A Level Biology

ATP

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The structure of ATP
▪ ATP is the universal currency of energy.
▪ It is a nucleotide formed by the following components.
1. A nitrogenous base - adenine
2. Pentose sugar- ribose
3. 3 phosphate groups
▪ Phosphate groups link with ribose in a row.
▪ The two terminal bonds among phosphates act as high energy bonds.
Each of these contain 30.5 kJ·mol−1.
▪ This energy is liberated when ATP is subjected to hydrolysis by enzyme
ATPase.

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ATP as the energy ‘currency’
▪ When a phosphate group is removed
from ATP, adenosine diphosphate
(ADP) is formed and 30.5 kJ·mol−1 of
energy is released.
▪ Removal of a second phosphate
produces adenosine monophosphate
(AMP), and 30.5 kJ·mol−1 of energy Hydrolysis of ATP (Pi is inorganic phosphate,
is again released. H3PO4).
These reactions are all reversible. It is the
▪ Removal of the last phosphate, interconversion of ATP and ADP that is all-
leaving adenosine, releases only 14.2 important in providing energy for the cell:
kJ·mol−1. ATP + H2O ⇋ ADP + H3PO4 ± 30.5kJ

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▪ The rate of interconversion, or turnover, is enormous. It is estimated that a
resting human uses about 40 kg of ATP in 24 hours, but at any one time
contains only about 5 g of ATP. During strenuous exercise, ATP breakdown
may be as such as 0.5 kg per minute.

▪ The cell’s energy yielding reactions are linked to ATP synthesis. The ATP is
then used by the cell in all forms of work. ATP is the universal intermediary
molecule between energy-yielding and energy-requiring reactions used in a
cell, whatever the type of cell.

▪ In other words, ATP is the ‘energy currency’ of the cell. The cell ‘trades’ in
ATP, rather than making use of a number of different intermediates. ATP is
a highly suitable molecule for this role.

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▪ Not only is it readily hydrolysed to release energy, it is also small and water
soluble. This allows it to be readily transported around the cell.

▪ Energy transfers are inefficient. Some energy is converted to thermal

energy whenever energy is transferred. At the different stages in a multi-
step reaction such as respiration, the energy made available may not
perfectly correspond with the energy needed to synthesise ATP.

▪ Any excess energy is converted to thermal energy. Also, many energy-

requiring reactions in cells use less energy than that released by hydrolysis
of ATP to ADP. Again, any extra energy will be released as thermal energy.

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▪ Be careful to distinguish between molecules used as energy currency and
as energy storage.
▪ An energy currency molecule acts as the immediate donor of energy to the
cell’s energy-requiring reactions.
▪ An energy storage molecule is a short-term (glucose or sucrose) or long-
term (glycogen, starch or triglyceride) store of chemical potential energy.

Energy currency of the cell Stores of energy

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Synthesis of ATP
▪ Energy for ATP synthesis can become available in two ways. In respiration,
energy released by reorganising chemical bonds (chemical potential
energy) during glycolysis and Krebs cycle is used to make some ATP.
▪ However, most ATP in cells is generated using electrical potential energy.
This energy is from the transfer of electrons by electron carriers in
mitochondria and chloroplasts.
▪ It is stored as a difference in proton (hydrogen ion) concentration across
some phospholipid membranes in mitochondria and chloroplasts, which
are essentially impermeable to protons.

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▪ Protons are then allowed to flow down their
concentration gradient (by facilitated diffusion)
through a protein that spans the phospholipid
bilayer. Part of this protein acts as an enzyme
that synthesises ATP and is called ATP
synthase.
▪ The transfer of three protons allows the
production of one ATP molecule, provided that
ADP and an inorganic phosphate group (Pi) are
available inside the organelle.
▪ This process occurs in both mitochondria and
chloroplasts. The process was first proposed by
Peter Mitchell in 1961 and is called
chemiosmosis.

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ATP synthase has 3 binding sites and a
part of the molecule (𝜸) that rotates as
hydrogen ions (H+) pass. This produces
structural changes in the binding sites
and allows them to pass sequentially
through 3 phases:

▪ Binding ADP and Pi

▪ Forming tightly bound ATP
▪ Releasing ATP
Transverse section (TS) of ATP synthase
showing its activity.

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