Introduction to Bioenergetics

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Biology of Cells IA (Chemistry of Life) Karteikarten am Introduction to Bioenergetics, erstellt von Alice Hathaway am 09/01/2019.
Alice Hathaway
Karteikarten von Alice Hathaway, aktualisiert more than 1 year ago
Alice Hathaway
Erstellt von Alice Hathaway vor mehr als 5 Jahre
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Thermodynamics Cells appear to violate through high order 1st law = energy cannot be creates or destroyed 2nd law = in spontaneous process processes, entropy of universe increases
1st law impact Change in internal energy = heat energy absorbed - work done by system Places upper limit on energy cost - energy store less than or equal to energy coming in to system
2nd law impact Entropy = degree of disorder At equilibrium, no change in entropy When all reach equilibrium, entropy death Entropy hard to measure experimentally
Gibbs Free Energy Free energy = change in energy - temp x change in entropy
Impact of Gibbs For spontaneous reactions, change <0 - through high temperature/ large increase in entropy/ highly exothermic If >0. not spontaneous hence energy needed
ΔG' Standard Gibbs energy change for reaction at pH 7 Can measure by measuring equilibrium constant ΔG' = -RT ln [product]/[reactant]
State function Change processes same regardless of pathways
Couple reactions Can do this to make ΔG <0 Reaction thermodynamically unfavoured coupled to one that is to drive reaction
ATP is driving force Coupled to reactions to make thermodynamically favourable ΔG' = -30.4kjmol-1 Energy of hydrolysis depends on concentration of reactants nadproducts and concentration of Mg2+ and Ca2+ ~50jkmol-1 under typical conditions
Calculating ΔG value -30.5 + RT ln [ADP][Pi][H+]/[ATP]
Why exothermic? Phosphate and ADP more resonance stabilisation than ATP Electrostatic repulsion in phosphate More water can bind ADP and Pi than ATP
Phosphorylation potential phosphorylation potential between biologically important phosphorylated molecules Can be phosphorylated by those with lower potentials Phosphorylates those with higher potentials Phosphocreatine phosphorylates ADP - energy store to safeguard ATP
Measuring ATP changes Turnover of 0.5kj/min in exercise ATP buffered by phosphocreatine in many mammalian tissues In high energy demand/ lack of oxygen, Pcr decrease in concentration prior to depletion of ATP
Coupling ATP hydrolysis to chemical reactions Phosphorylates glucose so can be broken down ATP used to build peptides Join 2 nucleic acids to synthesise DNA ATP changes equilibrium constant by 10^5 - shifted to form product
Activated carriers
Reduction and oxidation In reduction, NAD+ receives H+ and 2e NADP+/NADPH used in biosynthesis Phosphate group acts as tag to allow recognition of redox system by enzymes Can achieve 2 redox potentials - ATP synthesis and metabolites
ACetyl Co A Reactive sulphur bonds CoA needed to catalyse acylation Hydrolysis G'=-31.5kjmol-1. Activated acyl group Universal acyl group carrier e.g. fatty acids
Activated Coenzymes Drive thermodynamically unfavourable reactions All contain adenine base - may have been used as reaction motif by early RNA catalysts
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