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CHEMISTRY TEST 2 > Module 3 Chemical Reactions > Flashcards

Module 3 Chemical Reactions Flashcards

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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

A

Transferase

21
Q

Enzyme that breaks bonds using water (hydrolysis)

A

Hydrolase

22
Q

Enzyme that catalyze REDOX reactions

A

Oxidoreductase

23
Q

Enzyme that catalyze elimination reactions

A

Lyase

24
Q

Enzyme that joins two molecules together

A

Ligase

25
Q

Enzyme that catalyze structural shifts (intramolecular group transfer)

A

Isomerase

26
Q

What is the Bronsted-Lowrey definition of an acid and base?

A

An acid is a proton donor

A base is a proton acceptor

27
Q

What is the Lewis definition of an acid and base?

A

An acid is an electron pair acceptor

A base is a electron pair donor

28
Q

What is nucleophilic substitution?

A

Addition of an electron rich species (nucleophile) to an electron poor species (electrophile)

29
Q

What is an aromatic substitution?

A

Substitution of a hydrogen on an aromatic ring with another group excluding oxygen or nitrogen.

30
Q

What is an acyl substitution?

A

Addition of an electron rich species (nucleophile) to an amide, esters, or carboxylic acids

31
Q

Two hallmarks to an elimination rxn?

A
  1. Removal of a group
  2. Double or triple bond formation
32
Q

Addition reactions usually involve _______ and _______.

Acyl substitution reactions involve ______, _________, and ________.

A

Aldehyde and Ketones (Addition Reactions)

Amides, Esters, and Carboxylic Acids (Substitution Reactions)

33
Q

Adding an OH to an aromatic ring is considered a ___________ reaction.

A

REDOX

34
Q

What kind of reaction is the very first step of glycolysis?

A

Isomerization

35
Q

In order for a process to be favored to work, Delta G needs to be _________.

A

Negative (aka spontaneous reaction)

36
Q

What does a catalyst do?

A

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
Q

What are the main type of catalyst in biological systems?

A

Enzymes

38
Q

What are the differences between fibrous and globular proteins?

A

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
Q

What are the characteristics of enzymes?

A
  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
Q

What is Delta S? How does this relate to enzymes?

A

Entropy, a measure of disorder. The most important factor for enzymes, enzymes work by creating more disorder in their enzymatic structure.

41
Q

What are co-factors?

A

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
Q

What are two types of cofactors and give examples?

A

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
Q

A favored reaction = __________
A disfavored reaction = _________

A

spontaneous
non-spontaneous

44
Q

What enzyme is involved with nucleophilic substitution reactions?

A

Transferases

45
Q

What enzyme is involved with acyl substitution?

A

Hydrolases

Ex: Ester to carboxylic acid

46
Q

What enzyme is involved with redox reactions?

A

Oxidoreductase

47
Q

What enzyme is involved with elimination reactions?

What enzyme is involved with addition reaction?

What enzyme is involved with isomerization?

A

Lyase

Ligase

Isomerase

CHEMISTRY TEST 2 (9 decks)

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