2O + NAD+  1/2 O2 + FADH2+ H+ → H2O + NAD+
 ΔE°’ = E°’ acceptor - E°’ donor  ΔG°’ = approx. -140 kJ/mol
 ΔE°’ = + 0.815 - (-0.321) = +1.136 V  FADH2 oxidation involves
 ΔG°’ = - n F ΔE°’ production 1.5 ATP
 ΔG°’ = - 2 x 96.485 x 1.136 = - 219.2
kJ/mol
 NADH oxidation involved in ADP
condenstaion with Pi to form ATP
(ΔG°’ = +30.3 kJ/mol).
 2.5 ATP / NADH ; 75.8 kJ.
 Reaction occurs at high ratio
[ATP]/[ADP]
Electron transport complex

• Oxidation and reduction: electron transfer between


reactants.
• NADH and FADH2 oxidation is gradual, where electron is
used to reduce O2, known as electron transport (transport
from NADH to O2).
• Steps are catalyzed by proteins on inner membrane known
as electron transport complexes I-IV.
• There is a mech. to capture energy from oxidation to
synthesize ATP.
The electron transport
system
• Divides oxidation-reduction process for better energy.
• 2 intermediate mol. Accept and transfer electrons.
• 4 electron transport complexes:
 complex I : NADH dehydrogenase (ubiquinone)
 complex II : Succinate dehydrogenase
 complex III : Ubiquinol-cytochrome-c reductase
 complex IV : Cytochrome-c-oxidase
• complex V : H+ transporting ATP synthase
Melepaskan e : oxidized
Menerima e : reduced
•The electron carriers of the respiratory
chain are organized into membrane-
embedded supramolecular complexes that
can be physically separated

Complexes I and II catalyze electron


transfer to ubiquinone from two
different electron donors: NADH
(Complex I) and succinate (FADH2)
(Complex II).
Complex I
(NADH:UQ reductase)
• NADH entrance
• Pathway: FMN, Cluster
4Fe.4S and Ubiquinone
• transfers 4H+ to
intermembrane space
Complex II
(Succinate dehydrogenase )

• FADH2 (succinate)
entrance
• Accepted by ubiquinone
• End product: Ubiquinol
Complex III (Ubiquinol-
cytochrome-c reductase)
 Ubiquinol entrance (UQH2)
 Pathway:
 Cyt b, UQ, 2Fe.2S, Cyt C1,
Cyt C (FeIII)
 2Fe.2S, Cyt C1, Cyt C
(FeIII)
 transfers 4H+ to
intermembrane space
 only transport one electron
from UQH2 to cytochrome c
at a time it must occur in 2
stages called Q cycle
Complex IV
(Cytochrome-c-oxidase)
• Input Cyt C (FeII)
• Pathway
CuA, Cyt a, Cyt a3, CuB,
Oksigen
• End product: H2O
Principles of energy
conservation in membrane
Effect of Chemicals
• Complex I, III and
IV as proton pump
• 1 NADH : 10H+ by
complex I, III and
IV
• 1 FADH : 6H+ by
complex III and IV

•Difference in H+ conc. (Diff. pH and


Diff. potential )
•Proton motive force
ATP synthesis
• H+ return into matrix
• 3 H+ req. to move rotor ATP synthase.
– (Phosphate re-enters the matrix with H+
by an electroneutral symport
mechanism. Pi entry is driven by, & uses
up, the pH gradient (equivalent to one
F1 mol H+ per mol ATP).
– Thus the equivalent of one mol H+
enters the matrix with ADP/ATP
exchange & Pi uptake. Assuming 3H+
Fo transported by F1Fo, 4H+ total enter the
matrix per ATP synthesized.)
• Rotor comprised of 3 compartments.
• Each comp. functions:
 Bind ADP and Pi
 Combine ADP and Pi to form ATP
 release ATP
ATP synthesis - Adenine
nucleotide and phosphate translocases
ATP synthesis

 H+ that re-enters matrix


 3H+ used for ATP synthesis
 1H+ for Phosphate re-enters the matrix
 Total 4 H+ returns into matrix
 For NADH
 Net result complex I, III, and IV : 10 H+ / NADH
 ATP ready for use: 10 / 4 = 2,5 ATP
 For FADH2
 Net result complex III and IV : 6H+ /FADH2
 ATP ready for use : 6/4 =1.5 ATP
Asam bongkrek,
Bongkrekic acid

Tempe gembus/bongkrek
Gembus tempe
ATP synthesis in
photosynthesis
 Proton accumulated in
thylakoid space.
 Concentration gradient
between inside and outside
as energy source for ATP
synthase.
 Proton passes through CF0-
CF1 ATP Synthase
 This movement activates
conversion of ADP and Pi into
ATP.
Thank You

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