Download presentation
Presentation is loading. Please wait.
Published byGervase Griffin Modified over 9 years ago
1
Chapter 8 An Introduction To Metabolism
2
Metabolism u The totality of an organism’s chemical processes. u Concerned with managing the material and energy resources of the cell.
4
Catabolic Pathways u Pathways that break down complex molecules into smaller ones, releasing energy. u Example: Respiration
5
Anabolic Pathways u Pathways that consume energy, building complex molecules from smaller ones. u Example: Photosynthesis
6
Energy u Ability to do work. u The ability to rearrange a collection of matter. u Forms of energy: u Kinetic u Potential u Activation
7
Kinetic Energy u Energy of action or motion.
8
Potential Energy u Stored energy or the capacity to do work.
9
Activation Energy u Energy needed to convert potential energy into kinetic energy. Potential Energy Activation Energy
10
Energy Transformation u Governed by the Laws of Thermodynamics.
11
1st Law of Thermodynamics u Energy can be transferred and transformed, but it cannot be created or destroyed. u Also known as the law of “Conservation of Energy”
12
2nd Law of Thermodynamics u Each energy transfer or transformation increases the entropy of the universe.
13
Entropy u Measure of disorder.
14
Summary u The quantity of energy in the universe is constant, but its quality is not.
15
Question? u How does Life go against Entropy? u By using energy from the environment or external sources (e.g. food, light).
16
Free Energy u The portion of a system's energy that can perform work.
17
Free Energy G = H - TS G = free energy of a system H = total energy of a system T = temperature in o K S = entropy of a system
18
Free Energy of a System u If the system has: u more free energy u it is less stable u It has greater work capacity
19
Free Energy Changes
20
Spontaneous Process u If the system is unstable, it has a greater tendency to change spontaneously to a more stable state. u This change provides free energy for work.
21
Chemical Reactions u Are the source of energy for living systems. u Are based on free energy changes.
22
Reaction Types u Exergonic: chemical reactions with a net release of free energy. u Endergonic: chemical reactions that absorb free energy from the surroundings.
23
Exergonic/Endergonic
24
Biological Examples u Exergonic - respiration u Endergonic - photosynthesis
25
Cell - Types of Work u Mechanical - muscle contractions u Transport - pumping across membranes u Chemical - making polymers
26
Cell Energy u Couples an exergonic process to drive an endergonic one. u ATP is used to couple the reactions together.
27
ATP u Adenosine Triphosphate u Made of: - Adenine (nitrogenous base) - Ribose (pentose sugar) - 3 phosphate groups
29
Adenine Ribose Phosphates
30
Key to ATP u Is in the three phosphate groups. u Negative charges repel each other and makes the covalent bonds between the phosphates unstable.
31
ATP u Works by energizing other molecules by transferring phosphate groups.
33
ATP vs Food u ATP: u Renewable energy resource. u Unstable bonds u Food: u Long term energy storage u Stable bonds
34
ATP Cycles u Energy released from ATP drives anabolic reactions. u Energy from catabolic reactions “recharges” ATP.
35
ATP Cycle
36
ATP in Cells u A cell's ATP content is recycled every minute. u Humans use close to their body weight in ATP daily. u No ATP production equals quick death.
37
Enzymes u Biological catalysts made of protein. u Cause the rate of a chemical reaction to increase.
38
Chemical Reaction AB + CD AC + BD AB and CD are “reactants” AC and BD are “products”
40
Enzymes u Lower the activation energy for a chemical reaction to take place.
42
Enzyme Terms u Substrate - the material and enzyme works on. u Enzyme names: Ex. Sucrase - ase name of an enzyme 1st part tells what the substrate is. (Sucrose)
43
Enzyme Name u Some older known enzymes don't fit this naming pattern. u Examples: pepsin, trypsin
44
Active Site u The area of an enzyme that binds to the substrate. u Structure is designed to fit the molecular shape of the substrate. u Therefore, each enzyme is substrate specific.
46
Models of How Enzymes Work 1. Lock and Key model 2. Induced Fit model
47
Lock and Key Model u Substrate (key) fits to the active site (lock) which provides a microenvironment for the specific reaction.
48
Induced Fit Model u Substrate “almost” fits into the active site, causing a strain on the chemical bonds, allowing the reaction.
49
Substrate Active Site
50
Enzymes u Usually specific to one substrate. u Each chemical reaction in a cell requires its own enzyme.
51
Factors that Affect Enzymes u Environment u Cofactors u Coenzymes u Inhibitors u Allosteric Sites
52
Environment u Factors that change protein structure will affect an enzyme. u Examples: u pH shifts u temperature u salt concentrations
53
u Cofactors: non-organic helpers to enzymes. Ex. Fe, Zn, Cu u Coenzymes: organic helpers to enzymes. Ex. vitamins
54
Enzyme Inhibitors u Competitive - mimic the substrate and bind to the active site. u Noncompetitive - bind to some other part of the enzyme.
56
Allosteric Regulation u The control of an enzyme complex by the binding of a regulatory molecule. u Regulatory molecule may stimulate or inhibit the enzyme complex.
57
Allosteric Regulation
58
Control of Metabolism u Is necessary if life is to function. u Controlled by switching enzyme activity "off" or "on” or separating the enzymes in time or space.
59
Types of Control u Feedback Inhibition u Structural Order
60
Feedback Inhibition u When a metabolic pathway is switched off by its end- product. u End-product usually inhibits an enzyme earlier in the pathway.
62
Structural Order u Separation of enzymes and metabolic pathways in time or space by the cell's organization. u Example: enzymes of respiration
64
Summary u Recognize that Life must follow the Laws of Thermodynamics. u The role of ATP in cell energy. u How enzymes work.
Similar presentations
© 2024 SlidePlayer.com. Inc.
All rights reserved.