Lesson 3, Chapter 6 Flashcards

(76 cards)

1
Q

what is a chemical reaction

A

process in which one or more substances are changed into other substances

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2
Q

when do chemical reactions occur

A

when atoms combine with or dissociate from other atoms

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3
Q

chemical bonds are energy relationships that involve what

A

the electrons of reacting atoms

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4
Q

what is metabolism

A

sum total of all chemical reactions that occur within an organism

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5
Q

what are the 3 states of matter and how can they be changed

A

solid, liquid, gas; physically or chemically

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6
Q

what is energy

A

the ability to do work

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7
Q

how much mass does energy have and how much space does it take up

A

0

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8
Q

what is kinetic energy

A

energy is doing work

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9
Q

what is potential energy

A

energy is inactive or stored

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10
Q

what are the forms of energy

A

chemical, electrical, mechanical, radiant

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11
Q

what is thermodynamics

A

study of energy interconversions

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12
Q

what is the first law of thermodynamics

A

energy cannot be created or destroyed, but can be transformed from one type to another

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13
Q

what is the second law of thermodynamics

A

transfer of energy from one form to another increases the entropy of a system

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14
Q

what is total energy

A

usable + unusable energy

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15
Q

what determines the direction of chemical reactions

A

change in free energy

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16
Q

what is free energy

A

amount of energy available to do work

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17
Q

__ = G + ___

A

H = G + TS

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18
Q

What is gibbs free energy used to predict

A

whether a chemical process is sponteanous or not

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19
Q

what is a spontaneous reaction

A

may have to provide some activation energy but occurs without input of additional energy and will proceed naturally

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20
Q

what is a non spontaneous reactions

A

a continuous energy input is necessary for the reaction to proceed

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21
Q

what is the key factor to see if the reaction is sponteanous

A

deltaG is negative

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22
Q

whats the proper word for sponteanous reactions

A

exergonic

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23
Q

how do u tell if a reaction isn’t sponteanous

A

deltaG is positive

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24
Q

whats the proper word for sponteanous

A

endergonic

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25
is the hydrolysis of atp exergonic or endergonic
exergonic
26
how can an endergonic reaction be coupled
to an exergonic reaction that the two reaction overall is thermodynamically favored
27
what is the major 'energy' molecule produced by metabolism
atp
28
what happens wherever a non-spon reaction needs to occur within the cell
atp is dispatched
29
what drives endergonic reactions
atp
30
what do cells use to drive reactions
atp hydrolysis
31
what happens to a phosphate during a couple reaction
from atp to glucose-phosphorylation
32
what do many proteins bind and use as a source of energy
atp
33
what is a catalyst
an agent that speeds up the rate of a chemical reaction without being consumed
34
what are the functions of enzymes
act as biological catalysts, increase the rate of chemical reactions, bind to substrates at an active site to catalyze reactions
35
main function of an enzyme
act as a catalyst
36
what can u use to recognize enzymes
-ase suffix
37
what is hydrolase
enzymes that facilitate the cleavage of bonds in molecules with the addition of the elements of water
38
what is activation energy
initial input of energy to start reaction
39
2 ways to overcome activation energy
large amounts of heat or using enzymes to lower activation energy
40
how do enzymes lower activation energy
bring reactants together so they don't have to expand energy moving about until they collide at random
41
whats an active site
where a reaction takes place
42
whats a substrate
reactants that bind to active site
43
what is a enzyme substrate complex
formed when enzyme and substrate bind
44
what is affinity
degree of attraction between an enzyme and its substrate
45
what is saturation
plateau where nearly all active sites are occupied by substrate
46
what is michealis constant (Km)
substrate concentration where velocity is half maximal valur or half of the active sites are occupied at one time
47
what does a high Km enzyme need
higher substrate concentration
48
what are enzyme inhibitors
molecules that interact with enzymes in some way and reduce the rate of an enzyme-catalyzed reaction or prevent enzymes to work in a normal manner
49
what is competitive inhibition
inhibitor molecules binds to active site
50
what does a non competitive inhibition do
lower Vmax without affecting Km
51
where does the inhibitor bind
allosteric site
52
what are prosethetic groups
small molecules permanently attached to the enzyme and aids in enzyme function
53
what is a cofactor
usually inorganic ion that temporarilty binds to enzyme to promote a chemical reaction
54
what is a coenzyme
organic molecule that participates in reaction but is left unchanged afterward
55
are enzymes affects by environment
yes
56
what are enzymes usually affected by
temperature and pH
57
where do chemical reactions occur
metabolic pathways
58
which pathway syntehsizes cellular components
anabolic
59
which pathway breakdown cellular components
catabolic
60
how are proteins synthesized
bonding amino acids
61
what is a catabolic reaction
breakdown of reactants
62
what are catabolic reactions used for
recycling building blocks and for energy to drive endergonic reactions
63
what are the 2 ways to make atp
substrate level phosphorlyation and chemiomosis
64
what are electron carriers/shuttles
small organic molecules that play key roles in cellular respiration (for anabolic processes)
65
how are electrons shuttled
redox reactions
66
what is a redox reaction
nad+ and fad gain/lose electrons
67
what is oxidation
removal of electrons
68
what is reduction
addition of electrons
69
what ensures a cell synthesizes molecules when needed
anabolic pathways
70
what are the regulations of metabolic pathways
gene, cellular, biochemical
71
what is feedback inhibition and rate limiting step
product of pathway inhibits early steps to prevent over accumulation of product. can also alter a pathway by regulating the slowest step in the reaction (Rate limiting step)
72
what is proteasome
a large complex that breaks down proteins using protease enzymes
73
what is the role of ubiquitin
tags target proteins to the proteasome to be broken down and recycled
74
what does ubiquitin tagging allow the cell to do
degrade improperly folded proteins, rapidly degrade proteins to respond to changing cell conditions, recycle amino acids for new proteins
75
what do lysosomes contain
hydrolases to break down proteins, carbohydrates, nucleic acids and lipids
76
what is autophagy
recycling worn out organelles using an autophagosome