Please enable JavaScript.

Coggle requires JavaScript to display documents.

Chap 8-9 (Aerobic Cellular respiration-oxygen and organic compounds break…

- - - - happens in the cytoplasm near mitochondria--no oxygen required
      - reactants- 1 glucose---2 NAD+ from ETS --- 2ADP + 2P
      - products- 2ATP -- 2 pyruvic acid -- 2 NADH go to ETS -- 2H+
      - energy investment and energy payoff phase--4 ATP are created and 2 are used-- so NET is 2 ATP
      - converting a 6 carbon glucose to 2 3 carbon pyruvate
    - - happens as it enters the cell
      - reactants- 2 pyruvic acid -- 2 NAD+ from ETS -- 2 Coenzyme A
      - products- 2CO2 -- 2NADH-go to ETS -- 2 Acetyl CoA
    - - Happens inside mitochondrial matrix
      - reactants- 2 Acetyl CoA -- 6 NAD+ from ETS -- 2 ADP + 2P --2 FAD from ETS
      - Products- 4 CO2 --6NADH go to ETS -- 2FADH2 go to ETS -- 2ATP
      - 2 turns- each Acetyl CoA goes around the cycle
    - - INNER mitochondrial membrane--uses oxygen
      - Reactants- 10 NADH -- 2FADH2 -- O2 --H+ -- ADP, P
      - Products- H2O -- 32 or 34 ATP -- NAD+ --FAD
      - Chemiosmosis-movement of ions across a semi permeable membrane
  - - - term is from use of oxygen as terminal electron acceptor
      - occurs in the cristae of the mitochondria
- - - - branching
      - linear
      - cyclical
    - - release energy
      - cut bonds
    - - consume energy
      - 'add'--creates more complex molecules from simpler ones
  - - - Thermal- kinetic energy associated with random movement of atoms or molecules
        
        heat is thermal energy being transferred from one object to another
      - potential-energy something possesses by virtue of location or structure
      - chemical energy- potential energy available for release in a chemical reaction
      - Kinetic-associated with motion
    - - 1st law of thermodynamics-energy cannot be created or destroyed just transferred or transformed
      - 2nd law of thermodynamics-all energy transfer or transformation increases the entropy of the universe
        
        entropy-disorder/randomness
        
        spontaneous process- when entropy is increased 'energetically favorable'
    - - processes with a negative delta G are spontaneous
      - delta G= G(final)-G(initial)
      - free energy is a measure of instability
      - equilibrium is max stability
      - reactions are classified by free energy
        
        endergonic
        
        absorbs free energy
        
        non-spontaneous
        
        exergonic
        
        release of energy
        
        spontaneous
  - - - chemical-pushing endergonic reactions
      - transport-pumping against direction of spontaneity
      - mechanical-ie muscle contraction
    - - using exergonic to drive endergonic
      - most is powered by ATP
        
        ATP--Adenine, ribose and 3 phosphate groups
        
        ATP is hydrolized to ADP
        
        cellular conditions lead to -13 kcal/mol delta G for ATP hydrolysis--standard conditions only lead to -7.3
        
        ATP is very unstable--phosphate groups all have neg charge and are like a compressed spring
        
        ATP hydrolysis often leads to change in shape or ability to bind to another molecule
        
        ATP is renewable
        
        ADP is phosphorylated to create ATP
        
        ATP cycle
      - phosphorylated intermediate--key to coupling exergonic and endergonic
    - - macromolecule that acts as a catalyst--speeds up a reaction
      - Activation energy
        
        ie-key ring contorted is unstable but once allowed back into shape with key on it is stable again
        
        amt of energy needed to push the reactants to the top of an energy barrier
        
        transition state--top of the hill energy spot
        
        many times this energy is absorbed through heat absorption
      - catalysis-process by which a catalyst selectively speeds up a reaction without being consumed
        
        enzyme lowers the activation energy barrier
        
        enzymes DO NOT change the delta G...just the activation energy
      - substrate-the reactant an enzyme acts upon
        
        when substrate and enzyme are bound they create an enzyme-substrate complex
        
        substrate only binds with active site
        
        induced fit- brings chemical groups of the active site into positions that enhance ability to catalyze reaction
      - most end in -ase
      - super fast--and then can be used again! Single enzyme molecule can act on 1,000 substrate molecules per second
      - mechanisms that lower activation energy
        
        orienting substrates correctly
        
        straining substrate bonds
        
        providing a favorable microenvironment
        
        covalently bonding to the substrate
      - enzyme is saturated when all active sites are engaged
      - effect of local conditions
        
        temperature- warmer/better because molecules are moving faster and collide more often with active site
        
        too hot and it denatures the proteins
        
        each enzyme has an optimal temp
        
        most human enzymes have optimal abt 35-40 C
        
        pH
        
        each has an optimal pH
        
        many are 6-8 but some lower like pepsin since it is in the stomach
        
        cofactor- non protein enzyme helper
        
        may be organic or inorganic
        
        if organic is known as a coenzyme
        
        most vitamins are coenzymes
        
        enzyme inhibitors
        
        competitive inhibitors-compete with substrate for active sites
        
        noncompetitive inhibitors- do not compete at the active site-impede enzymatic reaction by binding to another part of the enzyme making the active site less effective
        
        toxins and poisons are often irreversible enzyme inhibitors
        
        pesticides and antibiotics are also enzyme inhibitors
      - Must be regulated
        
        allosteric regulation-regulatory molecule binds to a protein at one site and affects the proteins function at another site
        
        may be inhibition or stimulation
        
        most allosterically regulated enzymes are created from two or more polypeptide subunits
        
        has inactive and active forms
        
        activator stabilizes the active form
        
        inhibitor stabilizes the inactive form
        
        cooperativity--allosteric type of regulation- substrate molecule primes enzyme to act on additional substrate more readily
        
        feedback inhibition- end product of a metabolic pathway shuts down the pathway
- - - - alcoholic- carbon dioxide and ethyl alcohol
      - lactic acid- carbon dioxide and lactic acid