Chapter 6 Flashcards by Allison Garrett

Metabolism

All chemical rxns in cell (catabolic and anabolic)

Bioenergetics, energy flow, through a living system

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Catabolic

break down/degradation
release energy

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Anabolic

Biosynthesis
absorb energy

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carbohydrate metabolism

cellular respiration (catabolic) in animal cells
photosynthesis (anabolic) in plant cells

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Cellular respiration

catabolic, breakdown sugar
C6H12O6 + 6O2 -> 6CO2 + 6H2O + energy

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Photosynthesis

anabolic, synthesize sugar
6CO2 + 6H2O + energy -> C6H12O6 + 6O2

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energy

ability to do work, bring about change
joules or calories

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Important types of energy

Solar (photons)
Chemical (chemical bonds)
mechanical (muscular contraction, cellular movement)

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Potential energy

Stored energy

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Kinetic energy

Energy of motion

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“free” energy

Gibbs free energy Willard Gibbs (1878)
portion of system energy available to preform work at uniform (temp/pressure)

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change in G = change in H - (T x change in S)

H = enthalpy ( total energy )
S = entropy (disorder)
T = absolute temp (kelvin)

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negative change in G

spontaneous process
change in H negative
Tchange in S very positive

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change in G

G final - G initial
more to less free energy
system becomes more stable and energy released can be used

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exergonic reactions

“energy outward”
net release
change in G = negative
spontaneous, released E to surroundings
metabolism -> heat
more reactants than products
high to low GFE

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Endergonic reactions

“energy inward”
net input
change in G = positive
not spontaneous
requires E from surroundings
coupled with exergonic rxn.s
low to high GFE

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Metabolism equilibrium

never at equilibrium

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activation energy

energy required to start reaction
High AE -> slows rxn
Low AW -> quickens rxn

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Energy and reactions

“contorts” reactants
transition state
allows rxn. to occur

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Thermodynamics

Study of energy flow/transfer of physical matter
in a system/environment

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1st law of conservation of energy

Energy cannot be created or destroyed, can be transferred/transformed, and can go from one form to another

Thermodynamics does not

Indicate if process is possible, will occur spontaneously, or what conditions are needed for the process

2nd law of thermodynamics

Energy transformations loose useable energy
Every transformation makes the universe less organized/ less organized, more disordered

Entropy

disorder

Universe prefers

entropy/disorder less energy to be disordered

Relative disorganization

S; disorder; at the end of process there's less energy and more S

ATP structure

Nucleotide (adenine) 5 carbon sugar (ribose) = adenosine 3 phosphates (triphosphate

ATP function

Chemical (anabolism) Transport (protein pumps) Mechanical (cilia movement)

Coupled reactions

exergonic energy fuels endergonic rxns

Adenosine triphosphate

ATP energy currency of cells Hydrolysis rxn -> water cuts P off Uses ATP to create ADP P and energy converts to ADP and creates energy

Adenosine diphosphate

ADP Dehydration rxn. -> produce H2O glucose degradation uses energy ADP and P to make ATP

Coupled reactions

one reaction endergonic one exergonic exergonic (ATP) fuels process phosphorylation (phosphate transfer) (ADP + P = ATP)

Enzymes

Catalyze metabolic rxns most require energy input lower activation energy enzyme doesnt change get energy out dont produce energy makes rxn. more likely to occur

-ase

enzymes

Lock-n-key model

substrate acts as key to specific enzyme interact via H bonds or ionic bonds initially thought

Induced fit model

Binding causes confirmation change interactions close together enhance catalytic ability

active sites

lower activation energy template for multiple substrates to combine R group microenvironment distort substrate shape and increase reactivity direct temporary chemical interactions

rate of enzymatic catalysis

Increased concentration of substrate increases rate of reaction to a point then reaction rates decline and must add more enzyme temp, pH, cofactors, coenzymes effect

Anabolic reaction

synthesis reaction enzymatic

Catabolic reaction

Degradation reaction enzymatic

Native function and activity

Native shape effected by change in concentration of substrate, optimal conditions, cofactors, coenzymes

cofactors

inorganic ions required for enzymes role

coenzymes

organic molecules, help enzymes function by combining with them

Inhibitors

Prevent enzyme from operating competitive and noncompetitive

Competitive inhibitors

bind to active site and prevent substrate from binding

Noncompetitive inhibitors

bind to another site on enzyme which causes the enzyme to change shape so substrate cannot bind

Allosteric activation/inhibition

process when noncompetitive inhibitor bonds to enzyme at secondary site changing function

Activator in allosteric activation

stabilizes function form

Inhibitor in allosteric activation

stabilizes inactive form

Cooperativity in allosteric activation

binding on one side increases likelihood for bonding on another multi-site enzyme/protein

Feedback inhibition

Reaction halted by product produced by reaction binds to enzyme ATP pathways; help save glucose