1) Introductione (2) History (3) Structure (4) list of mitochondrial enzymas a) enzymes of outer membrane b) enzymes of outer chamber c) enzymes of inner membrane d)enzymes of inner chambes (5)Mitochondrial enzymes 1 Subtypes and tissue distribution 2 Function 3 Substrate specificities 4 Clinical significance 5 Genetics (6) Enzymes of CAC (7) Enzymes of oxidative phosphorilation (8) Electron carrior and complex. (9) Respiratory chain inhibitors. (10) Conclution (11) refrences

1. By
KAUSHAL KUMAR SAHU
Assistant Professor (Ad Hoc)
Department of Biotechnology
Govt. Digvijay Autonomous P. G. College
Raj-Nandgaon ( C. G. )

2. Contents :-
(1) Introductione
(2) History
(3) Structure
(4) list of mitochondrial enzymas
a) enzymes of outer membrane
b) enzymes of outer chamber
c) enzymes of inner membrane
d)enzymes of inner chambes
(5)Mitochondrial enzymes
1 Subtypes and tissue distribution
2 Function
3 Substrate specificities
4 Clinical significance
5 Genetics
(6) Enzymes of CAC
(7) Enzymes of oxidative phosphorilation
(8) Electron carrior and complex.
(9) Respiratory chain inhibitors.
(10) Conclution
(11) refrences

3. •introduction ;
1) Mitochondria are sometimes described as "cellular power plants“ because
they generate most of the cell's supply of adenosine triphosphate (ATP), used
as a source of chemical energy .
2) The word mitochondrion comes from the Greek μίτος or mitos, thread +
χονδρίον or chondrion, granule.
3) the mitochondrion has its own independent genome
history;
•Kolliker (1850) first seen mitochondria in street
muscle cells.
•Flemming (1882) named fila .
•Altman (1892) named Bioplast.
•Benda (1898) named mitochondria.
•Nass (1963) Observed DNA in mitochondria.

4. structure;
A mitochondrion contains outer and inner membranes composed of phospholipid bilayers
and proteins.[6]
1.outer membrane:- It contains large numbers of integral proteins
called porins
2.inner membrane space:-, the concentrations of small
molecules such as ions and sugars in the intermembrane space is the
same as the cytosol.
3.inner membrane:-; Cardiolipin contains four fatty acids
rather than two and may help to make the inner membrane impermeable.
4.Cristae:- inner mitochondrial membrane, enhancing its ability to
produce ATP. These folds are studded with small round bodies known as
F1 particles or oxysomes.
5.matrix:-The major functions include oxidation of pyruvate
and fatty acids, and the citric acid cycle.
STRUCTURE OF MITOCHONDRIA

5. Outer membrane enzymes
*monoamine oxidase
*rotenone insensitive NADH cyt-c-reductace
*kynurenine hydroxylase
thiokinase
Outer chamber enzymes
*adenylate kinase
*nucieoside diphosphokinase
•List of mitochondrial enzymes;

6. Inner membrane enzymes
*respiratory chain enzymes
*ATP synthetase orxidase
*succinate dehydrogenase
*carnitine fatty acid acyl transferase
Inner chamber enzymes
*isocitrate dehydrogenase
*fumerase
*aconitase
*citrate snythetase
*alfa-keto acid dehydroge
*beta-oxidation enzymes
*L-malate hydrogenase
*L-amino levuline synthatase
*L-glutamate dehyrogenase

7. {1}enzymesof outer membrane
Monoamine oxidase :- Contents;
1. Subtypes and tissue distribution:-
2. Function:-
3. Substrate specificities
(1) Serotonin, melatonin, norepinephrine, and epinephrine are mainly
broken down by MAO-A.
(2)Phenethylamine and benzylamine are mainly broken down by MAO-B.
(3) Both forms break down dopamine, tyramine, and tryptamine equally.
4.Clinical significance
5. Genetics

8. Nuclieoside diphosphokinase :-
. enzymes of outer chember ;-
enzymes that catalyze the exchange of phosphate groups between different nucleoside
diphosphates.
Function:-
GTP + ADP → GDP + ATP
(1)Prokaryotic systems
(2) Eukaryotic systems:

9. {3}enzymes of inner membrane
{1} carnitine fatty acid acyl transferase :-
Carnitine is a quaternary ammonium compound biosynthesized from the amino acids lysine and
methionine. In living cells, it is required for the transport of fatty acids from the cytosol into the
mitochondria during the breakdown of lipids (fats) for the generation of metabolic energy
•Biochemistry
Biosynthesis -
Role in fatty acid metabolism –
Potential uses as a pharmaceutical
•Heart conditions
• Kidney disease and dialysis
•Effect in male infertility
•As an antidote in valproic acid poisoning
 As a weight loss supplyment

10. {4}enzymes of inner chamber
•Three stages of ceel respiration :-
•Oxidative decarboxylation [pyruvate to acetyl co-A
•CAC/ TCA/ Acetyl co-A catabolism/ kreb’s cycle
•ETC/ ETS/ oxidative phosphorylation.

11. [a]CAC/ KREB’S CYCLE ENZYMES;

12. Substrates Products Enzyme Reaction type Comment
Oxaloacetate +
Acetyl CoA +
H2O
Citrate +
CoA-SH
Citrate synthase
Aldol
condensation
irreversible,
extends the 4C
oxaloacetate to a
6C molecule
Citrate
cis-Aconitate +
H2O
Aconitase
Dehydration
reversible
isomerisation
cis-Aconitate +
H2O
Isocitrate Hydration
Isocitrate +
NAD+
Oxalosuccinate
+
NADH + H +
Isocitrate
dehydrogenase
Oxidation
generates
NADH
(equivalent of
2.5 ATP)
ROLEOF CACENZYEM’S

13. Oxalosuccinate
α-Ketoglutarate +
CO2
Decarboxylation
rate-limiting,
irreversible stage,
generates a 5C
molecule
α-Ketoglutarate +
NAD+ +
CoA-SH
Succinyl-CoA +
NADH + H+ +
CO2
α-Ketoglutarate
dehydrogenase
Oxidative
decarboxylation
irreversible stage,
generates NADH
(equivalent of 2.5
ATP),
regenerates the 4C
chain (CoA
excluded)
Succinyl-CoA +
GDP + Pi
Succinate +
CoA-SH +
GTP
Succinyl-CoA
synthetase
substrate-level
phosphorylation
or ADP→ATP
instead of
GDP→GTP,[7]
generates 1 ATP or
equivalent

14. Succinate +
ubiquinone (Q)
Fumarate +
ubiquinol (QH2)
Succinate
dehydrogenase
Oxidation
uses FAD as a
prosthetic group
(FAD→FADH2 in
the first step of the
reaction) in the
enzyme,[7]
generates the
equivalent of 1.5
ATP
Fumarate +
H2O
L-Malate Fumarase
H2O addition
(hydration)
L-Malate +
NAD+
Oxaloacetate +
NADH + H+
Malate
dehydrogenase
Oxidation
reversible (in fact,
equilibrium favors
malate), generates
NADH
(equivalent of 2.5
ATP)

15. 1)ACONITASE;-
A) Aconitase has an active [Fe4S4]2+ cluster,
which may convert to an inactive
[Fe3S4]+ form.
ISOCITRATE DEHYDROGENASE :-
Isozymes
NADP+ dependent Each NADP+-dependent isozyme functions as a homodimer:
NAD+ dependent The isocitrate dehydrogenase 3 isozyme is a heterotetramer
that is composed of two alpha subunits, one beta subunit, and one gamma subunit.

16. (3) FUMERASE:-
MACHANISMOF FUMARASE
Clinical significance
Fumarase deficiency is characterized by polyhydramnios and fetal brain
abnormalitie. In the newborn period, findings include severe neurologic
abnormalities, poor feeding, failure to thrive, and hypotonia.

17. (4) BETA –OXIDATION ENZYMES :-
1. Activation of fatty acids in the cytosol
2. Transport of fatty acids into mitochondria
(carnitine shuttle)
3. Beta oxidation proper in the mitochondrial
matrix.
(5) L-malate dehydrogenase
BETA OXIDATION CYCLE

19. {2} OXIDATIVE PHOSPHORILASION ENZYMES

20. Photosynthetic electron transport chain of the thylakoid membrane.

21. Electron carriers
(1) FMN –
2) Coenzyme Q

22. 3) Heme –
A prosthetic group of cytochromes.
Heme contains an iron atom embedded in
a porphyrin ring system.
The porphyrin ring structure is planar. The iron
atom of heme is usually bonded to two axial
ligands, in addition to the 4 N of the porphyrin
ring system.

23. 4) Cytochromes –
1) Are proteins with heme prosthetic groups.
.
2) Some cytochromes are part of large integral membrane
complexes, each consisting of several polypeptides and
including multiple electron carriers. . For example, hemes a and
a3 that are part of the respiratory chain complex IV are often
referred to as cytochromes a and a3.
Cytochrome c is instead a small, water-soluble protein, with a single heme group.
5) Iron-sulfur centers (Fe-S
Electron transfer proteins may contain multiple
iron-sulfur centers.

24. Respiratorychain
1) Most constituents of the respiratory chain are
embedded in the innen
Mitochondria membrane (or in the cytoplasmic
membrane of aerobic bacteria
2) Electrons are transferred from NADH to O2 via multi-
subunit inner membrane complexes I, III, & IV, plus
coenzyme Q and cytochrome c. Within each complex,
electrons pass sequentially through a series of electron
carriers.

25. Complex Name No. of
Proteins
Prosthetic
Groups
Complex
I
NADH
Dehydrogenase
46 FMN, 9 Fe-S
centers
Complex
II
Succinate-CoQ
Reductase
5 FAD, cyt b560, 3
Fe-S centers
Complex
III
CoQ-cyt c
Reductase
11 cyt bH, cyt bL,
cyt c1, Fe-SRieske
Complex
IV
Cytochrome
Oxidase
13 cyt a, cyt a3,
CuA, CuB

26. Respiratory chain inhibitorsinclude the following:
(A) Rotenone (a common rat poison) blocks electron transfer in complex I.
(B) Antimycin A blocks electron transfer in complex III.
(C) Cyanide and carbon monoxide inhibit complex IV.
ComplexI catalyzes oxidation of NADH,
with reduction of coenzyme Q:
NADH + H+ + Q � NAD+ + QH2
The initial electron transfers are:
NADH + H+ + FMN � NAD+ + FMNH2
FMNH2 + (Fe-S)ox � FMNH� + (Fe-
S)red + H+
Succinate Dehydrogenase
of the Krebs Cycle is also called
complex II or Succinate-CoQ Reductase. .

27. Complex III
accepts electrons from coenzyme QH2 that is generated by electron transfer in complexes I
and II. The structure and roles of complex III are discussed in the section on oxidative
phosphorylation. Cytochrome c1, a prosthetic group within complex III, reduces
cytochrome c, which is the electron donor to complex IV.
Cytochrome oxidase
(complex IV) carries out the following irreversible reaction:
O2 + 4 H+ + 4 e- � 2 H2O
So the ETC cycle has been completed.

28. REFERENCE
1.Advanced biology-Kent michael
2.Cell and molecular Biology-
Gerald Karp
3. Geoffrey M.Cooper-The cell a
moleculer approach.
4. molecular and cell biology- Lodish et.al.
Websites:
www.kbiotech.com
www.wikipedia.com