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Bioenergetics
The study of the various types of energy transformations that occur in living organisms
Energy
capacity to do work, or the capacity to change or move something
Thermodynamics
the study of the changes in energy that accompany events in the universe
First Law of Thermodynamics
The law of conservation of energy states that energy can neither be created nor destroyed. Cells are capable of energy transduction. The universe can be divided into systems and surroundings.
Second Law of Thermodynamics
events in the universe tend to proceed from a state of higher energy to a state of lower energy (spontaneous events). Every event is accompanied by an increase in the entropy of the universe
Transduction
conversion of energy from one form to another
Examples of energy transduction
electric energy can be transduced to mechanical energy when we plug a clock in. Chemical energy is converted to mechanical energy when heat is released during muscle contraction. Animals, such as fireflies and luminous fish, are able to convert chemical energy back to light
Where is chemical energy stored?
In certain biological molecules like ATP
photosynthesis
conversion of sunlight into chemical energy
What is a system?
a subset of the universe under study
What are the surroundings in a system?
everything that is not a part of a systemthat interacts with the system.
internal energy
energy of the system. change in Eis related to heat and work.
Exothermic reactions
reactions that lose heat
Endothermic
reactions that gain heat
First law of thermodynamics equation
change in E = Q - W, where E is internal energy, Q is heat energy, and W is the work energy
Spontaneous events
events that occur without the input of external energy (second law of thermodynamics)
Entropy
measure of randomness or disorder. associated with random movements of particles or matter
First and Second Law combined equation
change in H = change in G + T change in S, where free energy is change in G, enthlapy is change in H, change in s is change in entropy. change in g is spontaneity of the reaction. <0 reaction is exergonic, >0 it is endergonic
Enzymes
catalysts that speed up chemical reactions. almost always proteins. Can be conjugated with non-protein components
Cofactors
inorganic enzyme conjugates
Coenzymes
organic enzyme conjugates
Properties of enzymes
Present in small amounts, not permanently altered during course of reaction, can’t affect thermodynamics of reactions (only rates), highly specific for their particular reactants called substrates, produce only appropriate metabolic products, and can be regulated to meet needs of cell
Activation Energy
small energy input that is required for any chemical transformation. It slows the progress of thermodynamically unstable reactants
transition state
reactant molecules that reach the peak of the EA barrier
What happens without an enzyme?
only a few substrate molecules reach transition state
What happens when there is a catalyst?
a large proportion of substrate molecules can reach the transition state
Enzyme-substrate complex
when an enzyme interacts with its substrate if forms this (active sites)
active sites
substrate that binds to a portion of the enzyme. have complementary shapes with substrates that allow substrate specificity
What is the formation of an enzyme-substrate complex?
pyruvate kinase, PEP, and ATP
induced fit
shifts in the conformation after binding.
How have researchers determined the three dimension structure of an enzyme at successive stages during a reaction?
By using time-resolved crystallography
3 ways enzymes accelerate reactions
substrate orientation, changing substrate reactivity, and inducing strain in the substrate
How can Enzymes accelerate reactions through substrate orientation?
multiple substrates brought together in correct orientation to catalyze reactions. Changes in atomic and electronic structure occur in both enzyme and substrate during reaction.
How can enzymes accelerate reactions through changing substrate reactivity?
Substrate influenced by amino acid side chains at active site that alter chemical properties (e.g. charge) of substrate. This temporarily stabilizes the transition site.
How do enzymes accelerate reactions by inducing strain in the substrate?
enzyme changes conformation of substrate to being closer to conformation of transition state. Shifts in the conformation after binding cause an induced fit between enzyme and substrate. Covalent bonds are strained
Examples of ways enzymes accelerate reactions through changing substrate reactivity
Acidic or basic R groups on the enzyme may change the charge of substrate. Charged R groups may attract substrate. Cofactors of enzyme increase the reactivity of substrate by removing or donating electrons
Kinetics
Study of rates of enzymatic reactions under various experimental conditions. These rates can increase with increasing substrate concentrations until the enzyme is saturated
What happens when an enzyme is saturated?
Every enzyme is working at maximum capacity
Maximal velocity or Vmax
velocity at saturation
turnover number
number of substrate molecules converted to product per minute per enzyme molecule at Vmax
Michaelis Constant (KM)
substrate concentration at one-half of Vmax. Units of KM are concentration units. The KM may reflect the affinity of the enzyme for the substrate.
What do Lineweaver-Burk plots show?
plots of the inverses of velocity versus substrate concentrations. facilitate estimating Vmax and KM
Enzyme inhibitors
slow the rates for enzymatic reactions
irreversible enzyme inhibitors
bind tightly to the enzyme