the totality of chemical reactions occurring within an organism; the metabolism of a cell manages the material & energy resources of the cell
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anabolic pathway
invest energy to build large molecules from smaller molecules (Ex. Photosynthesis) -gaining free energy because its becoming larger and less stable, surrounding area loses free energy for use and decreasing entropy
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catabolic pathway
break large molecules down into smaller molecules and release energy. (Ex. Cellular respiration; glucose and other organic fuels are broken down in the presence of oxygen to carbon dioxide and water) -so losing free energy because it's smaller molecules with more stability, but the surrounding area gains free energy which means more entropy
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energy coupling
when the energy released from catabolic pathway can be stored and used to drive catabolic pathways -can help metabolism from reaching equilibrium, although it is mostly because things are always moving in and out of cell and being recycled
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energy
capacity to cause change or do work; Ability to move and/or rearrange matter
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kinetic energy
Energy of movement; Moving objects impart movement on other matter
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Thermal energy
KE associated w/ random movement of atoms & molecules
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Electromagnetic energy
KE associated w/ photons traveling from sun
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potential energy
stored energy w/ the capacity to do work; energy resulting from position or structure
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Chemical energy
potential energy that can be released by chemical reactions (energy from food released as it is broken down) -Complex molecules have more chem energy
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heat
the transfer of this energy from one molecule/object to another
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system
the matter under study
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surroundings
anything outside of the system
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open systems
Energy and matter can be transferred between the system and its surroundings
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closed system
unable to exchange energy and matter with its surroundings
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First Law of Thermodynamics
energy in the universe in constant; energy can’t be created or destroyed but it can be transferred and transformed
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Second Law of Thermodynamics
when transferred or transformed usable energy decrease, because some is converted to thermal energy and released as heat, which is unable to do work; thus, the entropy increases
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entropy
quantity that measures disorder or randomness; the more randomly arranged a collection of matter is, the greater its entropy Heat energy has the most entropy because it is random molecular motion
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spontaneous process
a process that occurs without any outside input of energy or outside help rarely happen and when they happen, takes years to happen though, which is why enzymes are preferred
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non-spontaneous process
a process that cannot occur without an input of energy or outside help
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free energy
Portion of a system's energy that can perform work when temperature is uniform throughout the system. (G)
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Know Gibbs Free energy formula and what each variable means
enthalpy: total energy in a biological system
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What does it mean when the change in free energy is positive?
it means that there is an absorption of free energy anabolic, endergonic ex: photosynthesis (takes solar energy and invests into bonds of glucose molecule)
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What does it mean when the change in free energy is negative?
it means that there is a release of free energy catabolic, exergonic ex: cellular respiration (breaks glucose bonds and energy stored becomes ATP)
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Be able to relate the amount of free energy in a system to the stability and work capacity of the system
the more free energy in the bonds the less stable because it’s bigger, more organized, lower entropy less free energy in bonds, more in external factors, more stable because smaller, less organized, higher entropy
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Endergonic reactions
intake of free energy, positive change in G
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Exergonic reactions
release of free energy, negative change in G
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What is the change in free energy when a cell has reached equilibrium?
no change in free energy
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How do cells keep from reaching equilibrium?
cells are constantly moving and recycling things in and out of the cell; energy coupling also na/k pumps
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Chemical Work
The pushing of endergonic reactions that would not occur spontaneously, such as the synthesis of polymers from monomers
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Transport Work
The pumping of substances across membrane against the direction of spontaneous movement
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Mechanical Work
Beating of cilia, Contraction of muscle cells, and Movement of chromosomes during reproduction
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energy coupling
The use of energy released by an exergonic process to drive an endergonic one; Mediated by ATP
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structure of ATP
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How much energy is released when ATP is hydrolyzed?
The 3 phosphate groups all have an equal negative charge, and like charges repel. The phosphates want to break off so they are very unstable.
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Explain how ATP drives cellular work through phosphorylation.
When ATP phosphorylates the phosphorylated intermediate (recipient of the terminal phosphate) the molecule becomes less stable with more free energy to do work Transport work: The transfer of a phosphate to a transport protein changes its shape and.or its ability to bind with another molecule Mechanical work involving motor proteins: ATP bonds to the motor protein, hydrolyzes, causes the motor protein to move, another ATP binds
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Describe the ATP cycle
Catabolic reactions fuel the phosphorylation of ADP to form ATP energy comes from cellular respiration or photosynthesis ATP is hydrolyzed and releases energy to do work in the cell
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Why don’t most spontaneous processes happen spontaneously?
They take a very long time to actually happen, usually years
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enzyme
A macromolecule that acts as a catalyst, a chemical agent that speeds up a reaction without being consumed
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activation energy
the energy needed to reach the transition state, the point where the bonds can break
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transition state
the state where the bonds of the reactants start to break
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What do enzymes do to catalyze reactions?
lower their activation energy
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substrate
The reactant(s) an enzyme acts on
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Explain why there is such high specificity for an enzyme and its substrate.
Specificity of the enzyme / substrate interaction is determined by the shape of the active site. Also R groups of amino acids on enzyme must be a complementary charge to the substrate
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active site
location on the enzyme that substrates bond to
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induced fit
When a substrate binds to the active site, it “grabs” the substrate in a tight fit
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catalytic cycle
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How do enzymes lower activation energy? (4 ways)
when an enzyme attached to substrate, the induced fit can stretch the substrate, which puts stress on the bonds and make them easier to break, thus lowering their activation energy provide a template in which the substrate can come together, in a way that a reaction can occur between them active site can't provide a microenvironment that is conducive to the reaction -ex. active site can have acidic R-groups and some reactions do better in low pH environment direct participation of the active site in the chemical reaction -might involve brief covalent bonding between the substrate and side chains of the amino acids of the enzymes
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Explain how substrate concentration influences the rate of reaction
increase in substrate concentration, increase rate of reaction until enzymes run out to convert decrease in substrate concentration, decrease rate, less substrate to convert
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Explain how temperature and pH (AND SALINITY) influence enzyme activity and reaction rates
-increase in temp: particles move around more and bump into one another more so reactions happen more frequently too high, enzyme denatures -decrease in temp: slows down because particles less active -pH changes activeness and shape of the enzyme - optimal pH is best
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cofactor
inorganic materials that help with enzymes catalyze reactions -Zinc, Iron, copper
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Coenzyme
organic materials that help enzymes catalyze reactions; other proteins that aren't enzymes
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competitive inhibitor
inhibitor that stops enzymatic activity by binding to the active site, blocking substrate -cell can overcome competitive inhibition by adding more substrate
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noncompetitive inhibitor
inhibitor that stops enzymatic activity by binding to a different site and changing the shape of the active site so the substrate can’t bind onto it
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What is allosteric regulation?
-activator locks the enzyme in its active form when the -active sites are exposed so more substrate can be made into product inhibitor locks the enzyme in an inactive form when the active site is not exposed Changes by a conformational change of shape
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What is the structural level of most proteins that are regulated allosterically?
Quaternary since there are multiple units
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Explain how ATP and ADP act as inhibitors and activators.
ATP is an inhibitor because it can’t allow the cell to do work immediately because it cannot be used as energy ADP + P is an activator because it can be instantly used to do work (phosphorylation)
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cooperativity
Substrate molecules bind to one active site and stabilize the other active sites so they remain in the active form. Substrates bound to one active site makes it easier for more substrates to bind to the other active site.
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Explain how feedback inhibition can shut off a metabolic pathway
Enzymes can be turned off by feedback inhibition. Metabolic pathways consist of a chain of reactions. Enzyme 1 makes the first molecule in the chain.(intermediate A) The final product (isoleucine) Once enough product is made it diffuses back to the 1st enzyme. Isoleucine binds to enzymes as a noncompetitive inhibitor because no more needs to be made.
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Enzyme structure/specificity essay
-EXPLAIN the enzymes active site and the substrate are similar in shape and charge -the active site is the most important region -substrate has to be complementary in shape and charge of the R-groups of amino acids in enzyme -Enzymes are proteins, have levels of structure -primary structure: dictates R-groups which determines charge, imwhat substrates its gonna react -tertiary structure; determines shape of active site -conformational change in shape -EXPLAIN catalytic cycle: substrate binds to active site of enzyme; enzyme catalyzed reaction; does so by decreasing the activation energy needed to get to transition phase; products are released from the enzyme enzyme active sites open for more substrates
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Explain the graph
-There is a certain amount of active sites for the increasing amount of substrate -at first there's a lot of production because of the high enzyme to substrate ratio -as substrate is added, there’s not enough enzymes to keep up with the inc in substrate so the rate slows -Explain how would you increase the reaction rate: increase enzyme concentration to make more active sites available for substrate
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Explain the graph
-each enzyme has a certain optimal temperature -as temp increases the particles move faster and bump into one another much more -more reactions happen and as a result the rate of reaction increases exponentially -the top of the curve is the max rate and the optimal temp -as the temp goes over the optimal temp the protein starts to denature and can’t catalyze anymore -optimal temp: the maximum point on the graph, the temp where the rate of reaction is highest
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Explain the graph
-This graph shows the rate of product synthesis as a reaction progresses (with time). The first increase in rate shows the amount of product increasing and production occurs. The sudden plateau is when all the substrate is used and no more product can be produced. -How would you calculate the rate for a given time interval: always y/x; product/time in this case
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