Bioenergetics

Bioenergetics
The transfer and utilization of energy in biologic systems is called bioenergetics. It makes use of a few
basic ideas from the field of thermodynamics, particularly the concept of free energy which provides a
measure of the energetic feasibility of a chemical reaction. It allows us to predict whether a reaction or
process can take place. Bioenergetics concerns only the initial and final energy states of reaction
components, not the mechanism or how much time is needed for the chemical change to take place (the
rate). In short, bioenergetics predicts if a process is possible, whereas kinetics measures how fast the
reaction occurs. (refer to PowerPoint presentations
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 forms, 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
(ETC). The coupling of electron transport with ATP synthesis is
called oxidative phosphorylation. It proceeds continuously in all
tissues that contain mitochondria.
ETC is located in the inner mitochondrial membrane and is the

final common pathway by which electrons derived from different
fuels of the body flow to oxygen (O2). The mitochondrion contains
an outer and an inner membrane separated by the intermembrane
space. Although the outer membrane contains special channels
(formed by the protein porin), making it freely permeable to most
ions and small molecules, the inner membrane is a specialized
structure that is impermeable to most small ions, including protons
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. The inner mitochondrial
membrane is unusually rich in protein, over half of which is
directly involved in oxidative phosphorylation. It also is highly
convoluted. The convolutions, called cristae, serve to greatly
increase the surface area of the inner membrane.
The matrix of the mitochondria is a gel-like solution, rich in

protein including the enzymes responsible for the oxidation of
pyruvate, amino acids, and fatty acids (by β-oxidation) as well as
those of the tricarboxylic acid (TCA) cycle. The synthesis of
glucose, urea, and heme occurs partially in the matrix of
mitochondria. In addition, the matrix contains NAD+ and FAD
(the oxidized forms of the two coenzymes that are required as
hydrogen acceptors), and ADP and Pi, which are used to produce
ATP. DNA (mtDNA) and RNA (mtRNA) and ribosomes are also
found in the mitochondria.
The inner mitochondrial membrane contains five separate protein complexes, called Complexes I, II, III,
IV, and V. Complexes I–IV each contain part of the ETC. These complexes accept or donate electrons to
the relatively mobile electron carriers, coenzyme Q and cytochrome c. Each carrier in the ETC can receive
electrons from an electron donor and can subsequently donate electrons to the next acceptor in the chain.
The electrons ultimately combine with O2 and protons to form water. This requirement for O2 makes the
electron transport process the respiratory chain, which accounts for the greatest portion of the body’s use
of O2.
With the exception of coenzyme Q, which is a lipid-soluble quinone, all members of this chain are
proteins. These may function as enzymes as is the case with the flavin-containing dehydrogenases, may
contain iron as part of an iron-sulfur center, may contain iron as part of the porphyrin prosthetic group of
heme as in the cytochromes, or may contain copper as does the cytochrome a + a3 complex.
1. Formation of NADH: NAD+ is reduced to NADH by dehydrogenases that remove two hydrogen
atoms from their substrate. Both electrons but only one proton (that is, a hydride ion [:H–]) are
transferred to the NAD+, forming NADH plus a free proton.
2. NADH dehydrogenase: The free proton plus the hydride ion carried by NADH are transferred to
NADH dehydrogenase, a protein complex (Complex I) embedded in the inner mitochondrial
membrane. Complex I has a tightly bound molecule of flavin mononucleotide (FMN), a coenzyme
structurally related to FAD that accepts the two hydrogen atoms (2e– + 2H+), becoming FMNH2.
NADH dehydrogenase also contains peptide subunits with iron-sulfur centers. At Complex I, electrons
move from NADH to FMN to the iron of the iron-sulfur centers and then to coenzyme Q. As electrons
flow, they lose energy. This energy is used to pump protons across the inner mitochondrial membrane,
from the matrix to the intermembrane space.
3. Succinate dehydrogenase: At Complex II, electrons from the succinate dehydrogenase–catalyzed

oxidation of succinate to fumarate move from the coenzyme, FADH2, to an iron-sulfur protein, and
then to coenzyme Q. no protons are pumped at Complex II because no energy is lost in this process.
4. Coenzyme Q: Coenzyme Q (CoQ) is a quinone derivative with a long, hydrophobic isoprenoid tail.
CoQ is a mobile electron carrier and can accept hydrogen atoms from NADH dehydrogenase
(Complex I), from succinate dehydrogenase (Complex II), and from other mitochondrial
dehydrogenases. CoQ transfers electrons to Complex III (cytochrome bc1). CoQ, then, links the
flavoprotein dehydrogenases to the cytochromes.
5. Cytochromes: The remaining members of the ETC are cytochrome proteins. 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
an acceptor and donor of electrons. Electrons are passed along the chain from cytochrome bc1
(Complex III), to cytochrome c, and then to cytochromes a + a3 (Complex IV). As electrons flow,
protons are pumped across the inner mitochondrial membrane at Complexes III and IV. Also
cytochrome c is a mobile carrier of electrons.
Electron transport chain. The flow of electrons is shown by the arrows.
Cytochrome a + a3: This cytochrome complex (Complex IV) is the only electron carrier in which the heme
iron has an available coordination site that can react directly with O2 and so also is called cytochrome
oxidase. At Complex IV, the transported electrons, O2, and free protons are brought together, and O2 is
reduced to water. Four electrons are required to reduce one molecule of O2 to two molecules of water.
Cytochrome oxidase contains copper (Cu) atoms that are required for this complicated reaction to occur.
Electrons move from CuA to cytochrome a to cytochrome a3 (in association with CuB) to O2.
Note: 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.
The free energy released as electrons are transferred along the ETC from an electron donor (reducing
agent or reductant) to an electron acceptor (oxidizing agent or oxidant) is used to pump protons at
Complexes I, III, and IV. The electrons can be transferred as hydride ions (:H–) to NAD+; as hydrogen
atoms (•H) to FMN, CoQ, and FAD; or as electrons (e–) to cytochromes. The ΔGo for the phosphorylation
of ADP to ATP is +7.3 kcal/mol. The transport of a pair of electrons from NADH to O2 through the ETC
releases 52.58 kcal. Therefore, more than sufficient energy is available to produce 3 ATP from 3 ADP
and 3 Pi (3 × 7.3 = 21.9 kcal/mol). For FADH2 is 2 ATP made per O atom reduced because Complex I is
bypassed.
Phosphorylation of ADP to ATP

The transfer of electrons down the ETC is energetically favored because NADH is a strong electron donor
and O2 is an avid electron acceptor. However, the flow of electrons does not directly result in ATP
synthesis.
Proton pump: Electron transport is coupled to the phosphorylation of ADP by the pumping of protons
across the inner mitochondrial membrane, from the matrix to the intermembrane space, at Complexes I,
III, and IV. This process creates an electrical gradient (with more positive charges on the outside of the
membrane than on the inside) and a pH gradient (the outside of the membrane is at a lower pH than the
inside). The energy generated by this proton gradient is sufficient to drive ATP synthesis. Thus, the proton
gradient serves as the common intermediate that couples oxidation to phosphorylation.
ATP synthase: The multisubunit enzyme ATP synthase (Complex V) synthesizes ATP using the energy
of the proton gradient. It contains a domain (Fo) that spans the inner mitochondrial membrane, and an
extramembranous domain (F1) that appears as a sphere that protrudes into the mitochondrial matrix.
Electron transport chain shown in association with the transport of protons (H+). A total of ten H+ are
pumped for each nicotinamide adenine dinucleotide (NADH) oxidized. H+ are not pumped at Complex
II.
[Notes from: Ferrier, D. R. (2014). Biochemistry (Lippincott Illustrated Reviews Series). Biochemistry
(Lippincott Illustrated Reviews Series).]

Bioenergetics

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Bioenergetics

Electron Transport Chain

Energy-rich molecules, such as glucose, are metabolized by a

ETC is located in the inner mitochondrial membrane and is the

The matrix of the mitochondria is a gel-like solution, rich in

3. Succinate dehydrogenase: At Complex II, electrons from the succinate dehydrogenase–catalyzed

Phosphorylation of ADP to ATP

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