1. Thermodynamics and ATP

2. Enzyme 1 Enzyme 2 Enzyme 3 A B C D Reaction 1 Reaction 2 Reaction 3
Figure 8.UN01
Enzyme 1
Enzyme 2
Enzyme 3 A B C D
Reaction 1
Reaction 2
Reaction 3
Starting molecule
Product
Figure 8.UN01

3. (a) First law of thermodynamics (b) Second law of thermodynamics
Figure 8.3
Heat
Chemical energy
Figure 8.3 The two laws of thermodynamics.
(a) First law of thermodynamics
(b) Second law of thermodynamics

4. Gibbs Free Energy ΔG = ΔH – TΔS
ΔH is change in enthalpy or total energy
ΔS is change in entropy
In a spontaneous process the ΔG is always negative.
System must either give up enthalpy OR
Have a positive TΔS
If ΔG is positive or Zero the process is NOT SPONTANEOUS

5. WHAT IS THE ΔG IN THESE EVENTS?
Figure 8.5b
WHAT IS THE ΔG IN THESE EVENTS?
Figure 8.5 The relationship of free energy to stability, work capacity, and spontaneous change.
(a) Gravitational motion
(b) Diffusion
(c) Chemical reaction

6. Amount of energy released (G  0)
Figure 8.6a
(a) Exergonic reaction: energy released, spontaneous
Reactants
Amount of energy released (G  0)
Energy
Free energy
Products
Figure 8.6 Free energy changes (G) in exergonic and endergonic reactions.
Progress of the reaction

7. Amount of energy required (G  0)
Figure 8.6b
(b) Endergonic reaction: energy required, nonspontaneous
Products
Amount of energy required (G  0)
Energy
Free energy
Reactants
Figure 8.6 Free energy changes (G) in exergonic and endergonic reactions.
Progress of the reaction

8. (a) The structure of ATP
Figure 8.8a
Adenine
Phosphate groups
Ribose
Figure 8.8 The structure and hydrolysis of adenosine triphosphate (ATP).
(a) The structure of ATP

9. Adenosine triphosphate (ATP)
Figure 8.8b
Adenosine triphosphate (ATP)
Figure 8.8 The structure and hydrolysis of adenosine triphosphate (ATP).
Energy
Inorganic phosphate
Adenosine diphosphate (ADP)
(b) The hydrolysis of ATP

10. Phosphorylated intermediate
Figure 8.9
Glutamic acid conversion to glutamine
(a)
NH3
NH2
GGlu = +3.4 kcal/mol
Glu
Glu
Glutamic acid
Ammonia
Glutamine
(b)
Conversion reaction coupled with ATP hydrolysis
NH3 1 P 2
ADP
NH2
ADP
ATP
P i
Glu
Glu
Glu
Glutamic acid
Phosphorylated intermediate
Glutamine
GGlu = +3.4 kcal/mol
(c)
Free-energy change for coupled reaction
Figure 8.9 How ATP drives chemical work: Energy coupling using ATP hydrolysis.
NH3
NH2
ATP
ADP
P i
Glu
Glu
GGlu = +3.4 kcal/mol
GATP = 7.3 kcal/mol
+ GATP = 7.3 kcal/mol
Net G = 3.9 kcal/mol

11. Protein and vesicle moved
Figure 8.10
Transport protein
Solute
ATP
ADP
P i P
P i
Solute transported
(a) Transport work: ATP phosphorylates transport proteins.
Vesicle
Cytoskeletal track
Figure 8.10 How ATP drives transport and mechanical work.
ATP
ADP
P i
ATP
Motor protein
Protein and vesicle moved
(b) Mechanical work: ATP binds noncovalently to motor proteins and then is hydrolyzed.

12. Energy from catabolism (exergonic, energy-releasing processes)
Figure 8.11
ATP
H2O
Energy from catabolism (exergonic, energy-releasing processes)
Energy for cellular work (endergonic, energy-consuming processes)
Figure 8.11 The ATP cycle.
ADP
P i

13. How is ATP Made in a Cell?
Substrate Level
Phosphorylation

14. Chemiosmosis Start with a mitochondrion or chloroplast Trap H+ in the
intermembrane space

15. Chemiosmosis Start with a mitochondrion or chloroplast Trap H+ in the
intermembrane space
How can this
lead to
ATP production?

16. ATP Synthase permeable to H+ H+ flow down concentration gradient
catalytic
head
rod
rotor
Enzyme channel in mitochondrial membrane
permeable to H+
H+ flow down concentration gradient
flow like water over water wheel
flowing H+ cause change in shape of ATP synthase enzyme
powers bonding of Pi to ADP: ADP + Pi  ATP
ADP P +
ATP
But… How is the proton (H+) gradient formed?