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First Law of Thermodynamics
Energy can be transferred or transformed but not created or destroyed.
Second Law of Thermodynamics
Every energy transfer or transformation increases entropy (disorder) of the universe.
Metabolism
The totality of an organism’s chemical reactions.
(Cont.) Energy is fundamental to these processes.
An emergent property that arises from orderly interactions between molecules.
Metabolic Pathway
Begins with a specific molecule and ends with a product.
Each step is catalyzed by a specific enzyme.
Two types: Catabolic and Anabolic.
Catabolic Pathways
Energy is released by breaking down complex molecules into simpler compounds.
The energy is then available to do cellular work.
Anabolic (A.K.A. Biosynthetic) Pathways
Energy is consumed to build complex molecules from simpler ones.
Energy
The capacity to cause change.
Exists in various forms, some of which can perform work.
(Can be converted from one form to another)
Potential Energy
_____ that matter possesses because of its location or structure.
Kinetic Energy
Associated with motion.
Thermal Energy
Kinetic energy associated with random movements of atoms or molecules.
Heat
The thermal energy transfer of one object to another.
Light
Another type of energy that can be harnessed to perform work.
(Hint: Photosynthesis)
Chemical Energy
Potential energy available for release in a _____ reaction.
Thermodynamics
The study of energy transformations.
(Cont.)
Open System: energy and matter can be transferred between the system and its surroundings
Isolated System: exchange with the surroundings cannot occur
Entropy
A measure of molecular disorder, or randomness.
Increased by energy transfers and transformations because some energy is always lost to its surroundings as heat.
Spontaneous Processes
Occur without energy input; they can happen quickly or slowly.
Increases entropy of the universe.
Nonspontaneous Processes
Energy is required, and in turn lowers the entropy of the universe.
Free Energy (G)
The portion of a system’s energy that can do work when temperature and pressure are uniform throughout.
ΔG = Gfinal state - Ginitial state
(Only reactions with negative Δ are spontaneous)
A measure of a system’s instability, its tendency to change to a more stable state.
Unstable systems (Higher Δ) tend to change so they become more stable (Lower Δ)
Exergonic Reaction
Proceeds with a net release of free energy and is spontaneous; ΔG is negative
(Ex. overall reaction for Cellular Respiration)
Endergonic Reaction
Absorbs free energy from its surroundings and is not spontaneous; ΔG is positive.
(Ex. photosynthesis, the reverse process of cellular respiration)
Work
A cell does three kinds:
Chemical - pushing endergonic reactions
Transport - pumping substances across membranes against the direction of spontaneous movement
Mechanical - such as beating cilia or contracting muscle cells
Energy Coupling
The use of an exergonic process to drive an endergonic one, to do work
ATP
Composed of ribose, adenine and a chain of 3 phosphate groups.
Used in energy coupling and to make RNA.
Hydrolysis of this releases energy and produced ADP and inorganic phosphate.
A renewable resource produced by addition of a phosphate group to ADP.
Catalyst
A chemical reaction that speeds up a reaction without being consumed by the reaction.
Enzyme
A macromolecule that acts as a catalyst; most of these are proteins.
Speeds up reactions without being consumed.
Specific for the reactions they catalyze.
Activation Energy
The energy required to start a reaction by contorting reactant molecules so the bonds can break.
Substrate
The reactant molecule on which an enzyme acts.
Becomes an enzyme-substrate complex when bound to an enzyme.
Active Site
The region of the enzyme to which the substrate binds.
Enzymes change shape due to chemical interactions with the substrate.
Induced fit brings chemical groups of the active site together.
Cofactors
Non-protein molecules that help carry out processes that are difficult for amino acids.
May be organic or inorganic.
An organic _____ is called a coenzyme.
Competitive Inhibitors
Bind to the active site of an enzyme and prevent the substrate from binding.
Noncompetitive Inhibitors
Bind to an alternate site on the enzyme, causing the active site to change shape and become less effective.
Allosteric Regulation
Occurs when a protein’s function at one site is affected by the binding of a regulatory molecule to a seperate site.
Cooperativity
The binding of one substrate molecule to the active site of subunit locks all other subunits into the active shape.
(Amplifies the response of enzymes to substrates.)
Feedback Inhibition
The end product of a metabolic pathway shuts down the pathway by inhibiting an enzyme that functions early in the pathway.
(Prevents the cell from wasting chemical resources by synthesizing more product than is needed)