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Bio102 - Energy
Bio102 - Energy
Bio102 - Energy
Energy
MS GOSHAN
LEARNING OBJECTIVES
to define what is meant by energy
to describe the difference between potential, kinetic, free and activation energy
To describe the functions of enzymes and enzyme inhibition
WHAT DOES A CELL USE
ENERGY FOR?
Cellular use of energy
Synthesis and breakdown of molecules
Transport of molecules
Ingestion and breakdown of pathogens
Exporting waste and toxic material
Movement of cells
The first law of thermodynamics, also known as Law of
Conservation of Energy, states that energy can neither be
created nor destroyed; energy can only be transferred or
changed from one form to another
Flow of energy through living systems = BIOENERGETICS
METABOLISM = all of the chemical reactions that take place
inside a cell
◦ Including those that release and consume energy
METABOLIC PATHWAYS
Two examples:
ANABOLIC PATHWAYS- creating bonds –
building large molecules from smaller ones
◦ Energy is stored in the bonds 🡪 requires energy
All living organisms have the challenge of obtaining energy that in a form that
can be transferred or transformed into energy that can be used for work
Eg/ chemical energy stored in food molecules transformed to ATP through
chemical reactions
THERMODYNAMICS
Second law of thermodynamics
◦ Refers to the quality of energy
◦ It states that as energy is transferred or transformed, more and more of it is wasted (mostly through heat energy
◦ The Second Law also states that there is a natural tendency of any isolated system to degenerate into a more disordered
state. (increase in entropy)
At a biological level
◦ Organisms are highly organised
◦ Require very large amount of energy to maintain a state of organisation / low entropy
POTENTIAL AND KINETIC ENERGY
Kinetic energy = the energy that a particle possesses due
to its motion
Potential energy = the energy stored within an object, due
to the object's position, arrangement or state.
On a molecular level the formation of bonds requires
energy and braking bonds releases energy
◦ THEREFORE bonds contain potential energy in the form of
CHEMICAL ENERGY
FREE ENERGY
FREE ENERGY –
◦ the energy left after the loss of energy through a reaction
◦ Effectively it’s the usable energy from a metabolic reaction
By controlling the readiness of enzymes an organism can control the presence or rate of reactions
Enzymes are controlled by
◦ pH
◦ Salt concentration
◦ Temperature
◦ Co-enzymes
◦ INHIBITION
Allosteric inhibition
Allosterically regulated
enzymes have multiple
protein sub-units
◦ Attachment of allosteric
inhibitor means structure of
all activation sites changes
slightly to reduce efficacy
◦ Opposite for allosteric
activators
Recap questions:
What is the difference between anabolic and catabolic reactions
What is the most common energy source for living organisms?
What is the form of energy used by cells?
What is the first and second law of thermodynamics?
What is the difference between Kinetic and Potential energy?
What is the difference between Free and Activation energy?
Define enzyme?
What methods of inhibition of enzymes are there?
Importance of Co-enzymes and Co-factors
Enzymes work most optimally with the aid of other substances
They bond to them with covalent or hydrogen bonds
◦ Bonding creates most optimal structure for the function of the enzyme \
Enzyme function is partly regulated by abundance and availability of these co-factors and co-enzymes
Feedback Inhibition
Mechanism for enzyme regulation
Cells have evolved to use the products of a reaction to regulate enzyme activity
ATP- ADENOSINE TRIPHOSPHATE
- Addition of phosphate group
requires high amount of energy –
high energy bond formed
- Phosphate groups –ve charge
repel eachother = molecule is quite
unstable
- Release of one or more phosphate
group = release of energy
- Process called HYDROLYSIS
GLYCOLYSIS
First step towards cellular
respiration to yield ATP
Glucose converted to 2
Pyruvate molecules
Occurs inside the cytoplasm
of all cells
GLYCOLYSIS- Energy requiring half
Step 1: enzyme HEXOKINASE catalyses the phosphorylation of glucose
◦ Process requires ATP (where the phosphate comes from)
◦ Negatively charged phosphate group means glucose molecule is no longer able to exit the cell through the plasma
membrane
GLYCOLYSIS
Step 2: An Isomerase enzyme converts glucose-6-phosphate into an isomer Fructose-6-phosphate
GLYCOLYSIS
Step 3: phosphorylation of Fructose-6-phosphate
◦ Catalysed by PHOSPHOFRUCTOKINASE – rate limiting enzyme (less active at low ADP levels)
◦ Second ATP molecule donates a high energy phosphate = Fructose-1,6-Bisphosphate
GLYCOLYSIS
Step 4: fructose-1,6-bisphosphate is highly unstable because of phosphate group
◦ Aldolase enzyme used to cleave it into 2 3-Carbon isomers