1.

Flavins have widely varying E​o/​ values compared to NAD which has a constant
value since the flavins are sometimes covalently or tightly associated with protein
molecules whilst the NAD molecules are not tightly associated with the proteins.
The E​o/​ of the flavins varies with the proteins by which it is associated with.

2. In total there are three iron sulphur complexes. The three complexes are:

A single iron ion bound by four cysteine residues which contributes a total of four
chelated sulphur ions on the iron.

2Fe-2S cluster- In this the two iron ions are bridged by two sulphide ions and
bound by four cysteine residues each contributing a sulphur ion. In total there are
six chelated sulphur ions.

4Fe-4S cluster- In this complex the four Fe ions are bridged by four sulphide ions
and bound by four cysteine residues. In this complex there are a total of eight
chelated sulphur ions.
 The Rieske iron sulfur complex differs from the other iron sulphur complex since
it has two nitrogen molecules that are from histidine residues chelated onto one of
the Fe ion.

3. Cytochromes are proteins that contains a iron-heme prosthetic group which gives
them the ability to absorb visible light in their reduced and oxidised state making
them distinguishable from each other. The cytochromes facilitate only one electron
oxidation/reduction and like the flavins its redox potential of the heme-iron atom
at the center of the porphyrin ring is dependant on the protein environment it is in.
There are three types of cytochromes present in mammalian mitochondria. These
are known as :

Cytochrome A- The a type cytochrome has a porphyrin ring with an attached

ethylene group, a hydrophobic chain and a carbonyl group. It forms the longest
waveband of 600nm in the presence of visible light and the heme cofactor is
tightly associated with its protein. There is no covalent association. This
cytochrome is an integral protein of the inner membrane of the mitochondria.

Cytochrome B- the b type cytochrome is an integral protein of the inner membrane

that has a porphyrin ring with two ethylene group attached to the ring. It absorbs
visible light at 559 nm and the heme cofactor is tightly but not covalently
associated with its protein.

Cytochrome C- The c type cytochrome has a porphyrin ring with two cysteine
residues attached. It absorbs visible light at 562 nm and the heme cofactor is
covalently associated with its proteins through cysteine residues. This cytochrome
 can act as an integral protein or a soluble protein that associates through
electrostatic interactions with the outer surface of the inner membrane.

4.

5. The mammalian complex I consists of 46 polypeptides chains and contains FMN,

iron sulphur complexes and Q. Complex I is L shaped and has matrix arm and a
membrane arm. NADH₂ becomes dehydrogenated by NADH dehydrogenase and
passes its two protons to FMN to produce FMNH₂. FMN acts as an adapter since
the iron sulphur complexes can only facilitate one electron oxidation/reduction at a
time. The FMNH₂ passes one election at a time through a series iron-sulphur
complexes to the N-2 iron sulphur complex of the matrix arm. The N-2 complex
then transfers the protons to Q to form the semiquinone QH and then QH₂ which
diffuses into the bilayer because of its hydrophobic nature. At this complex energy
is conserved since the energy that is released from the redox reactions that occur
within the complex is used to pump protons from the matrix into the
intermembrane space.

6. Complex II contains four different subunits, A,B,C and D, and 5 prosthetic groups
. Subunits A and B extend into the matrix and contain three 2Fe-2S centers, FAD,
and a binding site for succinate whilst C and D are integral protein that each have
three transmembrane helices and contains heme b and a binding site for
ubiquinone. In complex II, succinate is converted to fumarate by the removal of
two protons and two electrons by succinate dehydrogenase. The two protons and
electrons are picked up by FAD to produce FADH₂. Since the iron sulphur centers
can only facilitate one proton FAD acts as an adapter. FADH₂ sends one proton at
a time through the iron sulphur centers and to the ubiquinone binding site where it
 combines with ubiquinone (Q), to form the semiquinone QH and then ubiquinol
QH₂. The heme b of the complex is not in the direct path of the electron transfer
so it tends to keep the protons on the right track by preventing it from leaking out
of the system and reacting with oxygen to produce reactive oxygen species which
causes the mutation of DNA.
7. The net reduction of ubiquinone in the mammalian mitochondria can also occur
via the glycerol 3 phosphate shuttle and the beta oxidation of fatty acyl coA.

In the glycerol 3 phosphate shuttle, the reduction of dihydroxyacetone phosphate

from glycolysis is done by cytoplasmic glycerol 3 phosphate dehydrogenase and
NADH to produce glycerol 3 phosphate which is then oxidized by mitochondrial
glycerol 3 phosphate dehydrogenase and FAD. FAD which resides on the surface
of the inner mitochondrial membrane channels electrons into the respiratory chain
by picking up two protons from the glycerol 3 phosphate to form FADH₂ and in
turn reducing ubiquinone by transferring the two protons to it to form QH₂.

In the beta oxidation of fatty acyl coA, the electrons from FADH​2​ of the reduced
acyl coA dehydrogenase are transferred onto a flavoprotein called the
electron-transferring flavoprotein (ETF). The electron from ETF are then
 transferred to an iron sulphur protein known as ubiquinone oxidoreductase. This
protein then transfers electrons into the respiratory chain by reducing ubiquinone
(Q) to ubiquinol (QH₂).

Reference List

Lennon, Dr. Adrian. 2019. "ETC Lecture 1". Presentation, The University Of The
West Indies St.Augustine, , 2019.

Lennon, Dr. Adrian. 2019. "ETC Lecture 2". Presentation, The University Of The
West Indies St.Augustine, , 2019.

Nelson, David L, Michael M Cox, and Albert L Lehninger. 2013. ​Lehninger,

Principles Of Biochemistry.​ New York: Macmillan Higher Education.