Module 3 Chemical Reactions Flashcards

(47 cards)

1
Q

What are 6 reaction types?

A
  1. Acid/Base
  2. Substitution
  3. Elimination
  4. Addition
  5. REDOX
  6. Isomerization
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2
Q

Transfer of protons from one species to another

A

Acid/Base Reaction

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3
Q

Switching one group for another

A

Substitution

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4
Q

Removing a group completely from the molecule

A

Elimination

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5
Q

Adding a group to the molecule

A

Addition

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6
Q

Changing the oxidation state of a group on a molecule

A

REDOX

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7
Q

Rearrangement of groups within the same molecule

A

Isomerization

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8
Q

What are 3 reaction components?

A
  1. Nucelophile
  2. Electrophile
  3. Catalysts
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9
Q

What can receive electrons to form new bonds. They are electron poor species.

A

Electrophile

Carbocations, carbonyl groups, alkenes, alkynes

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10
Q

What are electron rich species?

Examples?

A

Nucleophile

Anions, heteroatoms with lone pair electrons, alkenes, alkynes

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11
Q

What is used to help increase the rate at which a reaction occurs?

A

Catalyst

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12
Q

________ donate electrons.

A

Nucleophile

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13
Q

_______ receive eletrons

A

Electrophile

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14
Q

Neutral to negative the atom is an ______

A

Electrophile

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15
Q

Neutral to positive, the atom is an ______

A

Nucleophile

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16
Q

Name the 3 substitution reactions

A
  1. Nucleophilic
  2. Aromatic
  3. Acyl
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17
Q

Is an alkene a nucleophile or electrophile?

A

It can be both, just depends on the reaction.

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18
Q

What is oxidation?

What is reduction?

A

Oxidation is loss of electrons (H+) or increase in the number of bonds to O or N.

Reduction is gain of electron (H+) or decrease in the number bonds to O or N.

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19
Q

What are the 6 classes of enzymes?

A
  1. Transferase
  2. Hydrolase
  3. Oxidoreductase
  4. Lyase
  5. Ligase
  6. Isomerase
20
Q

Enzyme that transfer functional groups

21
Q

Enzyme that breaks bonds using water (hydrolysis)

22
Q

Enzyme that catalyze REDOX reactions

A

Oxidoreductase

23
Q

Enzyme that catalyze elimination reactions

24
Q

Enzyme that joins two molecules together

25
Enzyme that catalyze structural shifts (intramolecular group transfer)
Isomerase
26
What is the Bronsted-Lowrey definition of an acid and base?
An acid is a proton donor A base is a proton acceptor
27
What is the Lewis definition of an acid and base?
An acid is an electron pair acceptor A base is a electron pair donor
28
What is nucleophilic substitution?
Addition of an electron rich species (nucleophile) to an electron poor species (electrophile)
29
What is an aromatic substitution?
Substitution of a hydrogen on an aromatic ring with another group excluding oxygen or nitrogen.
30
What is an acyl substitution?
Addition of an electron rich species (nucleophile) to an amide, esters, or carboxylic acids
31
Two hallmarks to an elimination rxn?
1. Removal of a group 2. Double or triple bond formation
32
Addition reactions usually involve _______ and _______. Acyl substitution reactions involve ______, _________, and ________.
Aldehyde and Ketones (Addition Reactions) Amides, Esters, and Carboxylic Acids (Substitution Reactions)
33
Adding an OH to an aromatic ring is considered a ___________ reaction.
REDOX
34
What kind of reaction is the very first step of glycolysis?
Isomerization
35
In order for a process to be favored to work, Delta G needs to be _________.
Negative (aka spontaneous reaction)
36
What does a catalyst do?
Increase reaction rate by lowering energy of activation. A catalyst will allow the reaction to go through alternate pathway. Catalyst do not appear in the product and are not consumed during the process.
37
What are the main type of catalyst in biological systems?
Enzymes
38
What are the differences between fibrous and globular proteins?
Fibrous Proteins - structural, found in cell membranes and transport groups. Globular Proteins- more spherical in nature, less rigid in their structure and can undergo confirmation changes.
39
What are the characteristics of enzymes?
1. Efficiency - work better than typical chemical catalyst. 2. Specificity- specific for individual chemical processes. 3. Well Regulated- adaptive to different metabolic, environmental conditions. Knows when to turn off.
40
What is Delta S? How does this relate to enzymes?
Entropy, a measure of disorder. The most important factor for enzymes, enzymes work by creating more disorder in their enzymatic structure.
41
What are co-factors?
They are non-protein components that are required to allow an enzyme to perform its role. They bind within enzyme to promote enzymatic processes.
42
What are two types of cofactors and give examples?
Inorganic Ions (Mg, Zn, Cu, Fe, Mn, Ni, Mb) Organic (Coenzymes)- derived from vitamins, NADH, Niacin, Thiamin, Folic Acids, Vitamin D, Riboflavin, Vitamin C.
43
A favored reaction = __________ A disfavored reaction = _________
spontaneous non-spontaneous
44
What enzyme is involved with nucleophilic substitution reactions?
Transferases
45
What enzyme is involved with acyl substitution?
Hydrolases Ex: Ester to carboxylic acid
46
What enzyme is involved with redox reactions?
Oxidoreductase
47
What enzyme is involved with elimination reactions? What enzyme is involved with addition reaction? What enzyme is involved with isomerization?
Lyase Ligase Isomerase