Bioenergetika dan Metabolisme

Bioenergetika dan Termodinamika

l Bioenergetics is the quantitative study of energy

transductions—changes of one form of energy into
another—that occur in living cells, and of the nature and
function of the chemical processes underlying these
transductions.
l Biological Energy Transformations Obey the Laws of
Thermodynamics
Review Termodinamika

l Gibbs free energy, G, expresses the amount of an

energy capable of doing work during a reaction at
constant temperature and pressure.
l Enthalpy, H, is the heat content of the reacting system.
l Entropy, S, is a quantitative expression for the
randomness or disorder in a system

∆G = ∆H – T∆S
Cells Require Sources of Free Energy

l Cells are isothermal systems—they function at essentially

constant temperature (and also function at constant pressure)
l The energy that cells can and must use is free energy,
l Heterotrophic cells acquire free energy from nutrient molecules,
and photosynthetic cells acquire it from absorbed solar radia-
tion.
l Both kinds of cells transform this free energy into ATP and
other energy-rich compounds capable of provid- ing energy for
biological work at constant temperature.
Standard Free-Energy Change Is Directly Related
to the Equilibrium Constant

Untuk reaksi: Contoh:

Calculate the standard free-energy change of the reaction
aA + bB → cC + dD catalyzed by the enzyme phosphoglucomutase
Glucose 1-phosphate <-> glucose 6-phosphate
given that, starting with 20 mM glucose 1-phosphate and no
glucose 6-phosphate, the final equilibrium mixture at 25oC
∆G’0 = -RT ln K’eq and pH 7.0 contains 1.0 mM glucose 1-phosphate and 19
dimana mM glucose 6-phosphate. Does the reaction in the direction
of glucose 6-phosphate formation proceed with a loss or a
gain of free energy?
Ans:
Standard Free-Energy Changes of Some Chemical Reactions
Actual Free-Energy Changes Depend on Reactant
and Product Concentrations

aA + bB → cC + dD
Standard Free-Energy Changes Are Additive

In the case of two sequential chemical

reactions, A <-> B and B <-> C, each
reaction has its own equilibrium constant
and each has its characteristic
standard free-energy change, ∆G’0total =
∆G’01 + ∆G’02

This principle of bioenergetics explains

how a thermo- dynamically unfavorable
(endergonic) reaction can be driven in the
forward direction by coupling it to a highly
exergonic reaction through a common
intermediate.
Standard Free-Energy Changes Are Additive
Phosphoryl GroupTransfers and ATP

The Free-Energy Change for ATP Hydrolysis

Is Large and Negative
The free-energy change for ATP hydrolysis is 230.5 kJ/mol under
standard conditions, but the actual free energy of hydrolysis (DG) of ATP
in living cells is very different: the cellular concentrations of ATP, ADP,
and Pi are not identical and are much lower than the 1.0 M of standard
conditions
Standard Free Energies of Hydrolysis of Some Phosphorylated
Compounds and Acetyl-CoA (a Thioester)

Mengapa ATP yang digunakan

sebagai energy currency dalam
sel ?
ATP Provides Energy by Group Transfers, Not by Simple
Hydrolysis

- ATP participates covalently in the enzyme-catalyzed

reaction to which it contributes free energy.
- ATP hydrolysis is exergonic
- ATP hydrolysis drives metabolism by shifting the
equilibrium of coupled reactions
Metabolisme
Metabolic Pathways Contain Many Recurring Motifs

l Activated Carriers of Electrons for Fuel Oxidation (1)

The reactive part of NAD+ is its nicotinamide ring, a pyridine
derivative synthesized from the vitamin niacin.
Metabolic Pathways Contain Many Recurring Motifs

l Activated Carriers of Electrons for Fuel Oxidation (2)

The reactive part of FAD is its isoalloxazine ring, a derivative
of the vitamin riboflavin (Figure 15.15).
FAD, like NAD+, can accept two electrons. In doing so, FAD,
unlike NAD+, takes up two protons.
Metabolic Pathways Contain Many Recurring Motifs

An Activated Carrier of Electrons for Reductive Biosynthesis

High- potential electrons are required in most biosyntheses because the precursors are more
oxidized than the products.

The electron donor in most reductive biosyntheses is NADPH, the reduced form of nicotinamide
adenine dinucleotide phosphate

NADPH is used almost exclusively for reductive biosyntheses, whereas NADH is used primarily for
the generation of ATP.

The extra phosphoryl group on NADPH is a tag that enables enzymes to distinguish between high-
potential electrons to be used in anabolism and those to be used in catabolism.
Metabolic Pathways Contain Many Recurring Motifs

An Activated Carrier of Two-Carbon Fragments

Coenzyme A, another central molecule in metabolism, is a carrier of acyl groups derived from the
vitamin pantothenate

The terminal sulfhydryl group in CoA is the reactive site

Acyl groups are linked to CoA by thioester bonds

CoA is the acetyl unit; this derivative is called acetyl CoA

Many activated carriers are derived from vitamins

l Almost all the activated

carriers that act as
coenzymes are derived
from vitamins.

l Vitamins are organic

molecules that are needed
in small amounts in the
diets of some higher
animals.
Jenis-jenis reaksi metabolisme
Oxidation–reduction reactions

Oxidation–reduction reactions are essential components of many pathways. Useful energy is

often derived from the oxidation of carbon com- pounds.
Ligation reactions

Ligation reactions form bonds by using free energy from ATP cleavage
Isomerization reactions

Isomerization reactions rearrange particular atoms within a molecule. Their role is often to
prepare the molecule for subsequent reactions such as the oxidation–reduction reactions
Group-transfer reactions

Isomerization reactions rearrange particular atoms within a molecule. Their role is often to
prepare the molecule for subsequent reactions such as the oxidation–reduction reactions
Group-transfer reactions

Group-transfer reactions play a variety of roles. A phosphoryl group is transferred from the
activated phosphoryl-group carrier, ATP, to glucose, the initial step in glycolysis, a key pathway
for extracting energy from glucose. This reaction traps glucose in the cell so that further
catabolism can take place.
Hydrolytic reactions

Hydrolytic reactions cleave bonds by the addition of water. Hydrolysisis a common means
employed to break down large molecules, either to facilitate further metabolism or to reuse
some of the components for biosynthetic purposes.
Addition or removal Functional groups

Functional groups may be added to double bonds to form single bonds or removed from single
bonds to form double bonds. The enzymes that catalyze these types of reaction are classified
as lyases
Metabolic processes are regulated in three principal ways

At the same time, metabolic control must be flexible, to metabolic activity to the
constantly changing external environments of cells.

Metabolism is regulated through control of:

- the amounts of enzymes
The amount of a particular enzyme depends on both its rate of synthesis and its rate of degradation.
The level of many enzymes is adjusted primarily by a change in the rate of transcription of the
genes encoding them
- their catalytic activities
Reversible allosteric control, feedback inhibition, reversible covalent modification, Many reactions in
metabolism are controlled by the energy status of the cell.
- the accessibility of substrates
In eukaryotes, metabolic regulation and flexibility are enhanced by compartmentalization. For example,
fatty acid oxidation takes place in mitochondria, whereas fatty acid synthesis takes place in the
cytoplasm. Compartmentalization segregates opposed reactions. The transfer of substrates from one
compartment of a cell to another (e.g., from the cytoplasm to mitochondria) can serve as a control point.
Metabolic processes are regulated in three principal ways