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Energy Transducing Membrane: Submitted by - Farheen Khan Roll No - 19Mbs007 Msc. Biosciences 1 Year (2 Semester)
Energy Transducing Membrane: Submitted by - Farheen Khan Roll No - 19Mbs007 Msc. Biosciences 1 Year (2 Semester)
Membrane
SUBMITTED BY –
Farheen Khan
Roll no –19MBS007
MSc. Biosciences
1st year (2nd semester)
ELECTRON TRANSPORT CHAIN
The electron transport chain uses the electrons from electron carriers to
create a chemical gradient that can be used to power oxidative
phosphorylation. Oxidative phosphorylation is a highly efficient method
of producing large amounts of ATP, the basic unit of energy for
metabolic processes. During this process electrons are exchanged
between molecules, which creates a chemical gradient that allows for
the production of ATP. The most vital part of this process is the electron
transport chain, which produces more ATP than any other part of
cellular respiration .
Complex I
To start, two electrons are carried to the first complex aboard NADH.
Complex I is composed of flavin mononucleotide (FMN) and an
enzyme containing iron-sulfur (Fe-S). FMN, which is derived from
vitamin B2 (also called riboflavin), is one of several prosthetic groups or
co-factors in the electron transport chain. A prosthetic group is a non-
protein molecule required for the activity of a protein. Prosthetic groups
can be organic or inorganic and are non-peptide molecules bound to a
protein that facilitate its function.
Prosthetic groups include co-enzymes, which are the prosthetic groups
of enzymes. The enzyme in complex I is NADH dehydrogenase, a very
large protein containing 45 amino acid chains. Complex I can pump
four hydrogen ions across the membrane from the matrix into the
intermembrane space; it is in this way that the hydrogen ion gradient is
established and maintained between the two compartments separated by
the inner mitochondrial membrane.
Q and Complex II
Complex II directly receives FADH2, which does not pass through
complex I. The compound connecting the first and second complexes to
the third is ubiquinone (Q). The Q molecule is lipid soluble and freely
moves through the hydrophobic core of the membrane. Once it is
reduced to QH2, ubiquinone delivers its electrons to the next complex in
the electron transport chain. Q receives the electrons derived from
NADH from complex I and the electrons derived from FADH2 from
complex II, including succinate dehydrogenase. This enzyme and
FADH2 form a small complex that delivers electrons directly to the
electron transport chain, bypassing the first complex. Since these
electrons bypass, and thus do not energize, the proton pump in the first
complex, fewer ATP molecules are made from the FADH2 electrons.
The number of ATP molecules ultimately obtained is directly
proportional to the number of protons pumped across the inner
mitochondrial membrane.
Complex III
The third complex is composed of cytochrome b, another Fe-S protein,
Rieske center (2Fe-2S center), and cytochrome c proteins; this complex
is also called cytochrome oxidoreductase. Cytochrome proteins have a
prosthetic heme group. The heme molecule is similar to the heme in
hemoglobin, but it carries electrons, not oxygen. As a result, the iron ion
at its core is reduced and oxidized as it passes the electrons, fluctuating
between different oxidation states: Fe2+ (reduced) and Fe3+ (oxidized).
The heme molecules in the cytochromes have slightly different
characteristics due to the effects of the different proteins binding them,
which makes each complex. Complex III pumps protons through the
membrane and passes its electrons to cytochrome c for transport to the
fourth complex of proteins and enzymes. Cytochrome c is the acceptor
of electrons from Q; however, whereas Q carries pairs of electrons,
cytochrome c can accept only one at a time
Complex IV
The fourth complex is composed of cytochrome proteins c, a, and a3.
This complex contains two heme groups (one in each of the
cytochromes a and a3) and three copper ions (a pair of CuA and one
CuB in cytochrome a3). The cytochromes hold an oxygen molecule very
tightly between the iron and copper ions until the oxygen is completely
reduced. The reduced oxygen then picks up two hydrogen ions from the
surrounding medium to produce water (H2O). The removal of the
hydrogen ions from the system also contributes to the ion gradient used
in the process of chemiosmosis.
THE CHEMIOSMOTIC THEORY
Although some ATP synthesis is catalysed by soluble enzyme systems
—for example, phosphoglycerate kinase in the glycolytic pathway—the
large majority is generated by membrane-bound enzyme complexes that
are restricted to a particular class of membrane. These ‘energy-
transducing’ membranes include the plasma membrane of simple
prokaryotic cells such as respiratory or photosynthetic bacteria, the
inner membrane of mitochondria, and the thylakoid membrane of
chloroplasts . These membranes have a related evolutionary origin
because chloroplasts and mitochondria are commonly thought to have
evolved from a symbiotic relationship between a primitive, nonrespiring
eukaryotic cell and an invading prokaryote. The membranes not only
catalyse ATP synthesis but also control the transport of ions and
metabolites and the oxidation state in their environment. Energy-
transducing membranes possess a number of distinguishing features.
Each membrane has embedded within it two distinct types of proton
pump. The nature of the primary proton pump depends on the energy
source used by the membrane. In the case of mitochondria or respiring
bacteria, an electron transfer chain catalyses the energetically ‘downhill’
transfer of electrons from substrates to final acceptors such as O2 and
uses this energy to generate an electrochemical gradient of protons. The
term electrochemical is important and tells us that the energy gradient
has electrical and chemical components (discussed later).
Photosynthetic bacteria exploit the energy available from the absorption
of quanta of visible light to generate a proton electrochemical gradient,
whereas chloroplast thylakoids utilise two photon capture processes in
series to generate the gradient and to drive electrons ‘uphill’ from water
to acceptors such as NADP+ . The detailed topologies of the
membranes differ, and to facilitate comparison it is a useful convention
to define the side of the membrane to which protons are pumped as the
P, or positive, side and the side from which they have originated as the
N, or negative, side .
In each case, the primary pump utilising either electrons (e−) from oxidations or
driven by photons (hν) pumps protons from the N (negative) compartment to the
P (positive) compartment. The photosynthetic bacterial photon-driven proton
pump involves an electron transport cycle (not shown), whereas in addition to
pumping protons, the chloroplast pumps electrons ‘uphill.’ Note that the ATP
synthase in each case is shown acting in the direction of ATP hydrolysis, when it
would also pump protons from the N- to the P-phase. The outer bounding
membranes (dashed) do not participate in energy transduction .
In contrast to the variety of primary proton pumps, all energy-
transducing membranes contain a highly conserved secondary proton
pump termed the ATP synthase or the H+ translocating ATPase. If this
pump were operating in isolation in a membrane, it would hydrolyse
ATP to ADP and Pi (shorthand for the phosphate anion) and pump
protons in the same direction as the primary pump. However, the
essence of the chemiosmotic theory is that the primary proton pump
generates a sufficiently large electrochemical gradient of protons to
force protons back through the secondary pump so that it reverses and
synthesises ATP from ADP and Pi . Note that metabolism (i.e.,
electron flow or ADP phosphorylation) within both the primary
pump and the secondary pump is tightly coupled to proton
translocation. Thus, it is generally accepted that there is nointernal
‘slip’ within these pumps that would allow one to occur without the
other. internal ‘slip’ within these pumps that would allow one to occur
without the other.
CHEMIOSMOTIC COUPLING
An ATP synthase complex is incorporated into a proton-impermeable
phospholipid membrane such that the ATP binding site is on the
outside.
(a) ATP is added, the nucleotide starts to be hydrolysed to ADP + Pi,
and protons are pumped into the vesicle lumen. As ATP is converted
to ADP + Pi, the energy available from the hydrolysis steadily
decreases, whereas the energy required to pump further protons against
the electrochemical gradient that has already been established steadily
increases.
(b) Soon an equilibrium is attained.
(c) If this equilibrium is now disturbed, for example, by removing ATP,
the ATP synthase will reverse and attempt to re-establish the
equilibrium by synthesising more ATP.
Net synthesis, however, would be very small because the
electrochemical gradient of protons would rapidly collapse and a new
equilibrium would be established. For continuous ATP synthesis, a
primary proton pump, driven in this example by photons (hν), is
required to pump protons across the same membrane and replenish the
gradient of protons. A proton circuit has now been established. This is
what occurs across energy-conserving membranes:
ATP is continuously removed for cytoplasmic ATP-consuming
reactions, while the electrochemical gradient of protons, Δp, is
continuously replenished by the respiratory or photosynthetic electron-
transfer chains.
REFERENCES
Bioenergetics DAVID G. NICHOLLS Buck Institute for
Research on Aging, Novato, California, USA STUART J.
FERGUSON Department of Biochemistry, University of
Oxford, W.R. Miller Fellow of St. Edmund Hall, Oxford,
UK
https://www.sciencedirect.com/science/article/pii/B9780125
181242500060
https://courses.lumenlearning.com/wm-
biology1/chapter/reading-electron-transport-chain/
http://fig.cox.miami.edu/~cmallery/255/255etc/chemiosm.ht
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