Monday, September 29, 2014

Chapter 8: Introduction to Metabolism

8.1 An organism's metabolism transform energy and matter, subject to the laws of thermodynamics

Metabolism 
-All of an organism's chemical reactions
-Manages the resources of the cell
Metabolic pathways
-Molecules are changed in a series of steps
-Each step is catalyzed by an enzyme

Metabolic Pathways
Catabolic

  • Breaks down complex molecules
  • Release energy
  • Downhill
  • Cellular Respiration
Anabolic
  • Build more complex molecules
  • Absorbs energy
  • Uphill
  • Synthesis of proteins
Energy
  • The capacity to cause change.
  • Exists in various forms, some of which may be used to perform work
Ex:
-Kinetic
-Thermal(heat): random movement of atoms/molecules
-Light

1st Law of Thermodynamics: the energy of the universe is constant, cannot be created or destroyed - only transferred. *The principle of conservation of energy

2nd law of Thermodynamics: every energy transfer or transformation increases the entropy of the universe. *Causes more disorder/randomness and expansion of universe.

Entropy
-A measure of disorder or randomness
-Therefore every energy transformation makes the universe more disordered
-Increased entropy is sometimes obvious and sometimes not. Heat is often by product that increases entropy

Spontaneous process
  • Occurs on its own
  • Does not require the input of energy
  • Must increase entropy of universe
  • Is "energetically favorable"
Ex.
-Explosion
-Old car rusting

8.2 The free energy change of a reaction tell us whether or not the reaction occurs spontaneously 
  • What is free energy?
-Portion of energy in a system available to perform work where temp and pressure are uniform(like in a living cell)
-Measure of a system's instability
  • Free energy (G)
-Equilibrium will have the lowest possible G for that system ( a valley of free energy)
Δ G = change in free energy(G)
  • Process is only spontaneous + perform work when moving towards equilibrium.
  • Systems never spontaneously move away from equilibrium.
Exergonic Reaction
-Energy outward
-Net release of (G)
-Spontaneous
-Downhill
Endergonic Reaction
-Inward
-Absorbs
-Stores this (G) in molecules
-Nonspon.
-Uphill

8.3 ATP powers cellular work by coupling exergonic reactions to endergonic reactions

  • Cellular work
-Chemical: Ex. Biosynthesis
-Transport: Ex. Active Transport
-Mechanical: Ex. Movement
Energy coupling: Uses an exergonic reaction to drive an endergonic
                             ATP is the source of energy for most cellular processes

ATP Perform Work
-Hydrolysis
-Sometimes w/ phosphorylated intermediate

8.4 Enzymes speed up metabolic reactions by lowering energy barriers

Reactions

  • Molecule needs to reach a contorted unstable state before a bond can change.
  • Energy is required to reach the contorted state called transition state. This is activation energy-"energy required to start a reaction"
Enzymes
  • Lower the activation energy barrier
  • Does not "create" energy - to produce energy producing reaction
  • Speed up reactions that would've occurred either way
  • Are very specific - ie. they're proteins and have specific activation sites for specific func.
How it works
  • Line up substrates correctly.
  • Bending substrates toward transition site - ie. makes bonds easier to break, less energy needed.
  • Provides nice microenvironment - ie. pH pockets.
  • Participates in reaction - Temp. covalent bonds so the active site is the same from beginning to end of reaction.
Rate of Reaction
  • Partially determined by substrate concen.
  • Saturation means all active sites are busy so increasing substrate will not increase rate. Must increase enzyme concen, instead.
Effects on Enzyme Activity
  • Optimal conditions
  • Temp - ie. inc. temp inc. movement & activity until too hot then denatures.
  • pH
Cofactors: nonprotein helpers - may be organic or inorganic
Coenzymes: an organic cofactor

Enzyme Inhibitions

  • Irreversible if they bind to an enzyme via covalent bonds - ie. poison such as sarin & penicillin 
  • Reversible if bound by weak bonds - ie. non/competitive inhibitors
8.5 Regulation of enzyme activity helps control metabolism

-Allosteric regulation: protein's func. is controlled by a regulatory molecule at a separate site
  • May inhibit or stimulate activity
  • Cooperativity: allosteric regulation where one substrate stimulates other active sites
-By time
  • Inhibition or activation
  • Multi enzyme complex where the product of one step is the substrate for another - ie. factory belt
-By Space
  • In organelles
  • In membranes
Feed-back inhibition: End product of a pathway acts as an off switch by inhibiting an early enzyme in the path