ELECTRON TRANSPORT CHAIN

PRESENTED BY : GUIDED BY:

NAME: GAYATREE PANI MISS. DEBAYANA PRIYADARSHINI
ROLL NO:20ZOO-004 DEPARTMENT OF ZOOLOGY
UG 3RD YEAR 1
 CONTENTS
 INTRODUCTION
 LOCATION OF ELECTRON TRANSPORT CHAIN
 COMPONENTS/ ELECTRON CARRIERS
 ELECTRON TRANSPORT CHAIN EQUATION
 ELECTRON TRANPORT CHAIN COMPLEXES
• Complex- I
• Complex- II
• Complex- III
• Complex- IV
 IMPORTANCE OF ELECTRON TRANSPORT CHAIN
 CONCLUSION
 REFERENCE
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INTRODUCTION
 Oxidative phosphorylation is the culmination of energy yielding metabolism in aerobic
organism.
 Oxidative: Degradation of carbohydrates, fats & amino acids converge at the final stage of
cellular respiration, in which the energy of oxidation drives the synthesis of ATP.
 Phosphorylation: Mechanism by which photosynthetic organisms capture energy of
sunlight.
 It is the final stage of aerobic oxidation of bio molecules in eukaryotes occurs in the
mitochondria.
 Oxidative phosphorylation involves the reduction of O2 to H2O with electrons donated by
NADH & FADH2.
• Aerobic oxidation of pyruvate by the citric acid cycle.
• Oxidation of fatty acids & amino acids
 Electron transport chain is the process by which NADH & FADH 2 are oxidized & a proton
gradient is formed.
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LOCATION OF ELECTRON TRANSPORT CHAIN
 Electron transport chain in eukaryotes takes place in the inner
mitochondrial membrane.
 Mitochondrion is a double membraned organelle consists of
an outer membrane & an inner membrane.
 There are two compartments in the mitochondria:
• Matrix
• Inter membrane space
 The outer membrane is highly permeable to ions contain
enzyme for citric acid cycle.
 Inner membrane is impermeable to various ions & contains
un-charged molecules, ETC & ATP synthesizing enzymes.

Fig-1 Biochemical anatomy of a Mitochondrion

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COMPONENTS/ ELECTRON CARRIERS
 ETC contains a series of electron carriers – Flavins, Iron Sulphur
Centers, Quinones & Heme in a specific sequence through which
electrons are transferred from substrate to oxygen.
• FMN: (Flavin Mononucleotide)- At the beginning of ETC, the
electrons from NADH are transferred FMN reducing it to FMNH 2.
NAD + H+ + FMN NAD + FMNH2
• Ubiquinon: (Coenzyme Q)- It is membrane soluble low
molecular weight compound.
• Q is a lipid soluble molecule that diffuses within the lipid bi-
layer, & shuttle electrons from complex – I & II & pass them to
complex- III.
• Ubiquinon can accept one electron to become the semi-quinon
.
radical ( QH) or two electrons to form ubiquinol (QH2).
FMNH2 + Q FMN + QH2 Fig-2: Reduction of Ubiquinon (Coenzyme Q)

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COMPONENTS/ ELECTRON CARRIERS
 Cytochromes: These are proteins with characteristics strong absorption of visible light
due to their iron containing heme prosthetic groups.
 Mitochondria contain three classes of cytochromes, designated a,b & c.
 Transfers electrons from complex three to four
 Fe-S clusters: Iron-sulfur proteins (non-heme iron proteins) play a critical role in a wide
range of reduction reactions in biological system.
 Iron ions in these Fe-S complexes cycle between:
• FE2+ (Reduced state)
• FE3+ (Oxidized state)
 Unlike quinones and flavins, iron-sulfur clusters generally undergo oxidation reduction
reactions without releasing or binding protons.

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ELECTRON TRANSPORT CHAIN EQUATION
 The electron transport chain consists of a series of oxidation-
reduction reactions that lead to the release of energy.
NADH + ½ O2 + H+ + ADP+ Pi NAD+ + ATP + H2O

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Fig-3 Electron transport chain complexes
ELECTRON TRANPORT CHAIN COMPLEXES
 Complex – I (NADH: Ubiquinon oxidoreductase / NADH dehydrogenase)
• Transports electrons from NADH to Ubiquinon
• It is a large enzyme composed of 42 polypeptide chains including a FMN
containing flavoprotein & at least 6 iron-Sulfur (Fe-S) clusters.
• NADH molecule binds at the complex release 2e - electrons & oxidized to NAD+.
• Electrons from NADH pass through a flavoprotein with the co-factor FMN &
reduces it to FMNH2.
• Then electrons pass through the Fe-S clusters & finally transfer to the Ubiquinon
& reduce it.
• A protein gradient generated, as a result 2H + move from matrix to Ubiquinon & it
fully reduced to form Ubiquinol.
NADH + H + Q
+
NAD + QH2
+

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ELECTRON TRANPORT CHAIN COMPLEXES (Cont.)
 Complex – I (NADH: Ubiquinon oxidoreductase / NADH dehydrogenase)
• The endergonoic transfer of 4 protons from the matrix to inter membrane space
occurs.
• The matrix becomes negatively charged with the departure of protons &
indicated as negative (N) side.
• The intermembrane space become positively charged by receiving protons,
indicated as positive (P) side.
• The net reaction is NADH + 5HN+ + Q NAD+ + QH2 + 4HP+

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ELECTRON TRANPORT CHAIN COMPLEXES (Cont.)
 Complex – I (NADH: Ubiquinon oxidoreductase / NADH dehydrogenase)

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Fig-4 NADH Ubiquinon oxidoreductase Complex - I
ELECTRON TRANPORT CHAIN COMPLEXES (Cont.)
 Complex – II (Succinate dehydrogenase)
• Transfer electrons from Succinate to Ubiquinon.
• Small simple complex contains 5 prosthetic group & 4 sub units (A,B,C & D)
• A Succinate binding side & a FAD binding side is present in subunit A.
• 3 Fe-S clusters in subunit B.
• They contain a heme group, heme b & a binding site for Ubiquinon.
• Succinate binds at the complex release electron & oxidises to fumarate.
• Electron release in the process take up by FAD & it reduces to form FADH 2.
• After that FADH2 donates electrons to Fe-S clusters.
• Finally electron moves to the Ubiquinon & it partially reduced to form
semiquinon.
• Water molecule binds at the active site donates 2H + to semiquinon & it fully
reduced to Ubiquinol.
• It does not pump any protons across the membrane.
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ELECTRON TRANPORT CHAIN COMPLEXES (Cont.)
 Complex – II (Succinate dehydrogenase)

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Fig-5 Succinate dehydrogenase Complex - II
ELECTRON TRANPORT CHAIN COMPLEXES (Cont.)
 Complex – III (Cytochrome bc1 Complex/ Ubiquinon: Cytochrome c oxidoreductase)
• Ubiquinol transferred the electron S to cytc present in complex-III which it collects
from complex-I & II.
• Q cycle- Ubiquinol oxidises & cyt C reduced.
• The complex is a dimer of identical monomers. The function core of each monomers
are three sub-units.
I. Cytochrome b (Green) with its two hemes (bH & bL)
II. Rieske iron-sulfur protein with 2Fe-2S centre
III. Cytochrome CI with its heme.

• After entering Complex – III QH2 donates one e- to heme bL , Then the e- transfer to
heme bH & finally to Ubiquinone & reduce partially to form aradical.
Q + e- Q- (Semi ubiquinone)

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ELECTRON TRANPORT CHAIN COMPLEXES (Cont.)
 Complex – III (Cytochrome bc1 Complex/ Ubiquinon: Cytochrome c oxidoreductase)
• Other one electron transfer to 2Fe-2S centre, then the e transmits to heme cI present
-

in cyctc & reduces it.

• The 2 protons (2H+) present in ubiquinol transfers to 2nd molecule of cutic & reduces
it.
• In 2 nd
step ubiquinol e -
to heme bL & then to heme bH .
.
• e transforms from heme bH to semi-ubiquinone e(Q ).
-

.
• 2H moves from matrix to Q and reduces fully to form ubiquinol. OH2 moves from
+

Complex-III to IV.
• 2nd electron got to 2Fe-2S centre & then to the heme C I of cytc. It donate e- to 2nd
molecule of cytc & it reduced.
• 2 H+ molecule present in-ubiquinol transfers to inter membrane space.

QH2 +2Cy + CI (Oxidized) + 2HN Q + 2cy + CI (Reduced) + 4HP+

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ELECTRON TRANPORT CHAIN COMPLEXES (Cont.)
 Complex – III (Cytochrome bc1 Complex/ Ubiquinon: Cytochrome c oxidoreductase)

Fig-6 Cytochrome bc1 Complex - III

ELECTRON TRANPORT CHAIN COMPLEXES (Cont.)
 Complex – III (Cytochrome bc1 Complex/ Ubiquinon: Cytochrome c oxidoreductase)

Fig-7 the Q cycle path of electrons through complex - III

ELECTRON TRANPORT CHAIN COMPLEXES (Cont.)
 Complex – IV (Cytochrome C to O2 / Cytochrome oxidose)
• This carries e from cytochrome C to molecular oxygen, reducing it to H 2O.
-

• This have enzymes having 13 subunits.

• Subunits 2 has cytochrome C binding site. Bi-Nuclear centre (Cu A) is also present.
• Subunit- I has two heme group hemea , heme a3 & cupper ion (CuB) is also present.
• Heme a3 & CuB together make a second bi-nuclear centre (Fe-Cu) centre.
• The third Subunit-III has no co-factors but may provide a channel through which
oxygen diffuses to active sites.
• 4 cytc complexes bind at subunit-II
• Cyctc donate 4e s to the binuclear centre CuA .
-

• From here electrons pass through hemea to the Fe-Cu centre (heme a3 & CuB)

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ELECTRON TRANPORT CHAIN COMPLEXES (Cont.)
 Complex – IV (Cytochrome C to O2 / Cytochrome oxidose)
• O2 enters to complex IV through SU-3 & binds to heme a 3.
• O2 is reduced to its peroxy deritive (O22-) by 2 electrons from the Fe-Cu centre.
• Delivery of 2 more electrons from cytc converts O22- to two molecule of water, with
consumption of four substrate protons (4H+) from matrix.
• At the same time four protons (4H+) are pumped from +e matrix to inter membrane
space.

4C + C (Reduced) + 8HN + O2
+
4Cu + C (Oxidized) + 4HP + 2H2O
+

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ELECTRON TRANPORT CHAIN COMPLEXES (Cont.)
 Complex – IV (Cytochrome C to O2 / Cytochrome oxidose)

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Fig-8 Path of electrons through complex - IV
IMPORTANCE OF ELECTRON TRANSPORT CHAIN
 The end products of the electron transport chain are 30-32 ATPS & 44 moles of H 2O.
 The synthesized ATP molecules are subsequently used in other energy consuming
activities such as the bio synthesis of complex macromolecules.
 Excess, deficient & absence of ETC function can cause mitochondrial stress and
dysfunction.
 Examples of consequences of disturbed ETC activities are- Depleted cellular ATP,
Inhibition of complex- I activity & mutation in genes.

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CONCLUSION
 ETC is a group of protein complexes that facilitates transfer of electrons which is
essential for ATP.
 Malfunctioning ETC can result in deleted energy levels & function of radicals.
 This is useful & applicable in agricultural practices & drug design.

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REFERENCE
 Nelson,D.L., Cox,M.M., (2005).Lehninger Principle of Biochemistry, W.H.Freeman and
Company, Fourth edition, 690-702.
 Jain, J.L., Jain, S., Jain,N., (2005). Fundamentals of Biochemistry, S.Chand and Company
Ltd., Sixth edition, 522-541.
 Berg,J.M., Tymoczko,J.L., Stryer, L., (2012). Biochemistry, W.H.Freeman and Company,
Fifth edition, 734-750.

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