BIONERGÉTICA

Laura Emilia Cerón

Departamento de Química
Facultad de Ciencias Básicas y Aplicadas
Universidad Militar Nueva Granada
Las células tienen capacidad de aprovechar la energía y
canalizarla hacia el trabajo biológico para mantenerse
con vida, crecer y reproducirse.

La energía química (alimentos/ ATP) para llevar a cabo

la síntesis de macromoléculas complejas, altamente
ordenadas a partir de precursores simples.
Antoine Lavoisier reconoció
que los animales de alguna
manera transforman
combustibles químicos
(alimentos) en calor y que el
proceso de respiración es
esencial para la vida
Notable variedad de transducciones de energía, conversiones
de una forma de energía a otra, dichas conversiones de
energía son vitales para los organismos y están reguladas
por dos leyes de la termodinámica
Termodinámica
estudia los
cambios de
energía que
acompañan los
eventos en el
Universo
La primera ley es el principio de la conservación de la
energía: para cualquier cambio físico o químico, la
cantidad total de energía en el universo permanece
constante;

La segunda ley de la termodinámica, el universo siempre

tiende hacia un desorden creciente: en todos los procesos
naturales, la entropía del universo aumenta.
 doing work during a reaction at
e.
thalpy,
tureReaccionesand
and entropy
pressure.
que aprovechan, almacenan,are
When related
transfieren
a reac- to
y liberan la energíaeach
absorbida por los organismos (Sis. Reactante) de su entorno.
ly
ontentby
h the releasethe equation
of the reacting of free energy (that
Energía libre de Gibbs: G
variación total de E que es capaz

emand
er ¢Gchanges
5 kinds
¢H 2 soTchemi-
of as to possess
¢S less
de efectuar un trabajo durante una
reacción a P y T cte. (13–1)
nd products. When a
Variación de la E
free-energy change, DG, has a
+ endergónico
he Alrededores
change in Gibbs free energy of the
- exergónico
at,the
d it isreaction
said to be is exo-
said to be J/molexer-
is the
DHEntalpía change in enthalpy of the sys-
Cal/mol
f
onicthe products
reactions, isthe less
H contenido calórico de un sistema
system
Entropía S azar desorden
sistema gains
del

bsolute+ endotérmico
temperature, and DS is the
+ entropía crece
d DH -has, by conven-
yGofisthe positive.
exotérmico
system. By convention, J/mol*K
J/mol Cal/mol DS has
ing systems that take
 nt temperature and pressure. When a reac-
oceeds with the release ¢Gof5 free¢Henergy T ¢S
2 (that
n the system changes so as to possess less
nergy), theenergéticamente
Proceso free-energy favorable
change,- DG, hasEspontaneo
a
h DG is the change in Gibbs free energy
e value and the reaction is said to be exer-
Los organismos preservan su orden interno al tomar de los alrededores energía
In endergonic reactions,
nutrientes o the system gains
system, DH is the change in enthalpy of th
libre en forma de
ergycantidad
and DG isde
igual positive.
luz solar y regresar
energía: calor y la entropía
a sus alrededores una

is Elcalor
lpy, the
H,flujo
isdethe absolute
calor no escontent
heat una fuenteof
no produzca un trabajo
temperature,
de energía
the and
para las células, mientras
reacting el DS
. It reflects the number and kinds of chemi-
n entropy
nds in the
Los reactants
heterótrofos of andthe
adquieren system.
products.
energía When
libre de aBy convention,
las moléculas y los fotosintéticos la D
adquieren de la radiación solar absorbida. Ambos transforman esta energía libre
eal sign
en ATP ywhen
reaction
c; the heat
trabajo
entropy
releases heat,
otros compuestos
content
biológico
it is said toincreases
ricos en energía
of the products
a temperatura
becapaces and
exo- de proporcionarla
constante. is less
para el as
DH,
as
at ofathenegative
reactants and sign DH has,when by conven- heat is released
mber of
skcal/mol)
negative
equilibrium
molecules
constant,
of
as the reaction
enter
drivingK
A, B,
proceeds,
the actual
(p.
force,
C,
25).
the
and
and
In
magnitude
isD
concentrations
the of
of A, B, C,
gen-
which can b
mal
ken systems—they
to be constant
point of equilibrium, function
at 1 m M
Equation
indicating.
eq at
■ essentially
13–4; the
that no values
more of R, T, and DG9
equilibrium
on aA 1 bB constant
∆ as cC is
the 1
standard
given
free-energy
dD,
values.
by change
where
ature (and also function at constant pres-
DG is forb,
Condiciones
a,
negative thec,
and reaction,
estándarPhysi
approache
done by the reaction. standard conditions (298 K 5 25 whe
8C), conce
wthe
ical number
constants
is and
etics
DG98 c of
notBiochemical
for any based
a[C]reaction
source
[D]
the
on
of
aA
Reaction
reaction
dmolecules
1 this
energy
bB ∆
Types
proceeds,
of A,
biochemical
forcC B,because
C,
cells,
1 dD the
and
stan- dard
actual
D stat
and
of A products
and B are initially
decrease and present
the
Presión 1 atm, [ at
] = 11M
= concentrations M con
o
orable
te do
by
ng,
n are
the
!theprocesses,
5called
equation
work
eq onlya standard
equilibrium as itincrease.
b or, passes transformed
constant
for gases,
Noticeaisthat
to at (13–2)
given
zone
partial
when acon-
by
orpressures stants
reaction of
an
is at101.3
equi
G of a spontane- [A] [B] K9 ) to d
ndtemperature.
rve. are written with aenergy
The(kPa),
whenprime
c c dd
or (such
1
that
there atm,
is as
the
cells
no forceDG98
force
can and
drivingdriving the e q the
reactionsys
distinguish them [C]
from [C][D]
equilibrium
the
direction and is¢Gdefined
[D] untransformed is ] = 10 Mas
zero—Equation = the
con- O]standard
7) y [H stants
= 13–4 use
55,5 M redu
refreeis¢G a[D]
5simple
energy, relationship
!described by thebetween
Gibbs [H
free-
K¿ (pH
+ -7

cs and
states are
that the the molar concentrations (13–2)
2

¢G¿8 5 ln
RT (13–4)
TABLE 1
1eq e q
ed by chemists and change,
[A] a a bb DG8. By this definition, the standa
[B]
physicists.
[A] [B] (Note that most other [C]eq[D]eqtex1
ring
G,
mponentswhich
all allows
chemical
at the prediction
point
reactions of of the
equilibrium.
that0 5involve direc-
¢G 5 ¢G¿8 hydrogen
1 RT ln ions is [H
xtbooks
t require that
l[B],
reactions,
terms inuse
red the
the
their
are symbol
exact
those
pH DG89 rather
equilibrium
actually
0. Most prevailing
biochemical than
posi- DG98.
reactions, Our
[A]eq[B] use
eq
howeve o
ng
reacting [C],system
system
¢G¿8 and [D]
is not
lnare
K¿ at the molar concentrations
equilibrium, (13–3) the
of
ount
em DG98,of
under recommended
5
work
2R!
they
observation.canor
e q by
(in an
well-buffered international
theory)
The aqueous
perform
concentration com- mittee
solutions near pH 7;of
etion
as
f they components
toward
chemists grow and
and at
equilibrium the
biochemists,
and the
point
represents
is of
concentration
equilibrium.
intended of a
water to (55.5 M) are
is equation
mperature
free-energy
by the disorder express
and change the
pressure. effects
of a commonly
Heterotrophic
chemical
¢G¿8 5 2RT ln K¿emphasiz
a reacting
magnitude
ze that
action, the
and
system
of which
transformed
the term [C]
is
constant.
c
can
[D]
not
free
d
be
/[A]
at
energy,
a
[B]
equilibrium,
expressed
b DG9, is the criterion
is called
the
eq

n the
ee energy coursefromof nutrient molecules, and
Cálculo de ΔGº a partir de los datos del equilibrio de la enzima
fosfoglucomutasa que cataliza la reacción reversible:
Glucosa-1-fosfato = glucosa-6-fosfato.

Si se parte de una concentración 0,020M de glucosa-1-fosfato, se añade

la enzima y dejamos que transcurra la reacción en le sentido directo, o si
partimos de glucosa-6-fosfato 0,020M y dejamos transcurrir la reacción
en el sentido inverso, la mezcla final en equilibrio en ambos casos será
0,001M en glucosa-1-fosfato y 0,019M en glucosa-6-fosfato, a 25ºC y
pH=7,0.

Calcular la constate de equilibrio y con este parámetro, calcular la

variación de la energía libre estándar. R=8,315 J/mol K, el proceso es
endergónico o exergónico?
 ¢G¿8 5 2R! ln K¿eq (13–3)
R= 8,315 J/mol K

Glucosa-1-fosfato ⇌ glucosa-6-fosfato
rd free-energy change of a 25chemical + 273,15 = 298,15 K

implyKeqan alternative
= [glucosa-6-fostato]
[glucosa-1-fosfato]
mathematical way When
equilibrio en ambos casos será 0,001M en glucosa-1-
g its equilibrium constant. Table
fosfato y 0,019M 13–2
en glucosa-6-fosfato

lationship between
Keq = [0,019]
DG98 and K¿ . If the .
[0,001] eq
onstant for a given chemical reaction is
dard free-energy change of that reaction ,
tural logarithm of 1.0 is zero). If K¿eq of a
eater than 1.0, its DG98 is negative. If K¿eq
energy changes, ¢G¿18 and ¢G¿28, of the two reac-
13–3). two reactions overall
are reaction A B
sequential, ∆ C, which
cancels ou
: ¢G¿8
Reacciones
total 5 ¢G¿ 8
secuenciales
1 1 ¢G¿ 28.
reaction is the constant
overall reaction A ∆ C, which has its own and thus its own s
positive (1)DG98 can A 88n B change, ¢G¿18¢G¿8 total. The DG98 values
constant
(2)
tive. This is pos- B 88nand C thus ¢G¿
cal reactions 28its own standard
are additive. Fo
tants])change,
Sum: in Equa- ¢G¿8
A 88n C total A. The
∆ DG98
C,
¢G¿18 1 ¢G¿8 ¢G¿8 values
total is of
the sequen
sum of t
2
olute cal value reactions
than are additive.
free-energy changes, For¢G¿ the ove
18 and ¢
principle of bioenergetics explains how a thermo-
val ofA ∆
the prod- C, ¢G¿8 tions:
total
mically unfavorable (endergonic) reaction can be
is the
¢G¿8 sum
total 5 ¢G¿ of 1the
8 1 ¢G¿ individ
28.
ucts]/[reactants]
n infree-energy
the forward changes, direction by¢G¿ 18 andAit¢G¿
coupling
(1) to 2B
88n a of th
8, ¢
ln ([products]/
Este principio de ¢G¿8
tions:
y exergonic reaction 5 ¢G¿
through
bioenergética explica cómo 8 a1
una reacción ¢G¿
common 8.
termodinámicamente
interme-
desfavorable
total 1 a una (2) B exergónica
reacción2altamente 88n C ¢
queand are
(endergónica) se puede dirigir hacia delante, acoplándola
DG98
. For example, the
tenga unDGintermediario común
synthesis of Sum: glucose A6-phos-
free energy that (1) A 88n B 88n 8C
¢G¿ ¢
1
 -
ion exergonic:
taneously in the direction written. Another cellular
many organisms:
d
ac-
y- reaction, the hydrolysis of ATP to ADP and Pi, is very
llm-
or ATP
Glucose H Oglucose
1 P188n ADP 1 Pi1
88n 6-phosphate   ¢G¿8
H 2O 5 230.5 kJ/mol
exergonic: i 2 ¢G¿8 5 13.8 kJ/mol
a-
ded
s TheseATP two 1 reactions
H 2O share the common AMintermediates
to DG98ADP Pi  ¢G¿8 kJ/mol
13BioenergeticsAndBiochemicalReactionTypes.indd
1 Page 511 16/08/12 8:12 user-F408
will The positive value of88n predicts 5 230.5
that under standard
e
ut Pi and the H2reaction
O andwillmay be expressed as sequential
cts conditions tend not to proceed
These two reactions share the common intermediates spon-
e
on
The reactions:
taneously in the direction written. Another cellular
P and H2O and may be expressed as sequential
s
c-
the
i
reaction, the hydrolysis of ATP to ADP and Pi, is very
m- reactions:
(1)
exergonic: Glucose 1 Pi 88n glucose 6-phosphate 1 H2O 13.2 Chemi
ons
ed
y (2) ATP
(1) 1 HGlucose
ATP 1HP2iO
O 88n1ADP 88n
188n ADP
glucose
P   ¢G¿8 1 Pi kJ/mol 1 H2O
6-phosphate
5 230.5
ill 2 i

yts
ely The
Sum: ATP
(2) overall
ATP 11H2glucose
standardO 88n ADP
free-energy
88n Pchange
1 ADP
i is obtained
1 glucose by !
6-phosphate Bioener
These two reactions share the common intermediates
heby adding the values 88n
DG98glucose for individual reactions: relation
H2O ATP
Pi andSum: and1may ADP 1 glucose
be expressed 6-phosphate
as sequential
he system
reactions:
¢G¿8 5 13.8 kJ/mol 1 (230.5 kJ/mol) 5 216.7 kJ/mol
ns the law
(1) Glucose 1
The overall Pi 88n glucose
reaction 6-phosphate
is exergonic. 1 Hcase,
In this 2O energy ! All chem
ly (2)
storedATP
in 1
ATPH2Ois88n ADP
used Pi the synthesis of glucose
to1drive forces:
 Notice that H O is not included
by the in this
reaction. expression,
The as
equilibrium its ¢G¿8, isDG
constant ap
ute between the initial and final states is immaterial.
2
concentration
Glucose (55.5
P 88n ) is assumed
Mdrolysis
glucose of to remain
ATP is
6-phosphate unchanged
H O for!a given
Whe
We have said that DG98 is a way of expressing the
1 i 1 2
by the reaction. The equilibrium constant for the hy- equilibrium to g
ATP
uilibrium H
constantO 88n ADP P
is for a reaction.i For!¿reaction (1)] [Pi ]
1 2 1 [ADP
drolysis of ATP 5 2.0¢G¿8
3 105 5 and
M2R
eq 5
ove,
m: ATP 1 glucose 88n ADP 1 glucose 6-phosphate 2
[ATP ] reve
[ADP] [Pi ] ! The actual
!¿eq 5 5 2.0 3 105 M at e
The
[glucose 6-phosphate]
2
[ATP] equilibrium23constant for the two coupled
variable tha
!
21
!¿eq 1 5 5 3.9 3 10 M The
[glucose] [Pi ]
The equilibrium constant for the two coupled
[glucose reactions] [ADP
6-phosphate is concentrati
] [Pi ] inde
!¿eq 5
tice that H2O is not included in
3
this [glucose
expression, as [Pi ] [ATP ] DG 5 DG98
]its occu
[glucose 6-phosphate ] [ADP] [Pi ]
! When chem
23 21
!¿eq 5 5 (!¿ ) (K¿ ) 5 (3.9 3 10 M ) (2.0
ncentration (55.5 M[glucose
3 ) is assumed to remain
] [Pi ] [ATP] eq unchanged
1
eq
2 DG is3
7.8 2110
2 reac
the reaction.
5 (!¿eThe
q )(K¿ equilibrium
eq ) 5 (3.9 3constant
5 23 3
10 M )(2.0for the 3 10hy-M )
5
to go in the
1 2
over
olysis of ATP5 7.8is3 10 2
This calculation illustrates an important and positive
DGp
equilibrium constants: although thereverse DG98 valdire
WORKED
tions EXAMPLE
of ATP,13–2ADP,Calculation
and Pi inoferythrocytes
DGp are as shown
hydrolysis of ATP.in Table
The 13–5.
hydrolytic Assume
cleavage of the that
ation potent
the pH
alculate the is 7.0free
actual andenergy
the oftemperature is 37DG8C
hydrolysis of ATP, (body temperature). What does this
p, in human erythrocytes.
Calcule
hereveal
standard la energía
about
free energy libre
the amount real de
of hidrólisis
of hydrolysis of ATP de
energy is ATP, kJ/mol,
required to synthesize
and ATP under the sameandcel-
∆Gp, en eritrocitos humanos. La energía libre
230.5 TABLE 13–5theAdenine
concentra-
Nucleotide, Inorganic Phosphate,
onslular
of ATP, ADP, and Pi in erythrocytes are as shown in Table 13–5. Assume
conditions? thatConcentrations in Some Cells
Phosphocreatine
estándar de hidrólisis de ATP es -30.5 kJ / mol y
e pH is 7.0 and the temperature is 37 8C (body temperature). What does this Concentration (mM)*
las concentraciones de ATP, ADP y Pi en los
veal about the amount of energy required to synthesize ATP under the sameATPcel- ADP†
Solution: Theseconcentrations
eritrocitos of ATP,
muestran en el cuadro 13-5. ADP, and Pi in human erythrocytes AMP are Pi 2.25,
PCr
lar conditions?
Suponga que el pH es 7.0 y la temperatura es 37 Rat hepatocyte 3.38 1.32 0.29 4.8 0
0.25, and 1.65 mM, respectively. The actual free energy of hydrolysis of ATP8.05under
° C (temperatura corporal). ¿Qué revela esto Rat myocyte 8.05 0.93 0.04 28
lution:
theseTheconditions
concentrations
is of ATP,by
given ADP,
the and Pi in human(see
relationship erythrocytes
Eqn are
13–4) 2.25,
acerca de la cantidad de energía requerida para Rat neuron 2.59 0.73 0.06 2.72 4.7
25, and 1.65 mM, respectively. The actual free energy of hydrolysis of ATP under
sintetizar ATP en las mismas condiciones Human erythrocyte 2.25 0.25 0.02 1.65 0
ese conditions
celulares?
is given by the relationship (see Eqn 13–4) [ADP][P
E. coli cell i ] 7.90 1.04 0.82 7.9 0
¢Gp 5 ¢G¿8 1 RT ln
[ADP][Pi] [ATP]
*For erythrocytes the concentrations are those of the cytosol (human erythrocytes lack a nucleus and
¢Gp 5 ¢G¿8 1 RT ln mitochondria). In the other types of cells the data are for the entire cell contents, although the cytosol and the
Substituting the appropriate values [ATP]
we get mitochondria have very different concentrations of ADP. PCr is phosphocreatine, discussed on p. 526.

ubstituting the appropriate values we get †

This value reflects total concentration; the true value for free ADP may be much lower (p. 519).

(0.25233 1023)(1.65 3 1023)

¢G 5 230.5 kJ/mol 1 c (8.315 J/mol(0.25
p ? K)(310
3 10 K) ln 3 10 )
)(1.6523
d
¢Gp 5 230.5 kJ/mol 1 c (8.315 J/mol ? K)(310 K) ln d
(2.25 3 1023)
(2.25 3 1023)
24
5kJ/mol
5 230.5 230.5 1 kJ/mol 1 (2.58
(2.58 kJ/mol) ln 1.8kJ/mol)
3 1024 ln 1.8 3 10
5kJ/mol
5 230.5 230.5 1 kJ/mol 1 (2.58 kJ/mol)(28.6)
(2.58 kJ/mol)(28.6)
5 230.5 kJ/mol 2 22 kJ/mol
5 230.5 kJ/mol 2 22 kJ/mol
5 252 kJ/mol
5 252 kJ/mol
Note that the final answer has been rounded to the correct number of significant