BIOL EXAM 2 STUDY GUIDE CHPT 8
Energy
the ability to do work. can be stored or released
work
anything that requires energy
types of energy
heat//chemical
Heat energy
heating molecules up theyll move faster
chemical
energy in chemical bonds, bonds contain chemical energy. When u break a bond u release energy, building a bond requires energy
can energy be stored-released
Energy can be stored or released
potential energy
is stored energy. Chemical energy, in chemical bonds are potential energy
kinetic energy
is the energy of motion, when things are moving its kinetic energy
how can we measure energy in the form of calories?
1cal is = to the amount of heat required to raise 1gram of water to 1 degree C
is matter potential energy or kinetic?
potential energy
why is matter considered potential energy?
All Matter is potential energy bc matter is made of atoms held together by bonds
thermal energy
heat energy associated with random movement of atoms or molecules which is kinetic energy
is thermal heat energy kinetic or potential?
kinetic energy
thermodynamics
the study of energy and energy transfermation
2 types of thermodynamic systems
Closed system, open system
closed system
does not exchange energy or material, matter with anything outside of the system. The only truly closed system is the universe
open system
exchange energy and material. All living things are open systems
are biological systems open, or closed systems
open systems
are all living things open systems?
yes.
1st law of thermodynamics
Energy can never be created or destroyed, it can only be transferred or transformed. matter can neither be created or destroyed
what does 1st law of thermodynamics also apply to?
Matter. also called law of conservation of energy of matter
does the amount of energy remain constant in a closed system?
yes
is the amount of energy in the universe constant?
yes
2nd law of thermodynamics
in every reaction transfer or transformation entropy increases. (chaos)
is energy ever completely gone?
Even though energy can be lost from a system to the surroundings, it is never completely gone because of the 1st Law of thermodynamics
what is entropy?
the amount of disorder and chaos, in every reaction some useable energy is lost as heat.
endergonic reactions
require energy, ( energy input) build reactions as in dehydration synthesis.so they don't happen spontaneously
endothermic
if reactions specifically need heat
exergonic reactions
release energy( energy output) , happen spontaneously. Breaks reactions as in hydrolysis.
exothermic
if energy is released as heat
do reactant have a higher energy level than the product? or does the product have higher energy levels than the reactant?
reactants have HIGHER energy levels than the product
gibbs free energy
the energy that's available to do work in the system, its what metabolism is all abt
is free energy, essentially, potential energy?
Free energy is essentially potential energy
Delta G (ΔG)
the change in free energy.
what if ΔG is negative? ( less than 0 )
the reactant is be exergonic
the beginning of exergonic reactions
the reactant has a certain amount of energy . In exergonic reactions, the reactants have more potential energy than the products.
in exergonic, with a 10 and products at 3 what (ΔG) be?
(ΔG) will be negative (-7)
what if (ΔG) is greater than 0?
the reactant is endergonic, an uphill reaction. the product has more energy than the reactant
in endergonic, with a 10, and reactant at 3 what will (ΔG) be?
(ΔG) will be positive 7
spontaneous reactions
occur without additional energy, not instantaneous
the higher the (ΔG) the more...
unstable. more bonds is more free energy, less stability.
what is (ATP)
adenosine triphosphate
adenosine- (p-p-p)- 3 phosphates
whats the bond between phosphate groups ( p - p )?
terminal phosphate bond
terminal phosphate bond
a high energy bond
out of the 3 p-p-p in adenosine-p-p-p,
which p is the terminal phosphate?
the last phosphate
what happened when ATP is used as an energy source?
the phosphate bonds break
phosphorylation
is the addition of a phosphate group to another molecule.
is hydrolysis of ATP exergonic or endergonic?
an exergonic reaction
whats the product of ATP?
ADP+PI
what does hydrolyis of ATP yield?
product with less energy than reactants
what does "gradients are unstable" mean?
that they can hold a lot of potential energy
Activation energy
the energy required to start the reaction, all reactions need some type of activation energy
plants are autotrophs
( self-feeding) they make their own organic molecules
animals are heterotrophs
(consume) organic molecules
Energy intermediates
also called electron carriers
NAD+
grabs electrons, oxidize another molecule
NAD+
(in oxidized form)
+ e- + H to
NADH ( in reduced form ) for gaining electrons
Catalysts
molecules that lower activation energy
enzymes
biological catalysts, usually made of protein but can be made of RNA.
the most important thing about an enzyme (1)
they lower activation energy. They will denature if exposed to unoptimal temps or Ph
the most important thing abt an enzyme (2)
They're unchanged by the reaction. They are neither the reactants nor the products.
Catalase is reusable...
By lowering activation energy enzymes speed up the rate of reaction
enzymes have an active site binding to
the reactant( substrates), the reactant in enyme reactions
Active site is specific to..
the substrate and it matches the size shape and charge
what is it called when enzymes and substrate bond?
substrate complex
lock and key
the enzyme is the lock, the substrate is the key
shape of enzymes active site & substrate matching
The shape of the enzymes active site matches the substrate EXACTLY
in the induced fit model...
the enzyme changes shape to accommodate the substrate
what happens to molecules at lower temperatures?
molecules are moving slower NOT DENATURING
enzymes are saturated
adding more enzymes increase the rate of the reaction as long as substrate is constrant
enzyme inhibition
inhibiting enzymes bc cell wants fewer reactions – if you have to much of something you wont keep making it- cell bothers with inhibition bc it wants to reuse the enzyme
competitive inhibition
the inhibitor molecule competes with the substrate for the active site.
in competitive inhibition
Inhibitor mimic the shape of the substrate, blocking it from binding
non-competitive inhibition
inhibitor does not compete for active site, inhibitor binds to a site AWAY from the active site called the allosteric site 9( “allo” away from )
in non-competitive inhibition
Inhibitor bound to the allosteric site causes enzyme to change its shape, so now substrate cannot fit into active site