Unit 3 Exam Flashcards
kinetic energy
energy of motion
potential energy
stored energy
oxidation
loss of electrons
reduction
gain of electrons
1st law of thermodynamics
energy cannot be created or destroyed
2nd law of thermodynamics
the entropy in the universe will increase with time
entropy
(S) measure of randomness or disorder of the system
entropy of ice cubes to water
ice cubes (more ordered, less stable) melts to water (less ordered, more stable), entropy increases: disorder increases
which is more stable: ATP or ADP
ATP more unstable than ADP, adding phosphate groups to covalent bonds make them unstable, low activation energy to break these bonds
substrate
anything that can be acted upon by an enzyme (reactants)
active site
where the substrate binds
allosteric site
regulatory site
allosteric inhibition
where the pathway gets stopped
allosteric modulation
where the pathway gets activated
affinity
how strong/weak the association between enzymes and substrates
feedback inhibition
negative feedback loop, slows the sequence of reactions down
positive feedback loop
induces higher rates of pathways, more product
3 types of respiration
aerobic, anaerobic, and fermentation
aerobic
oxygen is final electron acceptor
anaerobic
some inorganic substance is the final electron acceptor
fermentation
some organic substance is the final electron acceptor, when glycolysis is not working hard enough to keep up, produces lactate or acetaldehyde (yeast cells), recycles NAD+
obligate pathways
have to do it
facilitative pathways
do it if you have to
NAD+
electron carrier, made of NMP and AMP
NMP
active part of NAD+
AMP
structural core of NAD+
inhibition enzyme for glycolysis
phosphofructokinase
inhibition enzyme for krebs cycle
pyruvate dehydrogenase, controls the oxidation of pyruvate, converts pyruvate to CoA for the cycle, inhibited by high levels of NADH
carbon fixation
inorganic carbon (CO2) to organic carbon (sugar)
uses for ATP
biosynthesis, transport across membrane, movement, and intracellular transport
ATP is also an allosteric inhibitor, inhibiting its own production when too much is being formed
which structures stabilize associations between substrates
proteins and RNA
influences of enzyme activity
temperature, pH, inhibitors, activators
competitive inhibition
blocks the active site, 2 molecules compete for same binding site, inhibitor molecule binds at active site prevents substrate from binding to that site
noncompetitive inhibition
binds to a location other than active site, allosteric inhibitor changes shape of enzyme so it cannot bind to substrate
free energy
(G) maximum energy available to do work in any system delta G = delta H - T delta S
endergonic
requires an input of energy for reaction to proceed, delta G> 0, non spontaneous
exergonic
energy is released in the reaction, delta G< 0, spontaneous
activation energy
initial input of energy
if activation energy high, the spontaneous reaction will occur…
slowly; i.e. iron rusting
what is ATP made of
made of adenine, ribose, and triphosphate group
where is ATP storing their energy
in phosphate group, each phosphate group is negatively charged, the covalent bonds are unstable by their repulsion, like a coiled spring
activation energy of ATP hydrolysis is quite high, how are we able to synthesize
enzymes act as catalysts by lowering the activation energy
metabolism
total of all chemical reactions in an organism
anabolism
chemical reactions that expend energy to build up molecules (dehydration reactions), i.e. acetyl coA
catabolism
reactions that harvest energy by breaking down molecules (hydrolysis)
autotrophs
organism that can use simple organic compounds to build all the complex organic molecules it requires as its own food source, self-feeders, ex. plants take sunlight to make glucose in photosynthesis
heterotrophs
fed by others, obtain organic compounds by eating either autotrophs (salad) or other heterotrophs (burger)
cellular respiration
involves the oxidation of organic compounds and using the energy released to form ATP
dehydrogenations
oxidation reactions, the electrons obtained from oxidizing food molecules are accompanied by a proton so that what is really being transferred is a hydrogen, not just an electron
how NAD+ works
coenzyme to facilitate transfer of electrons, after attaching to active site on an enzyme, it accepts a pair of electrons from the substrate and a proton to form NADH
2 mechanisms for ATP synthesis
substrate level phosphorylation and oxidative phosphorylation