2. These energy transformations can be
• divided into three principal phases:
• (1) oxidation of fuels (fat, carbohydrate,
and protein),
• (2) conversion of energy from fuel oxidation
into the high energy phosphate bonds of ATP
• (3) utilization of ATP phosphate bond energy
to drive energy-requiring processes.
4. Bioenergetics refers to cellular energy
transformations.
• The ATP-ADP cycle. In cells, the chemical bond energy
of fuels is transformed into the physiologic responses
necessary for life. The central role of the high-energy
phosphate bonds of ATP in these processes is
summarized in the ATP-ADP cycle . To generate ATP
through cellular respiration, fuels are degraded by
oxidative reactions that transfer most of their chemical
bond energy to NAD and FAD to generate the reduced
form of these coenzymes, NADH and FAD(2H). When
NADH and FAD(2H) are oxidized by O2 in the electron
transport chain, the energy is used to regenerate ATP in
the process of oxidative phosphorylation.
5.
6. Use of ATP
• Energy available from cleavage of the high-energy
phosphate
• bonds of ATP can be used directly for
• mechanical work (e.g., muscle contraction)
• transport work (e.g., a Na gradient generated by Na, K-
• ATPase). It can also be used for
• biochemical work (energy-requiring chemical reactions),
such as anabolic pathways (biosynthesis of large molecules
like proteins) or detoxification reactions. Phosphoryl
transfer reactions, protein conformational changes, and
the formation of activated intermediates containing high
energy bonds (e.g., UDP-sugars) facilitate these energy
transformations.
7. • Bioenergetics describes the transfer and utilization of
energy in biologic systems. It uses the concept of free
energy.
• Changes in free energy (ΔG) provide a measure of the
energetic feasibility of a chemical reaction and therefore
allow prediction of whether a reaction or process can
take place.
• The change in free energy is represented in two ways,
ΔG and ΔGo
• ΔG (without the superscript “o”), represents the change
in free energy and the direction of a reaction at any
specified concentration of products and reactants. ΔG,
then, is a variable.
• ΔGo(with the superscript “o”), represent the energy
change when reactants and products are at a
concentration of 1 mol/L.
8. The change in free energy, ΔG, can be used to
predict the direction of a reaction at constant
temperature and pressure.
• If ΔG is a negative number, there is a net loss of
energy, and the reaction goes spontaneously
(exergonic) i.e
A B
• If ΔG is a positive number, there is a net gain of
energy, and the reaction does not go
spontaneously from B to A. Energy must be
added to the system to make the reaction go
from B to A (endergonic)
• If ΔG = 0, the reactants are in equilibrium.
9.
10. • The free energy of the forward reaction (A → B) is
equal in magnitude but opposite in sign to that of the
back reaction.
• The ΔG of the reaction A → B depends on the
concentration of the reactant and product. At constant
temperature and pressure, the following relationship
can be derived
• ΔG = ΔGo + RT ln [B]
[A]
ΔGo is the standard free energy change
R is the gas constant (1.987 cal/mol . degree)
T is the absolute temperature.
[A] and [B] are the actual concentrations of the
reactant and product.
Ln represents the natural logarithm.
11. laws of thermodynamics
• First law of thermodynamics, the conservation
of energy: In any physical or chemical
• change, the total energy of a system, including
its surroundings, remains constant.
• Second law of thermodynamics: The universe
tends toward disorder. In all natural processes,
the total entropy of a system always increases.
• S Change in entropy, or increase in disorder
• G= H-T S h internal energy s
• G0 RTln K eq
13. Membranes of the mitochondrion:
The components of the electron transport chain are
located in the inner mitochondrial membrane.
Although the outer membrane contains special pores,
making it freely permeable to most ions and small
molecules,
the inner mitochondrial membrane is a specialized
structure that is impermeable to most small ions,
including H+, Na+, and K+, and small molecules such
as ATP, ADP, pyruvate, and other metabolites
important to mitochondrial function.
Specialized carriers or transport systems are required to
move ions or molecules across this membrane.
14. ELECTRON TRANSPORT CHAIN
Energy-rich molecules, such as glucose, are
metabolized by a series of oxidation reactions
ultimately yielding CO2 and water .The
metabolic intermediates of these reactions
donate electrons to specific coenzymes—
nicotinamide adenine dinucleotide (NAD+) and
flavin adenine dinucleotide (FAD)—to form the
energy-rich reduced coenzymes, NADH and
FADH2. These reduced coenzymes can, in turn,
each donate a pair of electrons to a specialized
set of electron carriers, collectively called the
electron transport chain.
15. Matrix of the mitochondrion:
This gel-like solution in the interior of
mitochondria is 50% protein which include the
enzymes responsible for the
oxidation of pyruvate, amino acids, fatty acids
(by β-oxidation), and those of the
tricarboxylic acid (TCA) cycle. The synthesis of
glucose, urea, and heme occur partially in the
matrix of mitochondria.
16. Organization of the electron transport chain
The inner mitochondrial membrane can be disrupted
into five separate protein complexes, called
Complexes I, II, III, IV, and V.
Complexes I–IV, each complex accepts or donates
electrons to relatively mobile electron carriers, such
as coenzyme Q and cytochrome c. Each carrier in the
electron transport chain can receive electrons from an
electron donor, and can subsequently donate electrons
to the next carrier in the chain. The electrons
ultimately combine with oxygen and protons to form
water. This requirement for oxygen makes the electron
transport process the respiratory chain, which accounts
for the greatest portion of the body’s use of oxygen.
Complex V catalyzes ATP synthesis and so is referred to
as ATP synthase
17. Reactions of the electron transport chain
1. Formation of NADH
NAD+ is reduced to NADH by dehydrogenases
that remove two hydrogen atoms from their
substrate. (e.g the dehydrogenases found in the
TCA cycle) forming NADH plus a free proton, H+.
18. 2. NADH dehydrogenase:
The free proton plus the hydride ion carried by
NADH are next transferred to NADH
dehydrogenase, a protein complex (Complex I)
embedded in the inner mitochondrial membrane.
Complex I has a tightly bound molecule of flavin
mono nucleotide (FMN, a coenzyme structurally
related to FAD, that accepts the two hydrogen
atoms (2e– + 2H+), becoming FMNH2.
NADH dehydrogenase also contains iron atoms
paired with sulfur atoms to make iron–sulfur
centers. These are necessary for the transfer of
the hydrogen atoms to the next member of the
chain, coenzyme Q (ubiquinone).
19. Coenzyme Q:
Coenzyme Q (CoQ) is also called ubiquinone.
CoQ is a mobile carrier and can accept
hydrogen atoms both from FMNH2, on NADH
dehydrogenase (Complex I), and from FADH2,
produced on succinate dehydrogenase
(Complex II).
CoQ transfers electrons to Complex III. CoQ,
then, links the flavoproteins to the
cytochromes.
20. Cytochromes:
The remaining members of the electron
transport chain are cytochromes. Each
contains a heme group (a porphyrin ring plus
iron). Unlike the heme groups of hemoglobin,
the cytochrome iron is reversibly converted
from its ferric (Fe3+) to its ferrous (Fe2+) form
as a normal part of its function as a reversible
carrier of electrons. Electrons are passed
along the chain from CoQ to cytochromes bc1
(Complex III), and cytochrome a + a3 (Complex
IV).
21. Cytochrome a + a3:
This cytochrome complex is also called as
cytochrome oxidase. At this site, the
transported electrons, O2, and free protons
are brought together, and O2 is reduced to
water .Cytochrome oxidase contains copper
atoms that are required for this complex
reaction to occur.
22. • Inhibition of electron transport inhibits ATP
synthesis because these processes are tightly
coupled.
Incomplete reduction of oxygen to water
produces reactive oxygen species (ROS), such
as superoxide (O2),hydrogen peroxide (H2O2)
and hydroxyl radicals (OH•). ROS damage DNA
and proteins, and cause lipid peroxidation.
Enzymes such as superoxide dismutase (SOD),
catalase, and glutathione peroxidase are
cellular defenses against ROS.
23. Release of free energy during electron
transport
Free energy is released as electrons are
transferred along the electron transport chain
from an electron donor (oxidation) to an
electron acceptor (reduction).
The electrons can be transferred as hydride
ions (:H–) to NAD+, as hydrogen atoms (•H)
to FMN, coenzyme Q, and FAD, or as
electrons (e–) to cytochromes.
24. Redox pairs:
Oxidation (loss of electrons) of one compound
is always accompanied by reduction (gain of
electrons) of a second substance. For example,
the oxidation of NADH to NAD+ accompanied
by the reduction of FMN to FMNH2.
NAD+ and NADH form a redox pair, as do FMN
and FMNH2. Redox pairs differ in their
tendency to lose electrons. This tendency is a
characteristic of a particular redox pair, and
can be quantitatively specified by a constant,.
25. ΔGo of ATP:
The standard free energy for the phosphorylation
of ADP to ATP is +7.3 kcal/mol. The transport of a
pair of electrons from NADH to oxygen via the
electron transport chain produces 52.58 kcal.
Therefore, more than sufficient energy is
available to produce three ATP from three ADP
and three Pi (3 x 7.3 = 21.9 kcal/mol), sometimes
expressed as a P:O ratio (ATP made per O atom
reduced) of 3:1. The remaining calories are used
for ancillary reactions or released as heat. [Note:
P:O for FADH2 is 2:1 because Complex I is
bypassed.]
