ch 6

Cards (55)

  • Thermodynamics
    Branch of chemistry concerned with energy changes
  • Cells are governed by the laws of physics and chemistry
  • Energy
    Capacity to do work
  • Two states of energy

    • Kinetic - energy of motion
    • Potential - stored energy
  • Heat
    Most convenient way of measuring energy
  • Calorie
    Heat required to raise 1 gram of water 1° C
  • Calorie on food labels

    Actually a kilocalorie (1000 calories)
  • Potential energy

    Energy required for the girl to climb to the top of the slide
  • Kinetic energy

    Stored potential energy released as the girl slides down
  • The Sun provides energy for most living systems
  • Photosynthetic organisms
    Capture energy from sunlight and store it as potential energy in the covalent bonds between atoms in the sugar molecules
  • Redox reactions

    Transfer electrons
  • Oxidation

    Atom or molecule loses an electron
  • Reduction
    Atom or molecule gains an electron, higher level of energy than oxidized form
  • Oxidation-reduction reactions (redox) are always paired
  • All activities of living organisms involve changes in energy
  • First Law of Thermodynamics

    Energy cannot be created or destroyed, energy can only change from one form to another, total amount of energy in the universe remains constant
  • Second Law of Thermodynamics

    Entropy (disorder) is continuously increasing, energy transformations proceed spontaneously to convert matter from a more ordered/less stable form to a less ordered/more stable form
  • Free energy (G)

    Energy available to do work, G = H - TS (H = enthalpy, T = absolute temperature, S = entropy)
  • Positive ΔG

    Products have more free energy than reactants, not spontaneous, requires input of energy, endergonic
  • Negative ΔG
    Products have less free energy than reactants, spontaneous, exergonic
  • Activation energy

    Extra energy required to destabilize existing bonds and initiate a chemical reaction
  • Catalysts
    Substances that influence chemical bonds in a way that lowers activation energy, cannot violate laws of thermodynamics, do not alter the proportion of reactant turned into product
  • ATP
    Adenosine triphosphate, primary energy "currency" used by cells, composed of ribose, adenine, and a chain of three phosphates, key to energy storage, bonds are unstable and release energy when broken
  • ADP
    Adenosine diphosphate, two phosphates
  • AMP
    Adenosine monophosphate, one phosphate, lowest energy form
  • ATP hydrolysis

    Drives endergonic reactions, energy released can supply the energy needed by the endergonic reaction
  • ATP not suitable for long-term energy storage, cells store only a few seconds worth of ATP</b>
  • Most enzymes are proteins, some are RNA (ribozymes)
  • Enzyme active site

    Pockets or clefts for substrate binding, forms enzyme-substrate complex, applies stress to distort particular bond to lower activation energy
  • Multienzyme complexes

    Subunits work together to form molecular machine, offer advantages in catalytic efficiency
  • Ribozymes
    RNA molecules that can catalyze reactions, can catalyze reactions on themselves (intramolecular) or on other molecules (intermolecular)
  • Enzyme function

    Rate depends on concentrations of substrate and enzyme, affected by temperature and pH
  • Competitive inhibitor
    Competes with substrate for binding to the enzyme
  • Noncompetitive inhibitor

    Binds to enzyme at a site other than active site, does not necessarily affect substrate binding
  • Allosteric enzymes

    Exist in active and inactive forms, allosteric inhibitors can bind to allosteric site and reduce enzyme activity
  • Inhibitor
    Substance that binds to enzyme and decreases its activity
  • Competitive inhibitor

    • Competes with substrate for binding to the enzyme (the inhibitor can but does not necessarily bind to the active site)
  • Noncompetitive inhibitor

    • Binds to enzyme at a site other than active site
    • Does not necessarily affect substrate binding to enzyme
    • Inhibits enzymatic activity
  • Allosteric inhibition is not always non-competitive; it can also be competitive and uncompetitive