Chapter 8 Flashcards

(36 cards)

1
Q

Laws of Thermodynamics

A

apply to all matter and all energy
transformations in the universe

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2
Q

First Law of Thermodynamics

A

Energy is neither created nor
destroyed

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3
Q

Seconded Law of Thermodynamics

A

When energy is converted
from one form to another, some of that energy becomes
unavailable to do work.

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4
Q

Entropy

A

measure of disorder in a system

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5
Q

Enthalpy (H)

A

total energy

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6
Q

Free Energy (G)

A

usable energy that can do work

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7
Q

Exergonic Reactions

A

Release free energy

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8
Q

Endergonic Reactions

A

Consume free energy

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9
Q

Catabolism

A

complexity decreases (generates disorder) Complex molecules

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10
Q

Anabolism

A

complexity (order) increases
Free energy + small molecules

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11
Q

Energy

A

Ability to do work/change

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12
Q

Enzyme Substrate-Complex (ES)

A

held together by hydrogen
bonds, electrical attraction, or covalent bonds

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13
Q

Exergonic

A

release energy (‐ΔG)

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14
Q

Induced fit

A

enzyme changes
shape when it binds substrate,
altering shape of active site

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15
Q

Kinetic Energy

A

energy of movement

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16
Q

metabolism

A

sum total of all chemical reactions occurring in a biological system at a given time

17
Q

non-competitive inhibitor

A

bind to enzyme at site other than
the active site

18
Q

potential energy

A

stored energy (stored as chemical
bonds, concentration gradient, or charge imbalance)

19
Q

products

A

substance present at the end of a reaction

20
Q

reactant

A

substance present at the beginning of a reaction

21
Q

ribozyme

A

(RNA) molecule that can catalyze chemical reactions

22
Q

standard free energy

A

the change in free energy that occurs when 1 mol of a substance in its standard state is formed from the component elements in their standard states. Free energy=change in enthalpy- Temperature in kelvin x change in entropy

23
Q

substrate

A

reactants; molecule(s) on which an enzyme exerts
its catalytic action

24
Q

transition state

A

eactive mode of the substrate (aka – reactant)
after there has been sufficient input of energy to initiate the
reaction

25
transition state intermediate
unstable reactants with high free energy
26
uncompetitive inhibitor
bind to enzyme‐substrate complex, preventing release of products
27
competitive inhibitor
compete with natural substrate for binding sites
28
activation energy
amount of energy required to start a reaction
29
active site
place on an enzyme where substrate binds
30
allosteric regulation
an effector binds an enzyme at a site different from the active site, changing the enzyme’s shape
31
reversible inhibition
inhibitor bonds noncovalently to the active site, preventing substrate binding
32
irreversible inhibition
inhibitor covalently bonds to side chains in active site and permanently inactivates the enzyme
33
Enzyme inhibitors
molecules that bind to the enzyme and slow reaction rates
34
Prosthetic groups
non‐amino acid groups bound to enzymes
35
inorganic cofactors
ions permanently bound to enzyme
36
coenzymes
small carbon‐containing molecules; not permanently bound