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ORGANIZATION OF
MITOCHONDRIAL
ELECTRON
TRANSPORT CHAIN
SEMINAR REPRESENTED BY
QAMRUNNISA ABDUL WAHID SHAIKH
MSC-I (MICROBIOLOGY)
MB 603-CELLULAR METABOLISM
CONTENT
A.CELLULAR RESPIRATION
a.STEPS INCLUDE IN CELLULAR RESPIRATION
B.ELECTRON TRANSPORT CHAIN
a.MITOCHONDRIAL ELECTRON TRANSPORT CHAIN
b.COMPLEXES OF MITOCHONDRIAL ELECTRON TRANSPORT CHAIN
c.complexes of ETC
COMPLEX I : NADH:ubiquinone oxidoreductase
COMPLEX II: Succinate dehydrogenase
COMPLEX III: Ubiquinone:cytochrome c oxidoreductase
COMPLEX IV:Cytochrome oxidase
COMPLEX V : ATP synthase complex
C.SUMMARY
D.REFRENCES
Cellular respiration is a set of metabolic reactions and processes
that take place in the cells of organisms to convert biochemical
energy from nutrients to  adenosine triphosphate (ATP) and then
release waste products.
Respiration is one of the key ways a cell releases chemical energy
to fuel cellular activity.
Nutrients that are commonly used by animal and plant cells in
respiration include sugar,amino acids and fatty acids, and the most
common oxidizing agent(electron acceptor) is molecular oxygen(O2).
The chemical energy stored in ATP and then be used to drive
processes requiring energy, including biosynthesis, locomotion or
transportation of molecules across cell membranes.
 
CELLULAR RESPIRATION:
STEPS INCLUDE IN CELLULAR
RESPIRATION:
ELECTRON TRANSPORT CHAIN:
An electron transport chain (ETC) is a series of complexes
that transfer electron from electron donor to electron
acceptor via redox (both reduction and oxidation occurring
simultaneously) reactions, and couples this electron transfer with
the transfer of protons (H+
 ions) across a membrane. This creates
an electrochemical proton gradient that drives the synthesis
of adenosine triphosphate (ATP), a molecule that stores energy
chemically in the form of highly strained bonds.
The final acceptor of electrons in the electron transport chain
during aerobic respiration is molecular oxygen although a variety of
acceptors other than oxygen such as sulfate exist in anaerobic
respiration.
MITOCHONDRIAL ELECTRON TRANSPORT
CHAIN:
Most eukaryotic cells have mitochondria, which produce ATP from
products of the citric acid cycle, fatty acid oxidation, and amino acid
oxidation.
At the mitochondrial inner membrane, electrons from NADH
and FADH2 pass through the electron transport chain to oxygen,
which is reduced to water.
The electron transport chain comprises an enzymatic series of
electron donors and acceptors.
 Each electron donor will pass electrons to a more electronegative
 acceptor, which in turn donates these electrons to another acceptor,
a process that continues down the series until electrons are passed to
oxygen, the most electronegative and terminal electron acceptor in
the chain.
Passage of electrons between donor and acceptor releases
energy, which is used to generate a proton gradient across the
mitochondrial membrane by actively pumping protons into the
intermembrane space, producing a thermodynamic state that has
the potential to do work.
The entire process is called oxidative phosphorylation, since ADP
is phosphorylated to ATP using the energy of hydrogen oxidation in
many steps.
NADH+H+
FMN
FeS
FeS
4H
+
NAD+
Q
4H
+
Succinate Fumarate
e-
Cyt c1
FeS
Cyt bL
Cyt bH
Cyt c
CuA
Cyt a
Cyt b3 CuB
½ O2+2H+
H2O
2H
+
Intermembrane
space
Inner
mitochondri
al membrane
Matrix
NADH:ubiquinone oxidoreductase or
NADH dehydrogenase
COMPLEX II: succinate dehydrogenase
ubiquinone:cytochrome c
oxidoreductase
COMPLEX III:
COMPLEX IV: cytochrome c oxidase
F1F0 ATP synthase complex: ATP
synthesis
COMPLEX V :
COMPLEXES OF MITOCHONDRIAL ELECTRON
TRANSPORT CHAIN:
COMPLEX I : NADH to Ubiquinone
NADH:ubiquinone oxidoreductase or NADH dehydrogenase
 It is a large enzyme complex , 850,000 Kd
 composed of 42 different polypeptide chains, including an FMN-
containing flavoprotein and at least six iron sulfur centers.
 Complex I is L-shaped, with one arm of the L in the membrane
and the other extending into the matrix.
NADH + 5H+
N +Q NAD+
+ QH2 +4H+
P
Complex I catalyzes two simultaneous and obligately coupled
processes:
(1) the exergonic transfer of a hydride ion to ubiquinone from
NADH and a proton from the matrix
(2) the endergonic transfer of four protons from the matrix to the
intermembrane space.
Amytal (a barbiturate drug), rotenone (a plant productcommonly
used as an insecticide), and piericidin A (an antibiotic) inhibit
electron flow from the Fe-S centers of Complex I to ubiquinone and
therefore block the overall process of oxidative phosphorylation.
COMPLEX II: Succinate to Ubiquinone
succinate dehydrogenase
It is the only membrane-bound enzyme in the citric acid cycle
It is an integral membrane protein.
it contains five prosthetic groups of two types and four different
protein subunits.
The enzyme contains three different iron-sulfur clusters and one
molecule of covalently bound FAD.
succinate is bound and a hydride is transferred to FAD to generate
FADH2 and fumarate. FADH2 then transfers its e- one at a time to the
Fe-S centers. finally transfer of 2 e-one at a time to coenzyme Q to
produce CoQH2.
No protons are translocated across the inner mitochondrial
membrane by complexII.
Succinate + CoQ Fumarate + CoQH2
Structure of Complex II
Two transmembrane subunits
C - green and D - blue
FAD – gold
Three sets of Fe-S centers - yellow
and red
Ubiquinone - yellow is bound to
subunit C and
heme b - purple is sandwiched
between subunits C and D.
A cardiolipin molecule is so tightly
bound to subunit C that it shows up in
the crystal structure - gray
spacefilling.
Electrons move -blue arrows
from succinate to FAD, then through
the three Fe-S centers to ubiquinone.
COMPLEX III: Ubiquinone to Cytochrome c
Cytochrome bc1 complex or ubiquinone:cytochrome c
oxidoreductase
Complex III has a beautiful dimeric
structure.
The bottom of the structure extends
75 Å into the mitochondrial matrix,
while the top of the structure extends
38 Å out into the intermembrane
space.
Myxothiazol, which prevents
electron flow from QH2 to the Rieske
iron-sulfur protein
Antimycin A, which blocks electron
flow from heme bH to Q
It passes the electrons form
CoQH2 to cyt c through a very unique
electron transport pathway called the
Q-cycle.
Q-CYCLE:
COMPLEX IV: Cytochrome c to O2
Cytochrome oxidase
Complex IV is a large enzyme (13 subunits; Mr 204,000) of the inner
mitochondrial membrane.
It contain two Cu ions complexed with the -SH groups of two Cys
residues in a binuclear center, two heme groups, designated a and a3,
and another copper ion (CuB).
Heme a3 and CuB form a second binuclear center that accepts
electrons from heme a and transfers them to O2 bound to heme a3.
Subunit I –has two heme groups, a and a3
copper ion CuB (green sphere).
Subunit II-contains two Cu ions complexed
with the -SH groups of two Cys residues in a
binuclear center.
Subunit III
Electron transfer through Complex IV is from cytochrome c to the CuA
center, to heme a, to the heme a3–CuB center, and finally to O2.
Path of electrons
through Complex IV
4 Cyt c (reduced) + 8H
+
N + O2 4 cyt c (oxidized) + 4H
+
P + 2H2O
COMPLEX V : F1F0 ATP synthase complex: ATP synthesis
The chemiosmotic model, proposed by
Peter Mitchell.
This enzyme complex embeded in inner
mitochondrial membrane. It synthesized ATP
in matrix, utilizing the energy of the proton
gradient (proton motive force) generated by
the ETC.
Synthesis of ATP in (F1) subunit. Proton
transport is coupled to ATP synthesis
About 4 H+ must move down the gradient for
each ATP produced
Free energy change for pumping one proton
is 20kJ/mol, thus for pumping 10 protons the
energy release is 200KJ/mol.
ATP formation requires 50KJ/mol of energy.
To emphasize this crucial role of the proton motive force, the equation
for ATP synthesis is sometimes written
ADP + Pi + nH+
P ATP + H2O +nH+
N
SUMMARY:
REFRENCES:
www.google.com
www.ncbi.nim.nih.gov.in
Lehninger- principles of biochemistry
THANK
YOU

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Electron transport chain final

  • 1. ORGANIZATION OF MITOCHONDRIAL ELECTRON TRANSPORT CHAIN SEMINAR REPRESENTED BY QAMRUNNISA ABDUL WAHID SHAIKH MSC-I (MICROBIOLOGY) MB 603-CELLULAR METABOLISM
  • 2. CONTENT A.CELLULAR RESPIRATION a.STEPS INCLUDE IN CELLULAR RESPIRATION B.ELECTRON TRANSPORT CHAIN a.MITOCHONDRIAL ELECTRON TRANSPORT CHAIN b.COMPLEXES OF MITOCHONDRIAL ELECTRON TRANSPORT CHAIN c.complexes of ETC COMPLEX I : NADH:ubiquinone oxidoreductase COMPLEX II: Succinate dehydrogenase COMPLEX III: Ubiquinone:cytochrome c oxidoreductase COMPLEX IV:Cytochrome oxidase COMPLEX V : ATP synthase complex C.SUMMARY D.REFRENCES
  • 3. Cellular respiration is a set of metabolic reactions and processes that take place in the cells of organisms to convert biochemical energy from nutrients to  adenosine triphosphate (ATP) and then release waste products. Respiration is one of the key ways a cell releases chemical energy to fuel cellular activity. Nutrients that are commonly used by animal and plant cells in respiration include sugar,amino acids and fatty acids, and the most common oxidizing agent(electron acceptor) is molecular oxygen(O2). The chemical energy stored in ATP and then be used to drive processes requiring energy, including biosynthesis, locomotion or transportation of molecules across cell membranes.   CELLULAR RESPIRATION:
  • 4. STEPS INCLUDE IN CELLULAR RESPIRATION:
  • 5.
  • 6. ELECTRON TRANSPORT CHAIN: An electron transport chain (ETC) is a series of complexes that transfer electron from electron donor to electron acceptor via redox (both reduction and oxidation occurring simultaneously) reactions, and couples this electron transfer with the transfer of protons (H+  ions) across a membrane. This creates an electrochemical proton gradient that drives the synthesis of adenosine triphosphate (ATP), a molecule that stores energy chemically in the form of highly strained bonds. The final acceptor of electrons in the electron transport chain during aerobic respiration is molecular oxygen although a variety of acceptors other than oxygen such as sulfate exist in anaerobic respiration.
  • 7. MITOCHONDRIAL ELECTRON TRANSPORT CHAIN: Most eukaryotic cells have mitochondria, which produce ATP from products of the citric acid cycle, fatty acid oxidation, and amino acid oxidation. At the mitochondrial inner membrane, electrons from NADH and FADH2 pass through the electron transport chain to oxygen, which is reduced to water. The electron transport chain comprises an enzymatic series of electron donors and acceptors.  Each electron donor will pass electrons to a more electronegative  acceptor, which in turn donates these electrons to another acceptor, a process that continues down the series until electrons are passed to oxygen, the most electronegative and terminal electron acceptor in the chain.
  • 8. Passage of electrons between donor and acceptor releases energy, which is used to generate a proton gradient across the mitochondrial membrane by actively pumping protons into the intermembrane space, producing a thermodynamic state that has the potential to do work. The entire process is called oxidative phosphorylation, since ADP is phosphorylated to ATP using the energy of hydrogen oxidation in many steps.
  • 9. NADH+H+ FMN FeS FeS 4H + NAD+ Q 4H + Succinate Fumarate e- Cyt c1 FeS Cyt bL Cyt bH Cyt c CuA Cyt a Cyt b3 CuB ½ O2+2H+ H2O 2H + Intermembrane space Inner mitochondri al membrane Matrix
  • 10. NADH:ubiquinone oxidoreductase or NADH dehydrogenase COMPLEX II: succinate dehydrogenase ubiquinone:cytochrome c oxidoreductase COMPLEX III: COMPLEX IV: cytochrome c oxidase F1F0 ATP synthase complex: ATP synthesis COMPLEX V : COMPLEXES OF MITOCHONDRIAL ELECTRON TRANSPORT CHAIN:
  • 11. COMPLEX I : NADH to Ubiquinone NADH:ubiquinone oxidoreductase or NADH dehydrogenase  It is a large enzyme complex , 850,000 Kd  composed of 42 different polypeptide chains, including an FMN- containing flavoprotein and at least six iron sulfur centers.  Complex I is L-shaped, with one arm of the L in the membrane and the other extending into the matrix. NADH + 5H+ N +Q NAD+ + QH2 +4H+ P
  • 12. Complex I catalyzes two simultaneous and obligately coupled processes: (1) the exergonic transfer of a hydride ion to ubiquinone from NADH and a proton from the matrix (2) the endergonic transfer of four protons from the matrix to the intermembrane space. Amytal (a barbiturate drug), rotenone (a plant productcommonly used as an insecticide), and piericidin A (an antibiotic) inhibit electron flow from the Fe-S centers of Complex I to ubiquinone and therefore block the overall process of oxidative phosphorylation.
  • 13. COMPLEX II: Succinate to Ubiquinone succinate dehydrogenase It is the only membrane-bound enzyme in the citric acid cycle It is an integral membrane protein. it contains five prosthetic groups of two types and four different protein subunits. The enzyme contains three different iron-sulfur clusters and one molecule of covalently bound FAD. succinate is bound and a hydride is transferred to FAD to generate FADH2 and fumarate. FADH2 then transfers its e- one at a time to the Fe-S centers. finally transfer of 2 e-one at a time to coenzyme Q to produce CoQH2. No protons are translocated across the inner mitochondrial membrane by complexII. Succinate + CoQ Fumarate + CoQH2
  • 14. Structure of Complex II Two transmembrane subunits C - green and D - blue FAD – gold Three sets of Fe-S centers - yellow and red Ubiquinone - yellow is bound to subunit C and heme b - purple is sandwiched between subunits C and D. A cardiolipin molecule is so tightly bound to subunit C that it shows up in the crystal structure - gray spacefilling. Electrons move -blue arrows from succinate to FAD, then through the three Fe-S centers to ubiquinone.
  • 15. COMPLEX III: Ubiquinone to Cytochrome c Cytochrome bc1 complex or ubiquinone:cytochrome c oxidoreductase Complex III has a beautiful dimeric structure. The bottom of the structure extends 75 Å into the mitochondrial matrix, while the top of the structure extends 38 Å out into the intermembrane space. Myxothiazol, which prevents electron flow from QH2 to the Rieske iron-sulfur protein Antimycin A, which blocks electron flow from heme bH to Q It passes the electrons form CoQH2 to cyt c through a very unique electron transport pathway called the Q-cycle.
  • 17. COMPLEX IV: Cytochrome c to O2 Cytochrome oxidase Complex IV is a large enzyme (13 subunits; Mr 204,000) of the inner mitochondrial membrane. It contain two Cu ions complexed with the -SH groups of two Cys residues in a binuclear center, two heme groups, designated a and a3, and another copper ion (CuB). Heme a3 and CuB form a second binuclear center that accepts electrons from heme a and transfers them to O2 bound to heme a3. Subunit I –has two heme groups, a and a3 copper ion CuB (green sphere). Subunit II-contains two Cu ions complexed with the -SH groups of two Cys residues in a binuclear center. Subunit III
  • 18. Electron transfer through Complex IV is from cytochrome c to the CuA center, to heme a, to the heme a3–CuB center, and finally to O2. Path of electrons through Complex IV 4 Cyt c (reduced) + 8H + N + O2 4 cyt c (oxidized) + 4H + P + 2H2O
  • 19. COMPLEX V : F1F0 ATP synthase complex: ATP synthesis The chemiosmotic model, proposed by Peter Mitchell. This enzyme complex embeded in inner mitochondrial membrane. It synthesized ATP in matrix, utilizing the energy of the proton gradient (proton motive force) generated by the ETC. Synthesis of ATP in (F1) subunit. Proton transport is coupled to ATP synthesis About 4 H+ must move down the gradient for each ATP produced Free energy change for pumping one proton is 20kJ/mol, thus for pumping 10 protons the energy release is 200KJ/mol. ATP formation requires 50KJ/mol of energy. To emphasize this crucial role of the proton motive force, the equation for ATP synthesis is sometimes written ADP + Pi + nH+ P ATP + H2O +nH+ N