Chapter 6 Flashcards
For Exam 2
What is the FIRST Law of Thermodynamics?
*“Law of conservation of energy”
*Energy cannot be created or destroyed, but can be transformed from one type to another
What is the SECOND Law of Thermodynamics?
Transferring from different kinds of energy will increase how disordered (entropy, jumbled all around) the system is and as this disorder (entropy) increases there is less energy to be used in organisms for change
Kinetic Energy VS Potential Energy
Kinetic-associated with movement
Potential- due to structure or location
H=G+TS
Explain what each letter means
H = enthalpy or total energy
G = free energy or amount of energy for work
S = entropy or unusable energy
T = absolute temperature in Kelvin (K)
Exergonic VS Endergonic
Exergonic = spontaneous
Energy is released by reaction
Endergonic = not spontaneous
Requires addition of energy to drive reaction
An endergonic reaction can be coupled to an exergonic reaction
How does ATP Hydrolysis work?
*Reaction favors formation of products
*The energy liberated is used to drive a variety of cellular processes
*****Describe how cells use the energy released by ATP hydrolysis to drive endergonic reactions. (Coupled reactions)
Catalyst
an agent that speeds up the rate of a chemical reaction without being consumed during the reaction
Enzymes
protein catalysts in living cells
They play a role in all functions of metabolism, i.e breaking up foods into forms that are more easily absorbed by the body.
Ribozymes
R N A molecules with catalytic properties
Activation Energy
*Initial input of energy to start a reaction
*Allows molecules to get close enough to cause bond rearrangement
*Can now achieve transition state where bonds are stretched
What are some common ways to overcome activation energy?
Large amounts of heat
Using enzymes to lower activation energy
How do enzymes lower activation energy?
*Straining bonds in reactants to make it easier to achieve transition state
*Positioning reactants together to facilitate bonding
Active Site
location where reaction takes place
Substrates
reactants that bind to active site
Enzyme-substrate complex
formed when enzyme and substrate bind
TRUE or FALSE– Enzymes have a low specificity for their substrate
FALSE. Have a high specificity
Lock and key metaphor for substrate and enzyme binding – only the right key (substrate) will fit in the lock (enzyme)
What are some Enzyme reactions?
Affinity – Degree of attraction between an enzyme and its substrate
Saturation - Plateau where nearly all active sites are occupied by substrate
Michaelis constant- Substrate concentration where velocity is half maximal value
Competitive VS. Noncompetitive VS. Irreversible Inhibition
Competitive inhibition-
Molecule binds to active site
Inhibits ability of substrate to bind
Noncompetitive inhibition-
Inhibitor binds to allosteric site, not active site
Irreversible inhibition-
Usually bind covalently to an enzyme to inhibit its function
Not a common way for cells to control enzyme function
The RNA is a true catalyst
TRUE or FALSE
TRUE
Catabolic Pathways VS. Anabolic Pathways
Catabolic pathways-
Breakdown cellular components
Exergonic
Complex–>Simple
Anabolic pathways-
Synthesis cellular components
Endergonic
Must be coupled to exergonic reaction
Simple–>Complex
Where do Chemical Reactions occur?
Metabolic pathways
Catabolic Reaction
Breakdown of reactants
Used for recycling building blocks
Used for energy to drive endergonic reactions
Energy stored in intermediates such as ATP, NADH
Example: Breakdown of glucose into two molecules of pyruvate during glycolysis; ATP is produced
What are the 2 ways to make ATP and describe them
Substrate-level phosphorylation-
Enzyme directly transfers phosphate from one molecule to another molecule
Chemiosmosis-
Energy stored in an electrochemical gradient is used to make A T P from A D P and Pi