Chapter 6 Flashcards

(61 cards)

1
Q

Kinetic energy

A

Energy in motion

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2
Q

Potential energy

A

Stored energy

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3
Q

First Law of Thermodynamics

A

Energy cannot be created or destroyed. Energy can only change from one form to another (e.g., potential to kinetic)

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4
Q

Second Law of Thermodynamics

A

Energy cannot be transformed from one form to another with 100% efficiency

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5
Q

Entropy

A

measure of randomness or disorder of a system

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6
Q

Free energy

A

energy available to do work

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7
Q

Endergonic

A

products have more free energy than reactants.

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8
Q

In an endergonic reaction, ∆G is ________.

A

Positive

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9
Q

Exergonic

A

products have less free energy than reactants

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10
Q

In an exergonic reaction, ∆G is ______.

A

Negative

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11
Q

Activation energy

A

energy that must be processed by a molecule in order for it to undergo a chemical reaction

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12
Q

Catalysis

A
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13
Q

ATP is composed of three components:

A
  1. Ribose (5-carbon sugar)
  2. Adenine (composed of two carbon-nitrogen rings)
  3. Three phosphates
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14
Q

Synthesis of ATP from ADP + Pi is _______, which results in a _______ delta-G.

A

Endergonic; positive

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15
Q

Hydrolysis of ATP to ADP + Pi is ________, which results in a _______ delta-G.

A

Exergonic; negative

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16
Q

Substrate

A

molecule on which an enzyme acts

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17
Q

Active site

A

region of an enzyme surface to which a substrate binds

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18
Q

Enzyme-substrate complex

A

complex formed when an enzyme binds with its substrate

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19
Q

Multienzyme complex

A

assembly of several enzymes catalyzing different steps in a sequence of reactions

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20
Q

What is the optimum temperature of enzymes?

A

35-40°C

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21
Q

What is the optimum pH of enzymes?

A

pH 6-8

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22
Q

Inhibitor

A

substance that binds to an enzyme and decreases its activity

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23
Q

Competitive inhibitor

A

Competes with substrate for the same active site

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24
Q

Noncompetitive inhibitor

A

Binds to enzyme in a location other than the active site, changing the enzyme’s shape so it cannot bind the substrate

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25
Allosteric site
part of an enzyme away from its active site
26
Allosteric activator
substance that binds to allosteric site to keep an enzyme in its active configuration
27
An allosteric activator _______ enzyme activity.
Increases
28
Metabolism
total of all chemical reactions carried out by an organism
29
Anabolism
chemical reaction that expends energy to build up molecules
30
Catabolism
chemical reaction that harvests energy by breaking down molecules
31
During a _______ reaction, complex molecules are broken down into simpler compounds.
Catabolic
32
Biochemical pathways
product of one reaction becomes the substrate of the next reaction
33
During _______ ________, end-product becomes allosteric inhibitor for the first enzyme in the biochemical pathway.
Feedback inhibition
34
Energy flows into ecosystems from the ______.
Sun
35
The most common way of measuring energy is as _____.
Heat
36
Redox reactions transfer ______ energy.
Potential
37
The reduced form of a molecule has ______ potential energy than the oxidized form.
Higher
38
When energy is converted to another form, some of it is lost as ______.
Heat
39
T or F: Order is more likely than disorder.
F: disorder is more likely than order
40
Order is ____ stable, and disorder is _____ stable.
Less; more
41
What are two ways the rate of reactions can be increased?
1. Increasing energy of reacting molecules (e.g., heating up reactants) 2. Lowering activation energy (e.g., catalysts)
42
T or F: Catalysts make endergonic reactions faster AND makes them spontaneous.
F: Catalysts make endergonic reactions faster BUT NOT spontaneous
43
How does carbonic anhydrase relate to homeostasis in the cell?
If blood becomes too acidic, certain reactions cannot happen. Carbonic anhydrase helps maintain level of pH of RBCs
44
Where do enzymes occur in a cell?
Cytoplasm and cell membranes/organelle membranes (e.g., mitochondria, nucleus)
45
What are 3 advantages of multienzyme complexes?
1. Keeps next substrate in association with correct enzyme 2. Limits unwanted side reactions 3. Controlled as a unit
46
What affects rate of enzyme catalyzed reactions?
1. Temperature 2. pH 3. Inhibitors and activators
47
The efficiency of biochemical pathways is coordinated/regulated by the cell. What is meant by efficiency?
- not making a product that is not needed - not making energy when there is enough energy - not wasting energy/chemical resources
48
An enzyme _____ activation energy.
Lowers
49
Increase in temperature of an uncatalyzed reactions _______ its rate.
Increases
50
What happens to an enzyme below the optimum temperature?
Enzyme’s shape is not flexible enough to permit induced fit (how well substrate fits inside active site)
51
What happens to an enzyme above the optimum temperature?
Forces are too weak to maintain enzyme’s shape; enzyme can denature
52
In Gibbs free energy, H =
Enthalpy, or the total energy in a molecule’s chemical bonds
53
In Gibbs free energy, TS =
Amount of disorder in the system
54
Gibbs free energy is symbolized by ______.
G
55
In an endergonic reaction, energy…
Must be supplied
56
In an endergonic reaction, energy…
Must be supplied
57
In an exergonic reaction, excess energy is
Released
58
In an exergonic reaction, excess energy is
Released
59
How does energy enter an ecosystem?
From the Sun
60
How do biological systems ‘locally’ work to decrease entropy?
By expending energy (ATP) constantly
61
How does ATP store energy?
By breaking bonds between P-groups (exergonic)