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Biological Oxidation by Satish

Biological Oxidation by Satish

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Published by: Biochemistry Den on Feb 09, 2012
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Life Sciences Study Materials
http://biochemden.in
Biological Oxidation---------------------------------------------------------------------------------------------------------------------------------
-------------------------------------------------------------------------------------------------------Prepared by
I.Satish Kumar
, Lecturer in Biochemistry
,http://biochemden.in
 1
 
(Life Sciences Study Materials)
(Useful for B.Sc. and M.Sc. Students)
 
I.Satish Kumar
Email:satishkumar.i1980@gmail.com 
http://biochemden.in 
Facebook:satishkumar.i1980@gmail.com Biochemistryden.den2@gmail.com 
 
My Sweet Name: _________________________________________________Class _______________________ Roll Number ________________________College Name: ___________________________________________________
 
Life Sciences Study Materials
http://biochemden.in
Biological Oxidation---------------------------------------------------------------------------------------------------------------------------------
-------------------------------------------------------------------------------------------------------Prepared by
I.Satish Kumar
, Lecturer in Biochemistry
,http://biochemden.in
 2
Biological Oxidation
STRUCTURE OF MITOCHONDRIAHISTORICAL:
1880 - Kolliker - observed in muscle cells of insects
1882 - Flemming- gave the name as “fila”
1894 - Altamann- gave systematic name observation name as “Bioblast”
1897-98 – Benda- gave name as “Mitochondria”. He stained the mitochondria with
“alizarin” and “crystal violet”.
1900 - Michaelis- stained mitochondria with “jaunus green”
1934 - Bensley & Hoperr said mitochondria is the site for the cellular respiration.
OTHER NAMES:
Fuchsinophilic granules,
Parabasal bodies,
Plasmosomes,
Fila,
Chondriosomes,
Vernicules
Bioblasts.
BIOCHEMISTRY & ANATOMY OF A MITOCHONDRION:
Mitochondria were first observed by “Altmann” in 1894 who described as “bioblasts”. Benda(1897) called them “mitochondria”. (mito
G
=thread; chondrion
G
=granule). The number of mitochondriavaries with the cell type and functional stages. In eukaryotes, approximately 2000 mitochondriasoccupies one-fifth of its total cell volume. The mitochondrial chemical composition is concerned,mitochondria consist of 65-70% proteins, 25-30% lipids, 5-7% DNA and 0.5%RNA. The4 outermembrane of the mitochondria has “porins”, which permits molecules upto 10kd. Matrix is gel likesolution, containing high concentration of soluble enzymes, substrate, nucleotide cofactors, ions.The mitochondrion is a subcellular organelle having the outer and inner membranes enclosingthe matrix. The inner membrane is highly selective in its permeabily characteristics. The innermembrane contains the respiratory chain and translocating systems. The knobs like protrusionsrepresent the ATP synthase system. The inner membrane is folded into a series of internal ridgescalled “Cristae”, which may be longitudinally or transversely oriented, branched or tabular. Hence, thereare two compartments in mitochondria: the intermembrane space between the outer and innermembranes and the matrix, which is bounded by the inner membrane. Most of the reactions of the TCAcycle and fatty acid oxidation occur in the matrix.
ENZYME LOCALIZATION IN MITOCHONDRIA:
LOCALISATION OF SOME ENZYMES IN RAT-LIVER MITOCHONDRIA:
 
Outer membrane
Monoamine oxidase
Kynurenine-3-monoxygenase
NADH dehydrogenase
Acyl. CoA Synthetase4
Phospholipase-A
2
 
Nucleoside diphosphate kinase
Space between the membranes:
Adenylate kenase
Creatine Kinase
 
Inner membrane:
 
NADPH dehydrogenase
Iron-Sulfur proteins
Cyt.b,c,c
1
and aa
3
 
F
1
ATPase
Succinate dehydrogenase
Carnitine acyl transferase
Matrix:
 
TCA Cycle enzymes
Fatty acyl-CoA oxidationenzyme.
 
Life Sciences Study Materials
http://biochemden.in
Biological Oxidation---------------------------------------------------------------------------------------------------------------------------------
-------------------------------------------------------------------------------------------------------Prepared by
I.Satish Kumar
, Lecturer in Biochemistry
,http://biochemden.in
 3 
Functions of mitochondria:
The mitochondria are organelles which transfer the chemical energy of themetabolites of the cell (through Krebs cycle and the respiratory chain.) into the high-energyphosphate bond of ATP. Thus, mitochondria are the “power house of the cell”, that producethe4 energy necessary for many vital cellular functions via, motility contraction (musclecontraction), biosynthesis of cell bioluminescence etc.
Mitochondriall Electron transport chain [MtETC]
Prokaryotic cells have no mitochondrial bodies; their plasma membrane appears tobe the site of electron transport and oxidative phosphorylation. Thus, all the cytochromepigment and a number of dehydrogeneous associated with the TCA Cycle, namely Succinic,malic and
α
-KG dehydrogenase, are localized in the bacterial plasma membrane.In 1948, A.L.Lehninger showed that in the animal cell, the mitochondrion was the solesite for oxidative phosphorylation, the TCA Cycle and fatty acid oxidation.
Components:
There are five different kinds of electron carriers that participate in the transport ofelectrons from substrates as they are oxidized in the mitochondria. Inb addition, Cu
+2
ispresent and functions in the enzyme, Cytochrome oxidase, that catalyzes the reduction of O
2
(1)
Nicotinamide Nucleotides:
Two pf the oxidations in the TCACycle involve the removal of the equivalent oftwo hydrogen atoms from the substrates,malate and isocitrate. In two others, thosecatalyzed by pyruvate dehydrogenase and
α
-Ketogularate dehydrogenase, the electronsare transferred first to lipoic acid and then via aflavorprotein to NAD
+
.SH
2
+ NAD
+
 
S + NADH + H
+
(2)
Flavoproteins:
These proteins contain a very tightly, sometimes covalently bound flavin nucleotide,either FMN (or) FAD. The oxidized flavin nucleotide can accept either one electron (or) two(yielding FADH
2
(or) FMNH
2
). The standard reduction potential of a flavin nucleotide, unlikethat of NAD (or) NADP, depends on the protein with which it isw associated. The flavinnucleotide should be considered part of the flavoproteins activesite, not as a resultant (or)product6 in the electron-transfer reaction. Because flavoproteins can participate in eitherone-or-two electron transfers, they can serve as intermediate between react6ions in whichtwo electrons are donated and these in which only one electron is accepted.NADH + H
+
+ FMN
NAD
+
+ FMNH
2
 Succinate + FAD
Fumarate + FADH
2
 (3)
Iron – Sulfur proteins:
This type of protein was first encountered as ferredoxin, a reducing agent involved innitrogen fixation and photosynthesis in plants before it was recognized to funct6ion inmt.E.T in animals.
The iron atoms are arranged in paris in an iron-sulfur bridge, which is bounded to thesulfur atoms of Cysteine residues in the protein.
Some iron-Sulfur proteins such as spinach ferredoxins contains only two iron atoms(Fe
2
S
2
) while others contain four (Fe
4
S
4
)(4)
Quinones:
Mitochondria contain quinine called “Ubiquinone” (also called “Coenzyme.Q”(or) simply “Q”) which is a lipidsoluble benzoquinone with a long isoprenoid sidechain. Ubiquinone can accept one electron to become the semiquinone radical (QH
*
)or two electrons to form ubiquinol (QH
2
), it can act at the junction between a twoelectron donor and a one-electron acceptor, because ubiquinone is both small and

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