Bioelectricity

In the recent decades, consumption of energy within the world is increasing enormously. Energy
sources are classified into three batches: fossil fuels, renewable sources and nuclear sources. The
non-renewable sources of energy, which include an enormous portion of energy consumption,
could be categorized into two major classifications: nuclear and fossil energy. Fossil fuels
negatively influence the nature owing to the emission of carbon dioxide. It follows logically
from what has been said that the consumption of fossil fuels has severely hazarded human life
through its drastic consequences, such as global warming and atmospheric pollution.
One of the latterly proposed alternative energy sources is fuel cell (FC) which generates energy
using high value metal catalysts. In actual fact, FC is of plethora advantages over other kinds of
energy generators, e.g. no emissions of environmental polluting gases (such as SOx, NOx, CO 2
and CO), higher efficiency, no existence of mobile parts, as a result, lack of sonic pollution.
Bioelectricity is the production of electricity by organisms on account of production of electrons
resulting due to their metabolism. These electrons produced can be captured so as to maintain a
stable or continuous source of energy production. Bacterial cells when provided a suitable
substrate can metabolize the components producing electrons which can be harvested and
utilized by connecting them through a circuit. These components can be packed into an assembly
called a ‘microbial fuel cell’ (MFC) proving to be a source of energy. Anaerobic digestion of
substrate by the micro-organisms is essential for the production of the electrons occurring due to
their metabolism.
Microbial fuel cell (MFC) uses an active microorganism as a biocatalyst in an anaerobic anode
compartment for production of bioelectricity. MFCs consist of anode and cathode chambers,
physically separated by a proton exchange membrane (PEM). Active biocatalyst in the anode
oxidizes the organic substrates and produces electrons and protons. The protons are conducted to
the cathode chamber through the PEM, and the electrons are conveyed through the external
circuit. Protons and electrons are reacted in the cathode chamber along with parallel reduction of
oxygen to water.
MFCs are devices that can convert chemical energy into electrical energy by the process of
oxidation of various carbon sources or even organic wastes carried out by electrochemically
active bacteria. Geobacter and Shewanella species account for the majority of the microbial
population that have been utilized in MFC technology. One of the most important merits of MFC
technology is its environment friendly nature as compared to other energy production
technologies that resulted in the emission of carbon dioxide and induce global warming. The
inclusion of waste products (solid waste biomass, food waste, domestic and other wastewaters)
as substrates in MFC technology makes it a more potent for sustainable energy generation.
There are a number of restrictions that MFC technology faces in terms of its utilization and
application in energy production. One of the most important demerits is the inability to scale up
MFC models on a large and commercial scale. The electricity production by MFC technology as
of currently when compared with methanogenic anaerobic digestion falls short of economical.

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 Electron Transport and Oxidative Phosphorylation
The endergonic synthesis of ATP from ADP and Pi in mitochondria is catalyzed by proton
translocating ATP synthase (Complex V). It is driven by the electron-transport process. complex
V is physically distinct from the proteins mediating electron transport (Complexes I–IV), the free
energy released by electron transport must be conserved in a form that ATP synthase can utilize.
Such energy conservation is referred to as energy coupling or energy transduction.
The chemiosmotic hypothesis
Proposed in 1961 by Peter Mitchell
It is the model most consistent with the experimental evidence.
It postulates that the free energy of electron transport is conserved by pumping H+ from the
mitochondrial matrix to the intermembrane space so as to create an electrochemical H+ gradient
across the inner mitochondrial membrane. The electrochemical potential of this gradient is
harnessed to synthesize ATP.
The flow of electrons through Complexes I, III, and IV results in pumping of protons across the
inner mitochondrial membrane, making the matrix alkaline relative to the inter membrane space.
This proton gradient provides the energy (in the form of the proton-motive force) for ATP
synthesis from ADP and Pi by proton-translocating ATP synthase (also known as (F1F0 –
ATPase, Complex V, F-type H + – ATPase).
Structure of Proton-translocating ATP synthase
Consists of two major substructures comprising 8 to 13 different subunits. Comprises two
functional units, F0 and F1 . F0 is a water-insoluble integral protein that contains proton
translocation channel. F1 is a water-soluble peripheral membrane protein. F1 has nine subunits of
five different types, with the composition 3β3γ. Three  and three β subunits are arranged like the
segments of an orange, with alternating subunits around a central shaft, the γ subunit. Each of the
three β subunits has one catalytic site for ATP synthesis. The amino acid sequences of the three β
subunits are identical but their conformations differ.
The F0 complex making up the proton pore is composed of three subunits, a, b, and c, in the
proportion a b 2 c 10-12 . The two b subunits of F 0 associate firmly with the  and β subunits of F1,
holding them fixed relative to the membrane. Subunit c is small, hydrophobic polypeptide,
consisting almost entirely of two transmembrane helices. The c subunits is attached to the shaft
made up of F1 subunits γ and δ.
Synthesis of ATP on the enzyme surface
In the reaction catalyzed by ATP synthase release of ATP from the enzyme is the major energy
barrier. The free-energy change for the formation of ATP from ADP and Pi in aqueous solution
is large and positive. On the enzyme surface, the very tight binding of ATP provides sufficient
binding energy to bring the free energy of the enzyme-bound ATP close to that of ADP + P i , so

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the reaction is readily reversible. The free energy required for the release of ATP is provided by
the proton-motive force.
Energy-dependent binding change mechanism for ATP synthesis by proton-translocating
ATP synthase
F 1 has three chemically identical but conformationally distinct interacting protomers: O, the
open conformation, has very low affinity for ligands and is catalytically inactive; L has loose
binding for ligands and is catalytically inactive; T has tight binding for ligands and is
catalytically active.

Uncoupling of Oxidative Phosphorylation

The presence in the inner mitochondrial membrane of an agent that renders it permeable to H+
uncouples oxidative phosphorylation from electron transport by providing a route for the
dissipation of the proton-motive force that does not require ATP synthesis. Uncoupling therefore
allows electron transport to proceed unchecked even when ATP synthesis is inhibited. 2,4-
dinitrophenol (DNP) and carbonylcyanide-p-trifluoro methoxy phenyl hydrazone (FCCP), have
been found to “uncouple” these processes.
Uncoupling in Brown Adipose
Tissue Functions to Generate
Heat
The dissipation of an
electrochemical H+ gradient,
which is generated by electron
transport and uncoupled from
ATP synthesis, produces heat.
Heat generation is the
physiological function of brown
adipose tissue. It contains
numerous mitochondria whose
cytochromes color is brown.
New-born mammals that lack fur, contain brown fat in their neck and upper back that
functions as a “biological heating pad.” These mitochondria contain the protein thermogenin
[also called uncoupling protein (UCP)].

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