Chapter 10.
1 ● Nucleoside triphosphate ATP - most
● Metabolism is central to all life commonly used form of cellular
Metabolism that are common to all energy
organisms ● Thermodynamics - energy changes
● Life obeys the law of in collection of matter called system
thermodynamics ● All other matter in the universe is
● The energy cells obtain from their called system
environment is most often conserved Law of Thermodynamics
as a molecule called ATP ● 1st Law - energy can be neither
ATP is used to supply energy created nor destroyed. Total energy
● Oxidation-reduction(redox) reactions of the universe remains
play a critical role in energy constant,redistributed
conservation ● 2nd Law - physical and chemical
● Chemical reactions that occur in processes proceed in such a way
cells are organized in pathways that the randomness or disorder of
● Each reaction of a pathway is the universe increases
catalyzed by an enzyme or a ● Entropy - Measure of Randomness
ribozyme ● Calorie - amt. Of heat energy
Enzyme and ribozyme speedup the needed to raise 1 gram of H20 from
reaction 14.5 to 15.5 degrees celsius
● The functioning of biochemical ● Joules - units of work capable of
pathways is regulated being done
Cellular work and Energy Transfers Free Energy Change predicts the nature
● Do work in order to survive and of a chemical reaction
reproduce ● ^G = ^H - T^S
● Chemical work - synthesis of ● ^G is the change in free energy
biological molecules, energy is ● ^H is the change in enthalpy
needed to increase the molecular ● T is the temperature in Kelvin
complexity of cell (Celsius + 273)
● Transport work - take up nutrients, 10.2
eliminates waste, maintain ion ● ATP - Cells energy currency, high
balances, ions must be transported energy molecule
across cell membranes against an ● ATP serves as link between
electrochemical gradient exergonic and endergonic reactions
● Mechanical work - energy is required ● Adenosine diphosphate and
for cell motility, movement of orthophosphate (P1)
structures such as partitioning ● Energy released is used to power
chromosomes endergonic reactions
● Energy - capacity to do work ● The very negative ^G’ of hydrolysis
● Physical and chemical processes of ATP: ability to transfer a
are results of the application or phosphoryl group to another
movement of energy molecule
● ATP is high phosphate transfer
potential, it readily donates a
phosphoryl group to another NAD+/NADH conjugate redox pair
molecule has a very negative E0 and NADH
● ATP can easily be made by cells can therefore give electrons to many
from ADP using molecules such acceptors, including 02
as phosphoenolpyruvate(PEP). 10.4 ETC: Sets of sequential redox
This mechanism is called substrate- reactions
level phosphorylation ● Reduction of 02 by NADH
● Guanosine 5’ - triphosphate (GTP) ● As glucose is catabolized, it is
supplies energy used during protein oxidized. Many of electrons released
synthesis from glucose are accepted by
● Uridine 5’ - triphosphate - used for NAD+, reducing it to NADH, which
synthesis of peptidoglycan and other transfers the electrons to 02
polysaccharides. ● Electrons are transferred to 02 via a
10.3 Redox Reactions series of electron carriers that are
● Free energy changes are related to organized into a system called
equilibria of all chemical reactions, electron transport chain
including equilibria of oxidation- ● The 1st electron carrier has the most
reduction negative E’0 each successive carrier
● Redox - electrons move from an is slightly less negative
electron donor to an electron ● Carriers direct the electrons to the
acceptor terminal electron acceptor (02)
● Electrons - packets of energy ● This protects the cells, from random
● The more electrons the more nonproductive reductions of other
energy rich the molecule is molecules in the cell
● Glucose can donate up to 24 ● ETC are associated in the plasma
electrons in redox reactions membranes / intracytoplasmic
● Each redox reaction consists of two membranes of bacterial and
half reactions. functions as the archeal cells
electron-donating(oxidation) and ● In eukaryotes they are localized to
electron-accepting(reduction) the internal membranes of
● The acceptor and donor of a half mitochondria and chloroplasts
reaction = conjugate redox pairs ● The electron carriers associated with
● Standard reduction potential (E0) ETC differ in terms of their chemical
- equilibrium constant for a redox nature
half reaction, measure of the ● Nicotinamide adenine dinucleotide
tendency of the donor of a half phosphate (NADPH), which donates
reaction to lose electron electrons to ETC, contain
● E0 are measured in volts, unit of nicotinamide ring that accepts 2
electrical potential or electromotive electrons and one proton from donor
force and a second proton is released
● Conjugate redox pairs area potential ● Flavin adenine dinucleotide (FAD)
source of energy and Flavin mononucleotide (FMN)
● Nicotinamide adenine dinucleotide bears two electrons and two protons
(NAD+) - electron acceptor. The on the complex ring
● Proteins bearing FAD and FMn are ● Many enzymes are composed only
often called flavoproteins of one part. But some have 2 part
● Coenzyme Q (CoQ) / ubiquinone is ● Apoenzyme the protein component
a quinone that transports 2 electrons ● cofactor is the non protein
and 2 protons component, include metal ions and
● Cytochromes and several other organic molecules
carriers use iron atoms to transport ● Holoenzyme=Apoenzyme + cofactor
one electron at a time ● If the cofactor is firmly attached to
● There are several different the apoenzyme it is a prosthetic
Cytochromes, each consisting of a group
protein and an iron-porphyrin ring. ● If the cofactor is loosely attached,
● Some iron containing electron- dissociate after product is formed it
carrying proteins lack a heme group is called coenzyme
and are called nonheme iron How enzymes speed up reactions
proteins. Often referred to as iron- ● If a reaction is endergonic, presence
sulfur proteins because the iron is of enzyme will not shift its
associated with sulfur atoms. Four S equilibrium so that more products
atom and 2 Fe atoms are formed
● Ferredoxin is an FE-S Protein active ● Activation Energy: required to bring
in synthesis related electron the reacting molecules together in
transport. Carry one electron at a the correct way to reach the
time transition state
10.5: Biochemical Pathway ● Enzymes accelerate reactions by
● Organism carry out a myriad of lowering the activation energy, more
chemical reactions, products are substrate molecules will have
called metabolites sufficient energy to come together
● Reactions are organized into and form products
biochemical pathways ● Enzymes bring substrates together
● Metabolite Flux: rate of turnover of a at a specific location called
metabolite. Used as a measure of active/catalytic site to form an
pathway activity and to understand enzyme-substrate complex
metabolic networks ● Induced fit model: enzyme changes
10.6: Enzymes and Ribozymes speed up shape when it binds the substrate so
cellular chemical reactions that the active site surrounds and
● Most of these catalysts are proteins precisely fits the substrate.
called Enzymes Hexokinase
● Other catalyst are RNA molecules ● Enzymes binds so that it is correctly
termed Ribozyme oriented. Orientation lowers the
Enzyme Structure amount of energy that the
● Catalyst: a substance that increases substrates required to reach the
the rate of a chemical reaction transition state
● Reacting molecules are called Substrate concentration affects enzyme
substrates activity
● Substances formed are products
● Enzyme activity varies in response ● Noncompetitive inhibitors - affect
to substrate concentrations enzyme activity by binding to the
● At very low substrate concentrations, enzyme at some location other than
enzyme binds substrates more often the active site
● Michaelis constant(Km) substrate ● Alters enzyme shape, rendering it
concentrations required for the inactive or less active
enzyme to achieve half-maximal ● Heavy metals such as mercury
velocity, is used to measure of the frequently are noncompetitive
apparent affinity of an enzyme for its inhibitors of enzyme
substrate Ribozymes: Catalytic RNA Molecules
● The lower the Km the lower the ● RNA Molecules also can catalyze
substrate concentration At which an reactions
enzyme catalyzes its reaction ● Ribozymes-Catalytic RNA molecules
● Enzymes with a low Km are said ● Ribozyme is located in ribosomes
to have a high affinity for their and is responsible for catalyzing
substrates. peptide bond formation between
● Enzymes with lower Km value are amino acids during protein synthesis
able to function better ● Best studied ribozyme cut
Enzyme denaturation destroys enzyme themselves and then join segments
activity of themselves back together
● Enzyme activity is also changed by 10.7 Metabolism must be Regulated to
alterations in pH and temperature maintain homeostasis and prevent waste
● When ph Deviates too greatly from
an enzyme's optimum,activity slows Metabolic pathways can be regulated in
and the enzyme may be damaged three major ways:
● If the temperature rises too much, 1. Metabolic Channeling
structures, enzyme structures will be 2. Regulation of Synthesis
disrupted (regulation of gene
● Bacteria and archaea grow best at Expression)
high temperature 3. Direct stimulation or inhibition
Enzyme Inhibition of the activity of the critical
● Most potent poisons are enzyme enzymes (posttranslational
inhibitors regulation)
● Competitive inhibitor : directly ● Cells often use multiple regulatory
competes with substrate at an approaches to coordinate their
enzyme’s catalytic site and prevents complex metabolic activities
the enzyme from forming a product ● Metabolic Channeling influences
● Resemble normal substrates but pathway activity by localizing
they cannot be converted to metabolites and enzymes into
substrates different parts of the cell
● p-aminobenzoate(PABA) - molecule ● One of the most common metabolic
used in the formation of the channeling mechanisms is
coenzyme folic acid compartmentation
● The differential distribution of
enzymes and metabolites among
separate cell structures or
organelles. It is particularly important
in Eukaryotes
● Regulation of Gene Expression -
Transcription and translation Rates
are altered to control the amount of
an enzyme present in the cell
● Posttranslational Regulation of
Enzyme Activity - in contrast to
regulation of gene expression, the
direct stimulation or inhibition of the
activity of critical enzymes rapidly
alters pathway activity
