exam 2 Flashcards
thermodynamics
the branch of chemistry concerned with energy changes
definition of energy
the capacity to do work
what are the two states of energy
- kinetic
2. potential
what is kinetic energy
energy of motion
what is potential energy
stored energy
forms of energy
mechanical, light, sound, heat, electrical, radioactivity
most convenient way of measuring energy
heat
what is one calorie
the heat required to raise 1 gram of water by 1 degree celcius
where does energy flow from into the biological world?
the sun
what captures the sun’s energy
photosynthetic organisms
what is the energy from the sun stored as
stored as potential energy in chemical bonds
oxidation
atom/molecule loses an electron
reduction
atom/molecule gains and electron, higher level of energy than oxidized from
redox reactions done in what
pairs
first law of thermodynamics
energy cannot be created or destroyed
what is the total amt of energy in the universe?
remains constant
what happens to heat during each conversion
some energy is lost as heat
second law of thermodynamics
energy always converts from a more ordered/less stable form to a less ordered/ more stable form
entropy
disorder, continuously increasing
disorder happens
spontaneously
order requires
energy
free energy equation
G = H - TS
in G = H - TS, what does G stand for
energy available to do work
in G = H - TS, what does H stand for
enthalpy
G = H - TS, what does T stand for
absolute temp
in G = H - TS, what does S stand for
entropy
what is enthalpy
energy in a molecules bond
what is entropy
unavailable energy
where do our photosynthetic organism reside?
algae, bacteria, eukaryotes in ocean, trees, mostly in water
how do humans capture energy
from plants, convert it to glucose
how is sunlight stored as potential energy
take carbon to fix them together, Carbon-Hydrogen bond is stored energy
role of reducing sugar
reduce other molecules
what is oxidation
atom or molecule loses an electron
what is reduction
atom or molecule gains and electron, higher level of energy than oxidized from
redox is always..
paired, to reduce you must oxidize must always be done at the same time
what is a big cause of disease in cells?
oxidation
energy states always go from..
more ordered and less stable state to a less ordered and more stable form (easier to keep room messy)
change in free energy equation
change in free energy = change in enthalpy - temperature x energy lost/not able to use
DeltaG = deltaH - TS
positive delta G
products have more free energy than reactants, H is higher and S is lower, not spontaneous, requires energy input, endergonic
negative dela G
products have less free energy than reactants, H is lower or S is higher o both, spontaneous, but may not be instantaneous, exergonic
what is extra energy required to do
destabilize existing bonds and initiate a chemical reaction
exergonic reaction rate depends on
activation energy required
larger activation energy proceeds more
slowly
how can activation energy rate be increased
- increasing energy of reacting molecules (heating)
2. lowering activation energy (enzymes- catalysts)
what happens to activation energy without catalysts
its a lot longer
what are catalysts
substances that influence (destabilize) chemical bonds in a way that lowers activation energy
catalysts do not and cannot do what
cannot violate laws of thermodynamics, cannot make endergonic reaction spontaneous, do not alter the proportion of reactant turned into product
what is ATP
adenosine triphosphate, chief “currency” all cells use
what is ATP composed of
ribose - 5 carbon sugar, adenine, chain of 3 phosphates
ATP 3 chain phosphates, describe
- key to energy storage
- bonds are unstable
- ADP - 2 phosphates
- AMP - 1 phosphate (lowest energy form)
What happens in the ATP breakdown
ATP —> ADP (diphosphate) —> AMP (monophosphate) –> usually converts to —> cAMP
what is cAMP?
cyclic AMP(monophosphate), signal molecules that tells the cell its low in energy
fats or carbs store longer term energy
fats
how do animals store energy
store gylcogen in muscles, break down into glucose, which breaks down in ATP
what drives endergonic reactions
ATP hydrolosis, coupled reactions in net -delta G )exergonic and spontaneous
how long do cells store ATP
only a few seconds
what are enzymes
most are proteins, based on amino acid structures, helix and sheet folding, disulfide bond, ionic interaction, globular structure, enzymes change shape of bond and not destroyed or used up, not changed or consumed in reaction
what does the shape of an enzyme do
stabilizes a temporary association between substrates
carbonic anhydrase with and without enzymes
without - 200 molecules of carbonic acid per hour made
with - 600,000 molecules formed per second with enzyme
look at enzyme, substrate, active site diagram
ch. 6, page 8
what is the active site
pockets or clefts for substrate binding, forms enzyme- substrate complex, precise fit of substrate into the active site, applies stress to distort particular bond to lower energy
what is induced fit
enzyme can work on bonds and give a product
better the fit,
better the activation, the quicker the activation will take place
where would enzymes be found
suspended in the cytoplasm or attached to cell membranes and organelles
multienzyme complexes
subunits that work together to form a molecular machine, the product can be easily delievered to the next enzyme, unwanted side reactions are prevented, all reactions ar controlled as a unit
where are proteins found
in lipid bilayer, cytoplasm
rate of enzyme-catalyzed reactions depends on
concentration of substrate and enzyme
what conditions affect the enzymes 3D shape and change the rate
optimum temp and pH
taq polymerase
works at high temps and helps finding DNA
what is an inhibitor
substance that binds to enzyme and decreases its activity
what is a competitive inhibitor
competes with substrate for active site
what is a noncompetitive inhibitor
binds to enzymes at a site other than an active site, causes shape change that makes enzyme ubable to bind to substrate
what can inhibitors bind to?
- active site
2. allosteric site
what is an allosteric site
a site where an inhibitor binds to, other than active site
what happens when an inhibitor binds
causes a conformational change
allosteric enzymes
enzyme that have allosteric site, enzyme that exists in active and inactive forms
where do most noncompetitive inhibitors bind to
allosteric site - chemical on/off switch
what is an allosteric inhibitor
binds to allosteric site and reduces enzyme activity
what is an allosteric activator
binds to allosteric site and increases enzymes activity
what is a metabolism
total of all chemical reactions carred out by an organism
anabolic reactions/anabolism
expends energy to build up molecules
catabolic reactions/catabolism
harvest energy by breaking down molecules
what are biochemical pathways
reactions that occur in a sequence, product of one reaction is the substrate for the next, many steps take place in organelles, assembly line
what is a feedback inhibition
end-product of pathway binds to an allosteric site on enzyme that catalyses first reaction in pathway, shuts down pathway so raw materials and energy are not wasted