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• Electron transport chain
• Inhibitors of electron transport chain
Definition:
The electron transport chain is a series of
electron transporters embedded in the
inner mitochondrial membrane that
shuttles electrons from NADH and
FADH2 to molecular oxygen
The energy-rich carbohydrates, fatty acids, amino
acids undergo a series of metabolic reactions and,
finally, get oxidised to CO2 and H2O.
The reducing equivalents from various metabolic
intermediates are transferred to coenzymes NAD*
and FAD to produce, respectively, NADH and FADH2.
 The latter two reduced coenzymes pass through
the electron transport chain (ETC) or respiratory
chain and, finally, reduce oxygen to water.
The passage of electrons through the ETC is
associated with the loss of free energy. A part of this
free energy is utilized to generate ATP from ADP and
Pi
Overview of electron transport chain
(A-Substrate; F,-Flavoprotein ; Cyts Cytochromes).
Mitochondrial matrix : The interior ground
substance forms the matrix of
mitochondria.l t is rich in the enzymes
responsible for the citric acid cycle, beta-
oxidation of fatty acids and oxidation of
amino acids.
The mitochondrion consists of five distinct
parts. These are the outer membrane, the
inner membrane, the intermembranes
pace,the cristae and the matrix
Mitochondrial organisation
Mitochondrion organisation
depiciting electron transport chain
Structural organisation of respiratory
chain
• The inner mitochondrial membrane can be
disrupted into five distinct respiratory or
enzyme complexes, denoted as complex I, Il,
III,IV and V .
• The complexes l-lV are carriers of Electrons
while complex V is responsible for ATP
synthesis.
Continued….
• Besides these enzyme complexes there are
certain mobile electron carriers in the
respiratory chain. These include NADH,
coenzyme Q, cytochrome C and oxygen
Multiprotein complexes in electron
transport chain
Components and reactions of
electron transport chain
• There are five distinct carriers that participate
in the electron transport chain (ETC).
• These carriers are sequentially arranged and
are responsible for the transfer of electrons
from a given substrate to ultimately combine
with proton and oxygen to form water.
1. Nicotinamide nucleotides
• Of the two coenzymes NAD+ and NADP+ derived
from the vitamin niacin, NAD+ is more actively
involved in the ETC. NAD+ is reduced to NADH + H+
by dehydrogenases with the removal of two
hydrogen atoms from the substrate (AH2).
• The substrates include glyceraldehyde-3phosphate,
pyruvate,i socitrate, alpha-ketoglutarate and malate.
AH2 + NAD+ A+ NADH + H+
2. Flavoproteins
• The enzyme NADH dehydrogenase
(NADHcoenzyme Q reductase) is a
flavoprotein with FMN as the prosthetic
group. The coenzyme FMN accepts two
electrons and a proton to form FMNH2. NADH
dehydrogenase is a complex enzyme closely
associated with non-heme iron proteins (NHl)
or iron-sulfur proteins (FeS).
NADH + H + FMN NAD + FMNH2
3. Iron-sulfur proteins
• The iron sulphur (FeS) proteins exist in the
oxidised (Fe3+) or reduced (Fe2+) state.
• One FeS participates in the transfer of
electrons from FMN to coenzyme Q. Other FeS
proteins associated with cytochrome b and
cytochrome c1 participate in the transport of
electrons.
4. Coenzyme Q
• Coenzyme Q is also known as ubiquinone
since it is ubiquitous in living system. lt is a
quinone derivative with a variable isoprenoid
side chain. The mammalian tissues possess a
quinone with 10 isoprenoid units which is
known as coenzyme Q10 (CoQ1o).
Coenzyme Q is a lipophilic electron carrier .lt
can accept electrons from FMNH2 produced
in the ETC by NADH dehydrogenase or
FADH2 produced outside ETC (e.g. succinate
dehydrogenase,acyl CoA dehydrogenase)
5. Cytochromes
• The cytochromes are conjugated proteins
containing heme group. The latter consists of
a porphyrin ring with iron atom.
• The iron of heme in cytochromes is alternately
oxidized (Fe3+) and reduced( Fe2+) which is
essential for the transport of electrons in the
ETC.
Continued…
• They were designated as cytochrome a , b and
c depending on the type of heme present and
the respective absorption spectrum.
Additional cytochromes such as c1, b1, b2, a3
etc. were discovered later.
• The electrons are transported from coenzyme
Q to cytochromes (in the order) b, c1,c,a and
a3.
Inhibitors of Electron
transport chain
The synthesis of ATP (phosphorylation) is
dependent on electron transport. Hence, all
the site-specific inhibi tors of ETC also inhibit
ATP formation
Inhibitors of Electron
transport chain
• 1. NADH and coenzyme Q : Fish polson rotenone,
barbituate drug amytal and antibiotic piercidin A
inhibit this site.
• 2. Between cytochrome b and c1 : Antimycin A -an
antibiotic, British antilewisite (BAL)-an antidote used
against war-gas-are the two important inhibitors of the
site between cytochrome b and c1.
• 3. Inhibitors of cytochrome oxidase : Carbon
monoxide, cyanide, hydrogen sulphide and azide
effectively inhibit cytochrome oxidase.Carbon
monoxide reacts with reduced form of the cytochrome
while cyanide and azide react with oxidized form.

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ETC.pptx

  • 1. • Electron transport chain • Inhibitors of electron transport chain
  • 2. Definition: The electron transport chain is a series of electron transporters embedded in the inner mitochondrial membrane that shuttles electrons from NADH and FADH2 to molecular oxygen
  • 3. The energy-rich carbohydrates, fatty acids, amino acids undergo a series of metabolic reactions and, finally, get oxidised to CO2 and H2O. The reducing equivalents from various metabolic intermediates are transferred to coenzymes NAD* and FAD to produce, respectively, NADH and FADH2.  The latter two reduced coenzymes pass through the electron transport chain (ETC) or respiratory chain and, finally, reduce oxygen to water. The passage of electrons through the ETC is associated with the loss of free energy. A part of this free energy is utilized to generate ATP from ADP and Pi
  • 4. Overview of electron transport chain (A-Substrate; F,-Flavoprotein ; Cyts Cytochromes).
  • 5. Mitochondrial matrix : The interior ground substance forms the matrix of mitochondria.l t is rich in the enzymes responsible for the citric acid cycle, beta- oxidation of fatty acids and oxidation of amino acids. The mitochondrion consists of five distinct parts. These are the outer membrane, the inner membrane, the intermembranes pace,the cristae and the matrix Mitochondrial organisation
  • 7. Structural organisation of respiratory chain • The inner mitochondrial membrane can be disrupted into five distinct respiratory or enzyme complexes, denoted as complex I, Il, III,IV and V . • The complexes l-lV are carriers of Electrons while complex V is responsible for ATP synthesis.
  • 8. Continued…. • Besides these enzyme complexes there are certain mobile electron carriers in the respiratory chain. These include NADH, coenzyme Q, cytochrome C and oxygen
  • 9. Multiprotein complexes in electron transport chain
  • 10. Components and reactions of electron transport chain • There are five distinct carriers that participate in the electron transport chain (ETC). • These carriers are sequentially arranged and are responsible for the transfer of electrons from a given substrate to ultimately combine with proton and oxygen to form water.
  • 11. 1. Nicotinamide nucleotides • Of the two coenzymes NAD+ and NADP+ derived from the vitamin niacin, NAD+ is more actively involved in the ETC. NAD+ is reduced to NADH + H+ by dehydrogenases with the removal of two hydrogen atoms from the substrate (AH2). • The substrates include glyceraldehyde-3phosphate, pyruvate,i socitrate, alpha-ketoglutarate and malate. AH2 + NAD+ A+ NADH + H+
  • 12. 2. Flavoproteins • The enzyme NADH dehydrogenase (NADHcoenzyme Q reductase) is a flavoprotein with FMN as the prosthetic group. The coenzyme FMN accepts two electrons and a proton to form FMNH2. NADH dehydrogenase is a complex enzyme closely associated with non-heme iron proteins (NHl) or iron-sulfur proteins (FeS). NADH + H + FMN NAD + FMNH2
  • 13. 3. Iron-sulfur proteins • The iron sulphur (FeS) proteins exist in the oxidised (Fe3+) or reduced (Fe2+) state. • One FeS participates in the transfer of electrons from FMN to coenzyme Q. Other FeS proteins associated with cytochrome b and cytochrome c1 participate in the transport of electrons.
  • 14. 4. Coenzyme Q • Coenzyme Q is also known as ubiquinone since it is ubiquitous in living system. lt is a quinone derivative with a variable isoprenoid side chain. The mammalian tissues possess a quinone with 10 isoprenoid units which is known as coenzyme Q10 (CoQ1o).
  • 15. Coenzyme Q is a lipophilic electron carrier .lt can accept electrons from FMNH2 produced in the ETC by NADH dehydrogenase or FADH2 produced outside ETC (e.g. succinate dehydrogenase,acyl CoA dehydrogenase)
  • 16. 5. Cytochromes • The cytochromes are conjugated proteins containing heme group. The latter consists of a porphyrin ring with iron atom. • The iron of heme in cytochromes is alternately oxidized (Fe3+) and reduced( Fe2+) which is essential for the transport of electrons in the ETC.
  • 17. Continued… • They were designated as cytochrome a , b and c depending on the type of heme present and the respective absorption spectrum. Additional cytochromes such as c1, b1, b2, a3 etc. were discovered later. • The electrons are transported from coenzyme Q to cytochromes (in the order) b, c1,c,a and a3.
  • 18. Inhibitors of Electron transport chain The synthesis of ATP (phosphorylation) is dependent on electron transport. Hence, all the site-specific inhibi tors of ETC also inhibit ATP formation
  • 19. Inhibitors of Electron transport chain • 1. NADH and coenzyme Q : Fish polson rotenone, barbituate drug amytal and antibiotic piercidin A inhibit this site. • 2. Between cytochrome b and c1 : Antimycin A -an antibiotic, British antilewisite (BAL)-an antidote used against war-gas-are the two important inhibitors of the site between cytochrome b and c1. • 3. Inhibitors of cytochrome oxidase : Carbon monoxide, cyanide, hydrogen sulphide and azide effectively inhibit cytochrome oxidase.Carbon monoxide reacts with reduced form of the cytochrome while cyanide and azide react with oxidized form.