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Patrishia Luber

4Bio1 Mitochondrial Structure & Function


Glycolysis in the cytosol + 10 reactions:
9: Mitochondrial Structure and Function Glucose pyruvate + NADH
Net synthesis of 2 ATP per molecule of glucose
First organisms were anaerobes
In the presence of oxygen:
Appearance of cyanobacteria 2.4-2.7 BYA which
NADH 30 ATP
produced atmospheric oxygen from
Pyruvate:
photosynthesis (split water to form oxygen)
Pyruvate gets transported to the matrix
Decarboxylated to form 2-carbon acetyl
9.1 Mitochondrial Structure and Function
group
Mitochondria are large enough to be seen Acetyl group is transferred to coenzyme A
under a light microscope and varies in their producing acetyl CoA
overall structure depending on the cell type ** decarboxylation and transfer of acetyl is catalyzed
ranging from 1-4 m in length by pyruvate dehydrogenase **
Fission is induced by contact with thin tubules
from the ER which initiates the constriction
If fusion > fission: elongated and interconnected
mitochondrion
If fission > fusion: more numerous and distinct
mitochondrion
Mitochondria also plays a vital role in the uptake
and regulation of calcium ions
o During high concentrations of calcium in the
cytoplasm, the mitochondria can take in the
excess caclcium

Mitochondrial Membranes
Two membranes:
Outer mitochondrial membrane: 50% lipid by
weight, contains porins (similar to bacterial
membranes)
Inner mitochondrial membrane: devoid of
cholesterol and rich in a phospholipid called
cardiolipin, is highly impermeable
o Inner boundary membrane: rich in
proteins responsible for the import of
mitochondrial proteins
o Cristae: invaginated membranous sheets;
contains large amounts of membrane surface
o Cristae junctions join the two
Matrix is the space within the mitochondria
while intermembrane space exists between ** Mnemonic:
the outer and inner mitochondrial membranes Intermediates: Goodness Gracious, Father Franklin
o Matrix is more viscous, gel-like due to high Did Go By Picking Pumpkins (to) Prepare Pies
protein content Enzymes: Hungry Peter Pan And The Growling Pink
o Intermembrane proteins play a role in Panther Eat Pies **
apoptosis
Mitochondrial matrix also contains ribosomes and Tricarboxylic Acid (TCA) Cycle/Krebs Cycle
circular DNA Substrate is oxidized in the matrix (except
o Nonchromosomal DNA codes for for succinate dehydrogenase)
mitochondrial proteins (13 in humans) Named after Hans Krebs
o Maternal inheritance; egg cell contains
mitochondria Process:
o The RNA polymerase in mitochondria is Acetyl CoA (2C) + oxaloacetate (4C) citrate
different than the ones the nucleus uses; it is (6C)
a single subunit similar to bacteriophages ** Citrate is decreased in chain length one carbon at
(bacterial viruses) a time to recycle the 4C oxaloacetate **
Isocitrate
9.2 Oxidative Metabolism -Ketoglutarate (5)
o CO2
o NAD NADH
1. Glycolysis in cytoplasm Succinyl-CoA (4)
Glucose (6C) 2 pyruvate (3C) o CO2
2. PDC Pyruvate Dehydrogenase o NAD NADH
Complex in matrix Succinate
Pyruvate acetyl-CoA o GDP + P GTP
3. Krebs Cycle in Matrix
Acetyl-CoA NADH +
FADH2
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(NADH + FADH2 are electron carriers)
4. Electron Transport Chain in
inner membrane
Patrishia Luber
4Bio1 Mitochondrial Structure & Function
Fumarate o Chemiosmotic mechanism
o FAD FADH2 o Each pair of electrons transferred from
Malate NADH 3 ATP
o Needs an input of water FADH2 2 ATP
Oxaloacetate (to be recycled) o Net gain is 36 ATP
o NAD NADH
9.2 Role of Mitochondria in ATP Formation
Energy is extracted by the mitochondria from
substrates by generating ionic gradients
Oxidative phosphorylation: ATP formation is
driven by energy released from electrons
removed during oxidation
Substrate-level phosphorylation: ATP is formed
directly by a transfer of phosphate group from a
substrate molecule to ADP

Oxidation-Reduction Potentials
**Reduced = gain electrons, lose H; Oxidized = lose
electrons, gain H**
**Reducing agent = removes e oxidized**
**Oxidizing agent = hoards H reduced**
Reducing agents are ranked according to
electron-transfer potential
Substances with high electron-transfer potential
are strong reducing agents (can lose H, can gain
e) such as NADH
Redox potential: voltage produced by a half-cell
under standard conditions
o G : difference between E0 = (E1 E2)
o (+) G = nonspontaneous
o (-) G = spontaneous
Electron Transport
Dehydrogenase enzyme catalyzes and
transfers pairs of electrons from substrates to
coenzymes
Forming NADH and FADH2
Succinate dehydrogenase FADH2

**Mnemonic: Can I Keep Selling Sex For Money,


Officer?** Types of Electron Carriers
**all four (except ubiquinone) are prosthetic groups, having
a non-amino acid component that are tightly associated
Importance of Reduced Coenzymes in Forming with proteins **
ATP Flavoproteins: polypeptide bound to Flavin
FADH2 and NADH produced from TCA contains adenine dinucleotide (FAD) or Flavin
high-energy electrons produced from oxidation mononucleotide (FMN)
Mitochondria are not able to import the NADH o Derived from riboflavin (vitamin B2)
formed by glycolysis in the cytosol and must o Capable of accepting 2 protons and 2
enter via: electrons
o Malate-aspartate shuttle and reduce NAD o NADH dehydrogenase and succinate
to NADH dehydrogenase
o Transfer electrons to FAD producing FADH 2 via Cytochromes: contain a heme
glycerol phosphate shuttle o Iron atom of heme undergoes a reversible
In forming ATP via Electron Transport Chain: transition from Fe3 Fe2
High-energy electrons are passed from FADH 2 or o Acceptance and loss on single electron
NADH to electron carriers in the electron- o 3 types: a, b, c
transport chain in the inner mitochondrial Three copper atoms
membrane o Located within a single protein complex of
o Releases energy in to form of the inner mitochondrial membrane
electrochemical gradient of protons o Accept and donate a single electron (Cu2
across the membrane Cu1)
o Low-energy electrons are passed to the final Ubiquinone (UQ/Q): lipid-soluble molecule
acceptor, Oxygen which becomes containing a long hydrophobic chains composed
reduced to water of 5-caron isoprenoid units
Controlled movement of protons back across the o Able to accept and donate 2 electrons and
membrane protons
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Patrishia Luber
4Bio1 Mitochondrial Structure & Function
o Ubiquinone [R] ubisemiquinone [R] Contains a heme group which attracts escaped
ubiquinol electrons which prevents the formation of
Iron-sulfur proteins: iron-containing proteins in superoxide radicals
which the iron is linked to inorganic sulfide Electron transfer is not accompanied by proton
ions as part of an iron-sulfur center translocation
o ~2 or 4 atoms of iron and sulfur linked to the Complex III: Cytochrome bc1
protein at cysteine residues Catalyzes the transfer of electrons from ubiquinol
o Capable of donating or accepting a single to cytochrome c
electron 4 protons are translocated for every pair of
o Redox-potential depends on the electrons
hydrophobicity and charge of amino acid Complex IV: Cytochrome c Oxidase
residues Translocation of 4 protons is coupled to
conformational changes for every 2 molecules of
In the ETC, electrons are passed downhill (loses water
energy) Contains 13 subunits; 3 are encoded by mtDNA
Final acceptor is Oxygen Water 4 protons are also consumed in the reaction to
transfer the electrons
Electron-Transport Complexes
In the electron transport chain: 9.4 Translocation and Establishment of PMF
Ubiquinone and cytochrome shuttle Translocation of the protons is electrogenic
electrons to and from the complexes (voltage-producing)
Complexes I, II, III, and IV of protein Makes the intermembrane space more acidic and
NADH enters via complex I the matrix more basic
FADH2 enters via ubiquinone Both the pH and the electric potential contribute
to the proton motive force need of the protons
to go back to the matrix where there is a lower
NADH Complex I (NADH concentration
Reductase)
Treatment with 2,4-dinitrophenol (DNP) made
Ubiquinone
cells continuously oxidize substrates without
FADH
generating any ATP
2
Complex III o Used as an inhibitor of ATP
(Cytochrome o Was prescribed as a diet pill, causing deaths
Reductase)
Complex II of patients
(Succinate Cytochrome C o The drug can uncouple oxidation and
dehydrogen phosphorylation because it combines with
ase) the protons and can carry the protons across
Cytochrome Oxidase
the membrane back to the matrix without
passing through the ATP synthase
Complex I, III, IV = coupling sites and are proton
pumps 9.5: The Machinery for ATP Formation
Complex I: NADH dehydrogenase Fernandez-Moran observed a layer of spheres
Mammalian version is L-shaped and has 45 attached to the inner membrane which was later
different subunits isolated by Racker which he called coupling
FMN-flavoprotein oxidizes NADH factor 1 (F1), an ATPase which hydrolyzes ATP
Electrons are transferred through 7 iron-sulfur Catalytic portion is the F1 sphere
centers
Electrons are transferred to ubiquinone (for Structure of ATP Synthase
transport) Mushroom-shaped protein complex with two
Movement of electrons is accompanied by 4 components:
protons from the matrix to the intermembrane o Spherical F1 head
space Conserved in bacterial and mitochondrial
Membrane embedded domain has -helixes ATP synthases
oriented parallel to the membranes surface and subunits are arranged alternately
Movement of the electrons to ubiquinone induces Each F1 contains 3 catalytic sites for
a conformational change causing the lateral ATP synthesis one on each subunit
movement of the helices tilting change in subunit connects it to the F0
ionic concentration forcing the protons to go o Basal F0 embedded in the inner membrane
outside Contains 3 different polypeptides
Complex II: Succinate dehydrogenase Contains a channel through which
Consists of 4 polypeptides: 2 hydrophobic anchor
protons are conducted from the
+ 2 hydrophilic subunits with succinate intermembrane space to the matrix
dehydrogenase
Pathway for FADH2 Basis of ATP Formation According to the Binding
Change Mechanism

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Patrishia Luber
4Bio1 Mitochondrial Structure & Function
The energy released by the translocation of Proton binds to an acidic residue (Asp61 in E.
protons is not used to drive ADP phosphorylation coli) on one of the c subunits
but to change the binding affinity for the active Proton binding causes the ring to move 30
site for the ATP product Bound proton is carried in a full rotation
Each active site progresses successively through before being released to another half-channel
3 distinct conformations that have different leading to the matrix
affinities for substrates and products
o The 3 catalytic sites has different chemical 9.6 Peroxisomes
properties Simple membrane-bound organelles that
o At any given instant, one site is L (loose),
contains a crystalline core of oxidative enzymes
one is T (tight), one is O (open) Multifunctional organelles containing more than
ATP is synthesized by rotational catalysis in which
50 enzymes for oxidation of very-long-chain fatty
one part of the ATP synthase rotates relative to acids (VLCFA) and synthesis of plasmalogens (a
another part class of phospholipids where one of the FA is
o Rotation is driven by the movement of linked to glycerol by an ether linkage not an
protons ester) which are abundant in the myelin sheaths
o Electrical energy in the proton gradient is Luciferase is also a peroxisomal enzyme
transduced to mechanical energy of a Form from preexisting organelles and uses the
rotating stalk
same proteins as mitochondria
The apical end of the is asymmetric allowing
Imports preformed proteins from the cytosol
different faces of it to interact with the subunits
similar to mitochondria
causing them to adopt L/T/O conformations
Site of synthesis and degradation of hydrogen
Yoshida showed the rotation via a fluorescently
peroxide, a highly reactive and toxic oxidizing
labeled actin filament attached to the subunit
agent
Rotary devices are rare in living organisms and
Plant seedlings contain glyoxisomes which
only occurs in two instances: ATP synthases and
break down the stored FA for energy and nutrition
bacterial flagella
into carbohydrate
12 C subunits of the F 0 base is assembled into a
ring that resides within the inner membrane; C
ring is attached to the stalk Diseases
Downhill movement of protons through the Zellweger syndrome lack peroxisomal enzymes
synthase drives the rotation of the C ring which due to defects in translocation of proteins from
provides torque that drives the rotation of the the cytoplasm into the peroxisome.
subunit leading to the synthesis and release of Adrenoleukodydstrophy is caused by lack of a
ATP peroxisomal enzyme, leading to fatty acid
Proton from the intermembrane space enters accumulation in the brain and destruction of the
a half-channel within in the stationary a myelin sheath of nerve cells.
subunit

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