Chala kenenisa(electron transport chain)

CELL BIOLOGY SEMINAR PRESENTATION on ELECTRON TRANSPORT CHAIN COMPLEXES

INSTRUCTOR:- Dr. SOLOMON GENET

ADDIS ABABA UNIVERSITYCOLLEGE OF HEALTH SCIENCES

DEPARTMENT OF MEDICAL BIOCHEMISTRY

BY:- CHALA KENENISA

PRESENTATION OUTLINE Objectives Dev’t in ETC and Mit. Experiments Introduction to ETC and OXPHOS and arrangements of complexes components of Complex I components of Complex II Ubiquinone(COQ) components of Complex III components of Complex IV components of Complex V Other components related with OXPHOS Conclusion References

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CHALA KENENISA;components of ETC complexes, AAU,CHS,Dept MedBiochem, 2016 2

SEMINAR OBJECTIVESThis seminar presentation longs to

◦ Explain trends of devt in ETC and Mit experiments◦ Describe electron transport chain and oxidative phosphorylation◦ Discuss the components and subunits of complexes of ETC

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Dev’t in ETC and Mit. Experiments Mitochondria were discovered in the late 19th century and

were described as a collection of granules forming threads inside the cell (Benda, 1898).

This view was confirmed by electron-microscopic observations of tissue, cultured cells and rat diaphragm muscle that revealed the existence of a mitochondrial network (mt-network), also known as mitochondrial reticulum

The central role of mitochondria in cellular energy production was demonstrated by the discovery of the respiratory chain and by the first investigations of oxidative phosphorylation (OXPHOS) (Chance and Williams, 1956; Mitchell, 1961).

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Dev’t in ETC and Mit. Experiments Most bioenergetic studies were performed on isolated

mitochondria from rat liver or muscle that do not maintain network continuity after fractionation procedures.

By contrast, it has become clear that the mitochondrion exists in living human cells as a large tubular assembly, extending throughout the cytosol and in close contact with the nucleus, the endoplasmic reticulum the Golgi network and the cytoskeleton

Historically, bovine heart mitochondria have been the system of choice for the structural characterization of eukaryotic OXPHOS complexes, because they can be purified in relatively large quantities.

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Experiments…continued The yeast Saccharomyces cerevisiae, which is amenable to a

large variety of molecular genetic tools, has become the model organism to study the biogenesis of mitochondrial complexes and the effect of mutations on OXPHOS components.

By contrast, mitochondria of photosynthetic organisms have been poorly characterized.

Characterization of Arabidopsis mitochondrial components through proteomic approaches has advanced significantly

Subcellular fractionation, fluorescence microscopy, western blotting, spectrophotometric assays, centrifugation are some of methods being used to study mitochondria.

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Introduction to ETC and OXPHOS Energy requirements of aerobic cells are met by oxidation of

carbohydrates, lipids, and proteins, which yields reduced coenzymes NADH and FADH2

The oxidation of NADH and FADH2 proceeds in a highly organized electron transport chain (ETC) mitochondrial system, which consists of complexes of proteins and coenzymes.

The ultimate electron acceptor is oxygen, which is converted to water.

The energy is conserved with the transport of electrons in the ETC as an electrochemical proton gradient, because protons (H+) are pumped out of the matrix to the intermembranal space.

The electrochemical proton gradient drives the conversion of ADP to ATP, when protons are channeled back into the matrix via ATP synthase.

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Introduction…continuedMitochondria play a number of vital roles in the

eukaryotic cell, among which the most important one is the production of ATP during oxidative phosphorylation (OXPHOS).

The heavily folded inner membranes of mitochondria called cristae accommodate many copies of the respiratory chain components, or OXPHOS complexes (I–IV). Together with ATP synthase (complex V) they form the machinery for production of ATP, the energy currency of the cell.

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Introduction…continuedComplexes I–IV are multisubunit enzymes that

work in concert to create an electrochemical proton gradient across the mitochondrial inner membrane that is used by the F1Fo ATP synthase (complex V) to produce ATP via oxidative phosphorylation, although complex II is not directly able to pump protons

NADH or succinate, generated during glycolysis, fatty acid oxidation and in the citric acid cycle, form the fuel for the respiratory chain.

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Introduction…continued During catalysis, there is electron transfer between the

complexes mediated by two small components: lipid-soluble ubiquinone and water-soluble cytochrome c.

They diffuse between the respiratory complexes I and II, and III and IV, respectively, and the latter takes them to form water from molecular oxygen.

The oxidoreduction reactions mediated by complexes I, III, and IV are coupled with protons transfer from the matrix to the intermembrane space. The energy associated with the proton gradient is used for the production of ATP by complex V (ATP synthase) or dissipated by uncoupling proteins (UCP).

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Introduction…continued Electron transport chain and oxidative phosphorylation

(OXPHOS) systems are organized into five complexes: I, II, III, IV, and V.

Each complex consists of unique species of molecules that include flavoproteins with tightly bound FAD or FMN, coenzyme Q, cytochromes, iron–sulfur (Fe-S) proteins, and copper-bound proteins.

The five complexes are coupled and function in a dynamic manner.

The direction of electron flow in the ETC is from a higher to a lower energy level.

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Fig 1. components of ETC05/03/2023


http://www.sciencedirect.com/science/article/pii/B9780123708731000216?np=y#gr1

Arrangements of ETC complexes Two different models have been proposed. The random collision model (Hackenbrock et al, 1986)

states that each complex exists as individual entities that diffuse freely in the lipid bilayer.

In this model, transfer of electrons occurs during random and transient collision events.

By contrast, the solid-state model (Chance and Williams, 1955) assumes a higher level of organization, such that the electron transport complexes assemble into supercomplexes, where efficient transfer of electrons occurs along predefined pathways.

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Arrangements…continuedThe solid-state model gained support from the

discovery of supercomplexes in bovine heart and yeast mitochondria by blue-native polyacrylamide gel electrophoresis (BN-PAGE) (Schägger and Pfeiffer, 2000).

A first 3D map of negatively stained supercomplex B from bovine heart, composed of complex I, dimeric complex III and complex IV, provided initial insights into the arrangement of the three complexes in the assembly (Schäfer et al, 2007

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Complex I Complex I is a flavoprotein and an NADH

dehydrogenase. It transfers electrons from NADH to hydrophobic mobile electron carrier CoQ via FMN and iron–sulfur clusters, leading to the formation of CoQH2. The passage of electrons by complex I is coupled to the transport of protons from the matrix to the intermembrane space of mitochondria. Complex I is inhibited by rotenone and Amytal.

It binds NADH substrate to the distal end of the hydrophilic arm and transfers two electrons, one at a time, via FMN and seven iron–sulphur clusters to the bound ubiquinone at the interface between two arms.

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Complex I…continuedIt is the largest enzyme of the electron transport

chain (ETC) and has a characteristic L shape with an extensive part being embedded in the lipid bilayer and a smaller shoulder protruding into the mitochondrial matrix.

Complex I from several organisms has been characterized, including beef heart (45 subunits), Arabidopsis and rice (42 subunits, and the fungi Neurospora crassa (39 subunits) and Yarrowia lipolytica (37 subunits).

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Complex I…continued Five to nine Complex I subunits (the ND subunits) are

usually encoded in the mitochondrial genome, whereas the remaining subunits are nuclear gene products

Including the 14 highly conserved subunits homologous to the prokaryotic type-I NADH dehydrogenase enzyme, all eukaryotic enzymes contain at least 33 subunits in common

Only three chaperones involved in Complex I assembly have been identified to date, CIA30 and CIA84 of N. crassa, and a paralogue (B17.2L) of the bovine B17.2 structural subunit

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Table 1. Components of complex IChlamydomonas

Counterparts in other organisms

Gene Protein

product Accession #

Homo sapiens/Bos taurus

Neurospora/Yarrowia

Arabidopsis

Constituents (Subunits) NUO10 Subunit 10 EDO9802

9 NDUFS7/PSST 19.3/NUKM NP_19673

8 NUO8 Subunit 8 EDO9698

8 NDUFS8/TYKY 21.3c/NUIM NP_17311

4 NP_178022

NUO5 24-kD subunit

EDP08001

NDUFV2/24 24/NUHM NP_567244

NUO9 ND9 subunit EDP05911

NDUFS3/30 31/NUGM Q95748

NUO7 49-kD ND7 subunit

EDP00001

NDUFS2/49 49/NUCM P93306

NUO6 51-kD subunit

EDP06369

NDUFV1/51 51/NUBM NP_196470

NUOS1 76-kD subunit

EDP03454

NDUFS1/75 78/NUAM NP_851103 NP_568550

nd1 Subunit 1 AAB93446

ND1 ND1/NU1M NP_085565



ND3 ND3 subunit EDP02792

ND3 ND3/NU3M P92533



ND4L ND4L subunit

EDP00050

ND4L ND4L/NULM NP_085525





NUOA1 8-kD subunit

EDP07892

NDUFA1/MWFE 9.8/NIMM NP_566330

ACP1 Acyl-carrier protein

EDO98915

NDUFAB1/SDAP

9.6/ACPM NP_176708

NUOB8 11-kD subunit

EDP01212

NDUFA2/B8 10.5/NI8M NP_199600

NUOB12

7-kD subunit

EDP07174

NDUFB3/B12 10.6/NB2M NP_178355

NUOB13

18-kD subunit

EDP08707

NDUFA5/B13 29.9/NUFM NP_568778

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Complex II Complex II, also known as succinate

dehydrogenase, is a member of the TCA cycle. It is the second independent entrance point of

electrons to the respiratory chain. It is not a proton pump and it does not contribute

directly to the proton gradient formation. It oxidizes succinate to fumarate, which is

coupled to the reduction of FAD to FADH2. The electrons from FADH2 are transferred to CoQ via Fe-S centers with the formation of CoQH2.

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Complex II…continuedIt comprises four distinct nucleus-

encoded polypeptides, SDH1 (the flavoprotein subunit), SDH2 (the iron-sulfur subunit), and two hydrophobic membrane anchors, SDH3 (subunit III) and SDH4 (subunit IV)

A single Complex II chaperone, TCM62, has been identified in yeast mitochondria

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Table 2. components of complex II

Chlamydomonas Counterparts in other organisms

Gene Protein product Accession #

Homo sapiens/Bos taurus Yeast Arabidopsis

SDH1 Subunit A EDP09580 SDHA SDH1 NP_179435NP_201477

SDH2 Iron-sulfur subunit

EDP08267 SDHB SDH2 NP_198881NP_189374

SDH3 Subunit b560, alternative splicing variant 1

EDP09244 SDHC (QPS1) SDH3 NP_196522

SDH3 Subunit b560, alternative splicing variant 2

EDP09245 SDHC (QPS1) SDH3 NP_196522

SDH4 Subunit D EDP09690 SDHD SDH4 NP_566077

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Ubiquinone (COQ) CoQ accepts electrons not only from both complex I and II

but also from other flavoprotein-linked dehydrogenases, namely fatty acyl-CoA dehydrogenase and glycerophosphate dehydrogenase.

Ubiquinone is a lipid composed of a redox-active benzoquinone ring connected to a long isoprenoid side chain (usually 6–10 units).

CoQ plays a central role in the mitochondrial respiratory chain since it shuttles electrons from Complex I, Complex II, and type-II NAD(P)H dehydrogenases to Complex III and AOX.

In addition, the redox state of CoQ regulates the activity of UCPs in land plants, mammals, and protists

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Complex III Complex III catalyzes the electron transport from CoQH2

to cytochrome c and also is the second site of proton transport from matrix to intermembrane space.

Complex III or cytochrome c oxidoreductase, which is known to exist in the membrane as a dimer, oxidises ubiquinone to ubiquinol and as a result it can pump two protons to the intermembrane space. The electrons from ubiquinol are passed to the carrier cytochrome c via cytochromes b and c1 of complex III

It consists of three different cytochromes and an Fe-S protein. Cytochromes contain the same iron–protoporphyrin IX heme prosthetic groups found in hemoglobin and myoglobin.

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Complex III…continued Unlike hemoglobin and myoglobin, the iron atoms of

the heme groups of cytochromes undergo oxidation and reduction cycles facilitating electron transport.

The terminal electron acceptor of electrons from CoQH2 is cytochrome c. It is a mobile electron carrier like CoQ, but is water soluble, loosely bound to the inner mitochondrial membrane.

Complex III is composed of ten well-conserved subunits, the oligomeric membrane protein complex contains three subunits carrying redox groups: cytochromeb, cytochrome c1, and a Rieske iron-sulfur protein (ISP).

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Complex III…continued The bc1 complex from Chlamydomonas was isolated

and resolved into nine subunits with molecular masses ranging from 10 kD to 50 kD and four of these polypeptides were identified: QCR1 or core I (53 kD), whose N-terminal sequence was obtained; cytochrome b, cytochrome c1, and the ISP.

Six other Complex III components were identified by searching the genome: QCR2 (core II), QCR7 (subunit VI), QCR8 (subunit VII or “ubiquinol-binding” protein), QCR6 (subunit VIII or “hinge protein”), QCR9 (subunit X), and QCR10 (subunit XI)

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Chlamydomonas


Gene Protein

product Accession #

Homo sapiens/Bos taurus

Yeast Arabidopsis

Constituents (Subunits) QCR1 50-kD core

1 subunit Peptidase beta subunit (beta-MPP)

EDP00713

UQCRC1/Core1 COR1/beta-MPP

NP_186858

QCR2 core 2 subunit

UQCRC2/Core2 QCR2 NP_566548 NP_175610

MPPA1MPPA2

Peptidase alpha subunit

EDP00385 EDP05489

cob Cytochrome b

AAB93440

CYB/III COB P42792

CYC1 Cytochrome c1

EDO96204

CYC1/IV CYT1 NP_189360 NP_198897

RIP1 Rieske iron-sulfur protein

EDP09520

UQCRCFS1/RISP,IX

RIP1 NP_196848 NP_568288

QCR7 14-kD subunit

EDP08285

UQCRB/VI, 14 kD QCR7 NP_849484 NP_194973

QCR8 9-kD subunit

EDP00113

UQCRQ/VII QCR8 NP_187697 NP_196156

QCR6 8-kD subunit

EDO99747

UQCRH/VIII QCR6 NP_178219 NP_172964

QCR9 7-kD subunit

EDO98612

UQCR10/X QCR9 NP_190841

QCR10 10-kD subunit

EDP00790

6.4 kD/XI QCR10 NP_565941

Assembly factors CBP3 Chaperone EDP0952

2 CBP3 CBP3 NP_19993

5 BCS1 Biogenesis

factor EDO97908

BCS1 BCS1 NP_850841

Table 3. components of complex III

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Complex IV is cytochrome c oxidase, and it is the final destination for the

electrons. It catalyzes the reduction of O2 by using electrons obtained

from reduced cytochrome c, with the formation of the end product, water; and it is the third proton pumping station.

It consists of four redox centers: cytochrome a, cytochrome a3, and two Cu ions.

Inhibitors of cytochrome c oxidase are carbon monoxide, azide, and cyanide.

It accepts electrons from cytochrome c and delivers them to an oxygen molecule to convert it to two water molecules. Four protons are pumped to the intermembrane space during this process.

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Complex IV…continued In yeast and mammals, the complex is composed of 12

and 13 subunits, respectively. In Arabidopsis, the enzyme is composed of 10–12 subunits but only 7 have been identified

Three subunits, usually encoded in the mitochondrial genome, comprise the catalytic core: COX1, which binds heme a, heme a3, and CuB; COX2, which binds CuA; and COX3.

The other subunits, all of which are nucleus-encoded, are considered to be regulatory proteins or polypeptides that participate in biogenesis of the complex.

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Table 4. components of complex IVChlamydomonas


Gene Protein product Accession #

Homo sapiens/Bos taurus Yeast Arabidopsis

Constituents (Subunits) COX1 Subunit 1 AAB93443 COI COI P60620 COX2a Subunit II,

protein IIa of split subunit

EDP00208 COII COII P93285

COX2b Subunit II, protein IIb of split subunit

EDP09974 COII COII P93285

COX3 Subunit 3 EDP04132 COIII COIII P92514 COX5b Subunit 4, 13 kD EDP08953 COX5B IV (COX4) NP_188185

NP_178140 COX5c 11-kD subunit EDP00106 N.I. N.I. NP_850738

NP_182260 COX13 12-kD subunit EDP03436 COX6A COXVIa

(COX13) NP_195496

COX12 COX subunit EDP05132 COX6B COXVIb (COX12)

NP_173661 NP_194535

COX90 COX subunit EDO98724 N.I. N.I. N.I. Assembly factors

SHY1 COX assembly protein

EDO97446 Surfeit1 SHY1 NP_566592

SCO1 COX assembly factor

EDO97370 SCO1, SCO2 SCO1, SCO2 NP_566339

COX10 COX assembly protein

EDO96513 COX10 COX10 NP_566019


EDO98350 COX11 COX11 NP_171743

COX15 COX assembly factor

EDP06678 COX15 COX15 NP_200420


EDP06214 AAH01702 COX16 NP_680684


EDO97130 COX17 COX17 NP_175711


EDO98825 OXA1 COX18, OXA1 (PET1402)

NP_201011


EDP08032 COX19 COX19 NP_849852


EDO98664 NP_077276 COX23 NP_171718

PET191 COX assembly protein

EDO98359 AAH47722 PET191 BAC43353

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Complex V The energy conserved by the electron transport chain

as an electrochemical proton gradient between the inner-membranal space and matrix is utilized in the formation of ATP from ADP. This process is known as Mitchell’s Chemiosmotic hypothesis and is catalyzed by ATP synthase, also known as complex V.

It consists of spheres known as F1 and that are attached to an integral membrane protein, F0.

The water-soluble F1-part consists of three α and three β catalytic subunits. The F1-part is connected to the membrane-embedded ring-like subunit c oligomer of the Fo-part by a central and a peripheral stalk.

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Complex V…continued The Fo-part is composed of subunits a (Su 6), A6L (Su

8), e, f, g, the central stalk consists of the γ, δ and ε subunits and the peripheral stalk is made from subunits OSCP (Su 5), b, d, F6 (h)

The translocation of protons occurs via the transmembrane channel F0.

ATP synthesis occurs on F1 subunits, which function as a rotating motor coupled to the formation of an anhydride bond between ADP and Pi.

Transport of two electrons from NADH yields three ATP (P/O=3) and transport of two electrons from FADH2 yields two ATP (P/O=2).

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Complex V…continued F0F1-ATP synthase is considered a molecular motor in

which a central rotor-stalk [γ/δ/ε/c10] (subunits of beef mitochondria) rotates around an axis perpendicular to the plane of the membrane, while other polypeptides constitute the fixed elements of the motor: subunit a, the catalytic core [α3/β3], the peripheral stator-stalk [OSCP/b/d/F6 ], and the so-called minor subunits [A6L/e/f/g]

Proton flux across subunit a causes a rotary movement of the membrane-embedded ring c10 and its bound, protruding central rotor-stalk. In a full cycle, three sequential 120° movements of subunit γ induce consecutive conformational changes in the three catalytic β subunits leading to substrate binding (ADP+Pi), ATP synthesis, and ATP release

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Complex V…continuedAdditional subunits play regulatory roles, such as

the inhibitory protein IF1 or are involved in the formation and stabilization of a dimeric complex, such as subunits e

The eukaryotic Complex V contains components similar to those found in bacteria, but possesses additional subunits.

In mammals, ATPase includes 16 subunits whereas the yeast enzyme comprises 20 components, 13 being essential for the structure of the complex

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Fig 2. structure of ATP synthase

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Table 5. components of complex VChlamydomonas Counterparts in other organismsGene Protein product Accession # Homo sapiens/Bos

taurusYeast Arabidopsis

Constituents (Subunits)ATP6 Subunit 6 EDP09230 ATP6/a ATPA /ATP6 P93298,P92547ATP9A Subunit 9, isoform A EDO97408 ATP5G3/c ATPC /ATP9 P60112,NP_178769ATP9B Subunit 9, isoform B EDO97377 ATP5G3/c ATPC(ATP9 P60112,NP_178769ATP1 Alpha subunit EDP07337 ATP5A1/α α (ATP1) P92549,NP_178788ATP1B Alp subunit isoform B EDP06403 ATP5A1/α α (ATP1) P92549,NP_17878ATP2 Beta subunit EDP04740 ATP5B/β β (ATP2) NP_568203,NP_680155,NP_568204ATP3 Gamma subunit EDO97956 ATP5C1/γ γ (ATP3) NP_180863ATP16 Delta subunit EDO99236 ATP5D/Δ Δ (ATP16) NP_199514ATP15 Epsilon subunit EDP06388 ATP5E/ε ε (ATP15) NP_175576ATP5 Subunit 5, OSCP

subunitEDP01322 ATP5O/

OSCPATP5 NP_196849

ASA1 Associated 60.6-kD EDP03873 N.I. N.I. N.I.ASA2 Associated 45.5-kD EDP00850 N.I. N.I. N.I.ASA3 Associated 36.3-kD EDO98373 N.I. N.I. N.I.ASA4 Associated 31.2-kD EDP08830 N.I. N.I. N.I.ASA5 Associated 14.3-kD EDP00370 N.I. N.I. N.I.ASA6 Associated 13.3-kD EDP06853 N.I. N.I. N.I.ASA7 Associated 19.5-kD EDP00858 N.I. N.I. N.I.ASA8 Associated 10.0-kD EDP01930 N.I. N.I. N.I.ASA9 Associated 12.0-kD EDP02597 N.I. N.I. N.I.

Assembly factorsATP11 Assembly factor 1 for

F1 componentEDP05655 ATPAF1 ATP11 NP_565778

ATP12a Assembly factor 2, splice variant a

EDP00509 ATPAF2 ATP12 NP_198882

ATP12b Assembly factor 2, splice variant b

EDP00510 ATPAF2 ATP12 NP_19888205/03/2023


Other components related to OXPHOS

1. Alternative NAD(P)H dehydrogenases

◦ In addition to the proton-pumping Complex I, plant and fungal mitochondria contain several type II NAD(P)H dehydrogenases. These enzymes, located at the surface of the mitochondrial inner membrane and facing either the intermembrane space or the matrix, allow electron transfer from NAD(P)H to ubiquinone. They are single, low molecular weight polypeptides whose activity is insensitive to rotenone

2. Alternative oxidases◦ Besides the classical terminal aa3-type oxidase, mitochondria from

plants, several fungi, and several protists also possess an alternative oxidase (AOX) that drives the electrons from the ubiquinol pool directly to molecular oxygen and does not contribute to the formation of an electrochemical gradient. The enzyme is thought to regulate mitochondrial respiratory electron flow and to protect plant cells from oxidative damage

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Other components…continued 3. Uncoupling proteins Uncoupling proteins (UCPs) belong to the mitochondrial anion

carrier protein family. UCPs are anchored in the inner membrane and compete with the F0F1-ATP synthase for the proton electron gradient built up by the activity of respiratory-chain Complexes I, III, and IV. They are present in all eukaryotes investigated except yeast, and their physiological roles are still under investigation and debate. A consensus function for UCPs might be the maintenance of energy balance during phosphorylating conditions, indirectly protecting the mitochondrion against reactive oxygen species by diminishing the reduced state of the respiratory chain

To date, three UCP-encoding genes have been identified in Chlamydomonas: UCP1, UCP2, and UCP3

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Other components…continued 4.pyruvate formate-lyase (PFL) (Kreuzberg, 1984), the enzyme that cleaves pyruvate into acetyl-CoA and formate. PFL is widespread in bacteria but rarely found in eukaryotes. The genes encoding PFL, phosphotransacetylase, and acetate kinase are present in Chlamydomonas and biochemical evidence exists for the presence of the corresponding protein products in mitochondria. Thus, an alternative route of mitochondrial ATP synthesis is present in Chlamydomonas involving pyruvate, acetyl-CoA, acetyl-phosphate, and acetate as end product.

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CONCLUSIONStudies of mitochondria and ETC advanced

since 19th century, still spaces.ETC is the main system for ATP productionComplexes in ETC has distinct roles and

are multi enzyme complexes with different numerous sub units of which complex I is the largest

There are also several proteins related to oxidative phosphorylation.

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References Daniel Dikova et al, Inner membrane dynamics in mitochondria; Journal of

Structural Biology, Volume 183, Issue 3, September 2013, Pages 455–466 Giovanni Benar et al, Mitochondrial bioenergetics and structural network

organization, Journal of Cell Science 120, 838-848 Published by The Company of Biologists 2007

M.K Bhugman,Chung.F;Essentials of Medical Biochemistry With Clinical Cases, (Second Edition); Chapter 13 – Electron Transport Chain, Oxidative Phosphorylation, and Other Oxygen-Consuming Systems,2015, Pages 187–204

Pierre Cardol et al, Chapter 13 – Oxidative Phosphorylation: Building Blocks and Related Components, Sceince direct, Elseiver B.V,

Yuriy Chaban et al, Review Structures of mitochondrial oxidative phosphorylation supercomplexes and mechanisms for their stabilisation , Institute of Structural and Molecular Biology, Malet street, Birkbeck College, London WC1E 7HX, UK b Electron Microscopy Group, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Netherlands, October 2013

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THANK YOU !!

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