3 - Biothermodynamics Flashcards
(28 cards)
What is the transfer of energy between and within living organisms?
Thermodynamics
What are the two main types of energy?
- Kinetic
- Potential
What is the energy of motion?
Kinetic Energy
What is the stored energy in chemical bonds?
Potential Energy
Which type of reaction is spontaneous and release energy?
Exergonic Reaction
Which type of reaction is non-spontaneous and required energy?
Endergonic Reaction
What is the DeltaH component in the Gibbs Free Energy Formula?
Enthalpy
What is the DeltaS component in the Gibbs Free Energy Formula?
Entropy
The breakdown of ATP into ADP + Pi + Energy is referred to as what?
ATP Hydrolysis
ATP Hydrolysis is what type of reaction?
Exergonic
What are the 3 Laws of Thermodynamics?
- Energy cannot be created or destroyed
- Entropy increases in closed systems
- Entropy minimizes as temperature approaches absolute zero
Non-protein structures that assist enzymes
Cofactors
What are the 2 types of Cofactors?
- Organic Cofactors
- Inorganic Cofactors
Example of an Organic Cofactor
Vitamins, Heme Groups
Example of an Inorganic Cofactor
Metal Ions (Fe2+ or Meg2+)
A product of a reaction binds to and inhibits the enzyme, preventing excess product formation is defined as what?
Feedback Inhibition
Maximum reaction rate is depicted by what variable?
Vmax
Substrate concentration at 1/2 Vmax is depicted by which variable?
Km
Which variable measures substrate affinity?
Km
Which type of inhibition occurs when an inhibitor binds reversibly to the enzyme’s active site and can be overcome by increasing substrate concentration?
Competitive Inhibition
Vmax is unaffected and Km increases in which type of inhibition?
Competitive Inhibition
Which type of inhibition occurs when an inhibitor binds to a site other than the active site, reducing enzyme activity?
Non-Competitive Inhibition
Vmax decreases and Km is unaffected in which type of inhibition?
Non-Competitive Inhibition
Which type of inhibition occurs when an inhibitor binds to the allosteric site, causing the enzyme to become inactive?
Allosteric Inhibition