energy compounds

ATP
entities NADH
molecules NADPH

FreeEnergy hydrolysis of ATP 7.3k

currents
energy ofthe cell
Dr. Mohannad Jazzar glucose highly
fak insoluble solublein
Hebron University
hydrophobia groups
hydrophilic rty
 Biochemicty siena field
• Bioenergetics : The quantitative study of energy extraction

transductions in living cells and the physical-chemical nature

underlying these processes.
• It’s a branch of biochemistry concerned with transformation of
energy and use of enzymes by living system

sharing p
The Flow of Electrons Provides Energy for Organisms

Autotrophes

Heterotrophes

All these reactions involving electron flow

are oxidation- reduction reactions
radiations O I II resources a gig
sun solar energy

riffing photosynthesis chloroplast plastids green

leaves's It ain't
 LAWS OF THERMODYNAMICS
4414401
We need to understand System, Heat, and Work

be Cx̅ 41
FIRST LAW (Law of conservation of energy)
Energy cant be created nor destroyed but changed from one form to other
said
The total E leave the system Tim
É9= Total E enters He
the system – stored internal E

In biological recation inside cell System: IKI I I I

091 systems sp
We are interested in Enthaply H
ithat content
ΔH = H product – H reactants ariigeinai.imEg

Exothermic Or Endothermic surrounding v1 system st

ab
far limits universe
to win gaga
maximumlimit f
 LAWS OF THERMODYNAMICS
irriversable
entropy
SECOND LAW (The equilibrium constant is a measure of Directionality)

the total amount of energy is de aligning with time

ΔG: calculate how far from equilibrium a reaction lies under specific
conditions and how much energy will be released to reach
equilibrium K
standard Ñ C
PH 7
ma
pI j
ΔG under specific standard conditions

standard I 81

Imo glue 686 Kical

Keq = 1
MIND
273 Kkal
µ
 LAWS OF THERMODYNAMICS

We need to understand System, Heat, and Work

SECOND LAW (Law of thermodynamic spontaneity, Possibility)

1-Physical chemical changes give useful energy undergo irreversible degradation into a
random form called entropy
2- total amount of energy in this universe declines with time

Heat content
Enthalpy H (The total energy of a system) is equal to:
Free energy G (The usable energy) + entropy S (the unusable energy).

∆G = ∆H – T∆S
12
7
b
Exergonic OR endergonic entropy
If
When ΔH is highly negative and ΔS is highly positive… IS
This reaction is Favorable
11 gas
 LAWS OF THERMODYNAMICS

Keq > 1 .... ΔG has negative value .... Reaction goes spontaneoslay to
the right (Forward)
A+ B --------------------C+D

Keq < 1 .... ΔG has positive value .... Reaction goes spontaneoslay to
the left (Reverse)
 ENERGY

Useful Useless [Entropy]

Free energy can do work at constant P, T Heat Energy do work at

constant P, varying T
this impossible in livings
 IF Entropy
614 Its Entropy Ia
• Degree of randomness and disorderness
• Change within………to explain this follow the
following examples
• Tea kettle
• Glucose oxidation
Glucose + 6O2 6CO2 + 6H2O
in
• Information entropy iq
interacting molecules 12 s liq
no of
7
1 gtroPYob.it I
 nd
Aspects of 2 Law
1. We must know system, surrounding, and universe
system
2. Standard state in which pH=7, T=298K, Concentration=1M, Atm.P=1
Energy pressure
volume
3. Enthalpy H=E+PV , enthalpy means warm within, or heat content , Surrounding
E=internal energy, PV pressure times volume.
Universe
4. Change in free energy is given by ΔG = ΔH - TΔS
that is change in free energy ,enthalpy and entropy respectively
5. When chemical reaction proceeds toward equilibrium then:
S increased and ΔS positive
ΔG decreased or negative
● ΔH negative ( when system looses heat), and positive when system absorbs heat

Tamara
Étudens loving
Nucleophiles: fi f
functional groups
rich in electrons and
capable of donating
them
Electrophiles:
electron-deficient
functional groups
that seek electrons

The relative
electronegativities:
F>O>N>C=S>P=H
E A
 50 50
Et

Cleavage of a C-C or C-H bond Hz H 16

Gbe 54 highlyelectronegative os.ie

IN
IT
He I
H At
hydride
proton

1 1
 Equilibrium Constants and
Standard Free-Energy Change
• For the reaction: aA + bB cC + dD

ΔGreaction = ΔGo’reaction + RT ln([C]c[D]d/[A]a[B]b)

• At equilibrium: Keq = [C][D]/[A][B] and

ΔGreaction = 0, so that:
mph
ΔGo’reaction = -RT ln Keq
gas constant
The standard free-energy change is directly related to
the equilibrium constant
Standard free-energy changes are
additive IGI.fi

13.8 30.5
Equilibrium constants are
multiplicative
ATP
 Phosphagens: Energy-rich storage molecules
631 3455 in animal muscle

•Phosphocreatine (PC) and phosphoarginine (PA)

are phosphoamides
•Have higher group-transfer potentials than ATP
•Produced in muscle during times of ample ATP
•Used to replenish ATP when needed via creatine
kinase reaction
 It 941
Fire flashes: glowing reports of ATP
• From chemical energy into light
energy.
• An pyrophosphate cleavage of ATP
to form luciferyl adenylate. In the
presence of O2 and luciferase, the
luciferin undergoes a multiple step
oxidative decarboxylation to
oxyluciferin and accompanied by
remission of light.
ciferaseenzyme I
 Equilibrium Constants and
Actual Free-Energy Change
For real-life situation in cell biology we will use the ΔG’

• For the reaction: aA + bB cC + dD

ΔG’ = ΔGo’ + RT ln ([C]c[D]d/[A]a[B]b)

Is a function of reactant and product concentrations and of the tempreture

The actual free energy of ATP hydrolysis is very diffrent

Phosphorylation potential
 Reaction coupling

ΔG1 = 13.8 kJ/mol and ΔG2 = -30.5 kJ/mol

 Chemical logic and common biochemical Reactions

Cells have the capacity to carry out thousands of specific (Enzyme catalyzed reactions)
On the enzyme active sites (Breaking and Forming of the new bonds)
metabolism 6

✔Reactions in living cells includes: Entities

- Oxidation-reduction (Dehydrogenases)
- Group transfer reactions (Kinases)
- H2O addition/removal (Hydrolases)
- Formation double bond (Lyases)
- Isomerization (Isomerases)
- Make and break C-C bonds (Ligases)
we
39933
 Cells need energy to do all their biological work

• To generate and maintain its highly ordered structure

(biosynthesis of macromolecules).

ATP
• To generate motion (mechanical work).

• To generate concentration and electrical gradients

movement
across cell membranes (active transport). meshanicalmaterial
ATP 26
I transfer of
M.itikfueta
• To generate heat and light.
passivetransport 24
simplediffusion
kings Ion
K.FI The Free Energy of ATP
• Energy from oxidation of metabolic fuels is
largely recovered in the form of ATP
hogxcavrenc StrustumLATW phoip

high-energy
phosphoanhydride c
bonds

Charge repulsion
Resonance stabilization
High Entropy adenine
Rhibiseanger
ATP
highelectronegativity I
Highrepultion L
4 6 Highlyunstablecompound
e
Exothermic fit
winorgani phosphate AAP 65,1 Hydrolysis2.34 off
 in ADP Is ATP twi
we
Hydrolysis of phosphoenolpyruvate (PEP)

III

in tonegativity

alloholform
he stable
Ii its a Tatomenform
ls.TW
• Catalyzed by pyruvate kinase, this reaction is followed by
spontaneous tautomerization of the product.
Pyruvate, tautomerization is not possible in PEP, and thus the
products of hydrolysis are stabilized relative to reactants.

Resonance stabilization Tomer

 Phosphagens: Energy-rich storage molecules
in animal muscle
Resonaca stabilization
•High-energy phosphate compound
•Phosphocreatine (PC) and phosphoarginine (PA)
•Have higher group-transfer potentials than ATP
•Produced in muscle during times of ample ATP
•Used to replenish ATP when needed via
Creatine and arginine kinase reaction

ATP hydrolesis inside our Body I enzyme action

 Phosphoryl-Group Transfer
•Phosphoryl-group-transfer potential - the ability
of a compound to transfer its phosphoryl group
•Energy-rich or high-energy compounds have
group transfer potentials equal to or greater than
that of ATP
• Low-energy compounds have group transfer
potentials less than that of ATP
Phosphoryl-Group Transfer
Larg free enrgy change that company ATP hydrolysis
High-energy phospahte compound

1 cal = 4.184 J
act
 potential engine
ATP provides energy by group transfers, Not by
posphately
simple hydrolysis --- in two steps
• A phosphoryl group is first
enzymatin Reaction transferred from ATP to
glutamate
• The phosphoryl group is
Glutamine
displaced by NH3 and
synthase
released as Pi

• ATP can carry energy from

high-energy phosphate
compounds produced by
catabolism to compounds
such as glucose,
converting them into
more active forms

I am
step I s
two steps
enzymephosphate 4 glutamylgroupit e
g i
Ps M 1
Nucleophilic displacement reaction of ATP

water ATP I a insisted

Thioesters---Hydrolysis of
acetyl-coenzyme A
• Acetyl-CoA is a
thioester with a large,
negative, standard free
energy of hydrolysis.

• Thioesters contain a
sulfur atom in the
position occupied by an
oxygen atom in oxygen
esters.
NADH and NADPH act with dehydrogenases as soluble
electron carriers

• From vitamin niacin (source of

redused the nicotinamide)
NA 9b
oxidized
Nap • NADH absorb at 340 nm.
Hases substrate a
• Most dehydrogenase that use
larrier NAD or NADP bind the cofactor
electron
dinucleotidein the conserved protein
adenin
amide domain
nicotine

is

Kidized

spectral light
 Vit-B3

VB water soluble vitamin

j istial A A
oxidized
reducedboidation Reduction
II insipid
What are the effects of Niacin Deficiency ?
 disorder
skin desese
if ftp.T

Dermatitis
ix IT Diarrhea
Dementia
is death

disease of four dies

Y
V83 niacin
Structure of oxidized and reduced FAD
and FMN

Reduced
2H 4 oxidizedand
1 Redox Rna
• Flavin Nucleotides are tightly
bound in flavoproteins. Accepts 1
or 2 electrons