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BIO111 > Exam 3 > Flashcards

Exam 3 Flashcards

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1
Q

Where does energy flow into the biological world from?

A

Energy flows into the biological world from the sun.

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2
Q

What do photosynthetic organisms do with solar energy?

A

Photosynthetic organisms capture this energy.

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3
Q

How is solar energy stored in photosynthetic organisms?

A

It is stored as potential energy in chemical bonds.

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4
Q

What is the source of all of Earth’s energy?

A

All of Earth’s energy comes from the sun.

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5
Q

What is an example of a food chain?

A

lion > giraffe > leaves > sun

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6
Q

What is activation energy?

A

The energy required for a reaction to occur, specifically the extra energy needed to destabilize existing bonds and initiate a chemical reaction.

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7
Q

How does activation energy affect the rate of an exergonic reaction?

A

The rate of an exergonic reaction depends on the activation energy required.

A larger activation energy means the reaction proceeds more slowly.

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8
Q

What are two ways to increase the rate of a reaction?

A
  1. Increasing the energy of reacting molecules (heating)
  2. Lowering activation energy.
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9
Q

What are catalysts?

A

Substances that influence chemical bonds in a way that lowers activation energy.

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10
Q

What does ATP stand for?

A

Adenosine triphosphate

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11
Q

What is the structure of ATP?

A

Composed of ribose, adenine, and a chain of 3 phosphates.

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12
Q

What is the key function of ATP?

A

Key to energy storage.

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13
Q

Why are the bonds in ATP significant?

A

Bonds are unstable.

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14
Q

What is the ATP cycle?

A

The ATP cycle involves the continuous building and breaking down of ATP to release energy.

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15
Q

Why is ATP important in muscle contraction?

A

ATP is crucial for muscle contraction and the sodium-potassium pump.

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16
Q

Is ATP suitable for long-term energy storage?

A

No, ATP is not suitable for long-term energy storage.

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17
Q

How much ATP do cells store?

A

Cells store only a few seconds’ worth of ATP.

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18
Q

What happens during ATP hydrolysis?

A

ATP hydrolysis splits ATP into ADP and inorganic phosphate.

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19
Q

What type of reactions does ATP drive?

A

ATP drives endergonic reactions.

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20
Q

What are most enzymes made of?

A

Most enzymes are proteins.

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21
Q

What does the shape of an enzyme do?

A

The shape of the enzyme stabilizes a temporary association between substrates.

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22
Q

Are enzymes changed or consumed in a reaction?

A

Enzymes are not changed or consumed in the reaction.

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23
Q

What is an enzyme?

A

A biological catalyst that speeds up chemical reactions in the body.

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24
Q

What is a substrate?

A

The substance on which an enzyme acts.

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25
What is the active site of an enzyme?
The specific region of an enzyme where the substrate binds.
26
What is an enzyme-substrate complex?
The temporary molecule formed when an enzyme comes into perfect contact with its substrate.
27
What does it mean for an enzyme to fit the substrate shape?
The enzyme's active site is specifically shaped to fit the substrate.
28
What is the ATP cycle?
The ATP cycle involves the conversion of ADP and inorganic phosphate into ATP, which is then used for energy. ## Footnote ATP is not stable for long-term energy storage.
29
What are enzymes?
Enzymes are biological catalysts, most of which are proteins.
30
What happens to enzymes during reactions?
Enzymes are not changed or consumed in reactions.
31
What is the active site of an enzyme?
The active site is a pocket or cleft where substrate binding occurs.
32
What is formed when a substrate binds to an enzyme?
An enzyme-substrate complex is formed.
33
How do enzymes lower activation energy?
Enzymes apply stress to distort particular bonds in the substrate, lowering the activation energy required for the reaction.
34
What is the induced fit model?
The induced fit model describes how the active site of an enzyme changes shape to better fit the substrate.
35
What may be suspended in the cytoplasm?
Erymes may be suspended in the cytoplasm.
36
What can be delivered easily to the next?
Molecular machines can be delivered easily to the next.
37
How can all coactions be controlled?
All coactions can be controlled as a unit.
38
What is believed about RNA?
It is believed that RNA evolved to be the first protein.
39
What is catalysis?
Catalysis is the process of catalyzing a reaction.
40
What is intermolecular catalysis?
Intermolecular catalysis is when RNA acts on another molecule.
41
What affects the rate of enzyme-catalyzed reactions?
Chemical or physical conditions that affect the enzyme's three-dimensional shape.
42
What are some factors that can affect enzyme function?
Optimum pH and temperature.
43
What are inhibitors and activators?
Inhibitors and activators influence the activity of enzymes.
44
What does the substrate sucrose consist of?
The substrate sucrose consists of glucose and fructose bonded together.
45
What happens when the substrate binds to the active site of the enzyme?
It forms an enzyme-substrate complex.
46
What occurs when the substrate and enzyme bind?
The binding places stress on the glucose-fructose bond, causing it to break.
47
What happens to the products after the reaction?
Products are released, and the enzyme is free to bind other substrates.
48
What is the role of enzymes in biochemical reactions?
Enzymes catalyze reactions and can be delivered easily to reactants.
49
How can reactions involving enzymes be organized?
Reactions can be controlled as a unit.
50
Where can enzymes be found within a cell?
Enzymes may be suspended in the cytoplasm or attached to cell membranes and organelles.
51
What are multienzyme complexes?
Subunits work together to form a molecular machine.
52
What is a benefit of multienzyme complexes?
The product can be delivered easily to the next enzyme.
53
What factors affect enzyme function?
Physical conditions that affect the dimensional shape of enzymes.
54
What are ecomplexes?
Ecomplexes are subunits that work together.
55
How can ecomplexes be delivered?
Ecomplexes can be delivered easily to the net.
56
How can ecomplexes be controlled?
Ecomplexes can be controlled as a unit.
57
What role do proteins play in enzyme function?
Proteins act as enzymes to catalyze reactions.
58
What is the significance of RNA in catalysis?
RNA is believed to have evolved to catalyze reactions.
59
What is the relationship between temperature and enzyme function?
Temperature affects the rate of enzyme-catalyzed reactions.
60
What factors can change the rate of enzyme-catalyzed reactions?
Any chemical or physical condition that affects the enzyme's three-dimensional shape can change the rate.
61
What is the optimum temperature for most human enzymes?
Most human enzymes work best at 40°C.
62
What is the optimum pH range for most human enzymes?
Most human enzymes work best within a specific pH range.
63
What is an inhibitor?
A substance that binds to an enzyme and decreases its activity.
64
What is a competitive inhibitor?
An inhibitor that competes with the substrate for the active site.
65
What is a noncompetitive inhibitor?
An inhibitor that binds to the enzyme in a location other than the active site, preventing substrate binding by changing the shape of the active site.
66
What are cofactors and coenzymes?
They are activators that assist enzymes.
67
What is an inhibitor?
A substance that binds to an enzyme and decreases its activity.
68
What is a competitive inhibitor?
An inhibitor that competes with the substrate for the active site.
69
What is a noncompetitive inhibitor?
An inhibitor that binds to the enzyme in a location other than the active site, preventing substrate binding by changing the shape of the active site.
70
What are cofactors and coenzymes?
They are activators that assist enzymes.
71
What are allosteric enzymes?
Allosteric enzymes exist in active and inactive forms.
72
What do most noncompetitive inhibitors bind to?
Most noncompetitive inhibitors bind to the allosteric site.
73
What is the function of an allosteric inhibitor?
An allosteric inhibitor is a substrate that binds to an allosteric site and reduces enzyme activity.
74
What is the role of an allosteric activator?
An allosteric activator binds to the allosteric site to keep the enzymes in active configuration and increase enzyme activity.
75
What are allosteric enzymes?
Allosteric enzymes exist in active and inactive forms.
76
What do most noncompetitive inhibitors bind to?
Most noncompetitive inhibitors bind to the allosteric site.
77
What is the function of an allosteric inhibitor?
An allosteric inhibitor is a substrate that binds to an allosteric site and reduces enzyme activity.
78
What is the role of an allosteric activator?
An allosteric activator binds to the allosteric site to keep the enzymes in active configuration and increase enzyme activity.
79
What is photosynthesis?
The process by which ONLY plants convert light energy, water (H2O), and carbon dioxide (CO2) into glucose and oxygen.
80
What is metabolism?
The total of all chemical reactions carried out by an organism.
81
What are anabolic reactions?
Reactions that expend/use energy to build up molecules.
82
What are catabolic reactions?
Reactions that harvest/get energy by breaking down molecules.
83
What is cellular respiration?
The process where glucose and oxygen are converted into ATP, water (H2O), and carbon dioxide (CO2). ## Footnote Equation: glucose + oxygen ------> ATP + H2O + CO2
84
What is the chemical equation for cellular respiration?
C6H12O6 + 6O2 --> 6CO2 + 6H2O + Chemical Energy (in ATP).
85
What are biochemical pathways?
Biochemical pathways are sequences of reactions where the product of one reaction serves as the substrate for the next.
86
Where do many steps of biochemical pathways take place?
Many steps take place in organelles.
87
What is feedback inhibition?
Regulation of biochemical pathways.
88
How does feedback inhibition work?
The end-product of the pathway binds to an allosteric site on the enzyme that catalyzes the first reaction in the pathway.
89
What is the purpose of feedback inhibition?
It shuts down the pathway so raw materials and energy are not wasted.

BIO111 (1 decks)

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