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BCH451 > Chapter 1: Foundations of Biochemistry > Flashcards

Chapter 1: Foundations of Biochemistry Flashcards

1
Q

Who is the father of biochemistry?

A

Albert Lehninger

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2
Q

What are Albert Lehninger’s significant contributions?

A

that the citric acid cycle occurs in mitochondria, mech for oxidative phosphorylation, mitochondrial structure/function, bioenergetics

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3
Q

What does biochemistry study?

A

the chemistry responsible for accelerating reactions, organizing metabolism and signaling in cells, and storing and transferring information

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4
Q

What are the four building blocks of biochemistry?

A

sugars (monosaccharides), lipids (fatty acids), amino acids, nucleotides

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5
Q

Can biological molecules have more than one functional group?

A

Yes! Most biological molecules have several functional groups

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6
Q

What is a structural isomer? Are there differences in properties?

A

the same atoms but different order of bonding, different properties

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7
Q

What is a stereoisomer? Are there differences in properties?

A

molecules with the same chemical bonds but different configuration, different properties

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8
Q

What is an enantiomer? Are there differences in properties?

A

mirror imaged stereoisomer, have identical physical properties and react identically with achiral reagents, BUT may ave different biological activity

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9
Q

What is a diasteromer?

A

not mirror imaged stereoisomer, have different physical and chemical properties

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10
Q

What are the two types of diastereomers?

A

cis and trans geometric isomers

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11
Q

What does cis mean?

A

all groups are on the same side

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12
Q

What does trans mean?

A

all the groups are on the opposite side

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13
Q

Can cis geometric isomers rotate to be trans geometric isomers?

A

No! there is no freedom of rotation due to double carbon bond

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14
Q

How are the interactions between biomolecules specific?

A

macromolecules have unique binding pockets, thus the binding of chiral biomolecules is stereospecific

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15
Q

How does the enzyme hexokinase exhibit stereospecifcity?

A

the enzyme is specific for D-glucose (produced in the body), not L-glucose (made in the lab); this glucose must fit into a pocket of the enzyme and interact via noncovalent interactions

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16
Q

If lexapro is an enantio-pure drug and citalopram is a racemic mixture, what drug is stronger?

A

lexapro

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17
Q

What is a eutomer?

A

the active isomer

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18
Q

What is a distomer?

A

the inactive isomer

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19
Q

Half of all drugs and nearly 90% of recently approved drugs are?

A

racemic mixtures

20
Q

Why are modern drugs usually racemic mictures?

A

cheaper, little to no greater therapeutic benefit

21
Q

In what general cases would only one enantiomer in a drug be required?

A

when the other enantiomer is toxic to the body, when the other enantiomer causes undesirable side effects

22
Q

What is the 1st law of thermodynamics?

A

energy can neither be created nor destroyed

23
Q

What is the 2nd law of thermodynamics?

A

a chemical or physical process goes spontaneously in the direction of greater disorder/entropy

24
Q

What is it called when a reaction breaks down something? Does is produce or consume energy?

A

catabolic, energy-producing

25
Q

What is it called when a reaction synthesizes something? Does is produce or consume energy?

A

anabolism, energy-consuming

26
Q

What three things must living systems do to maintain organization?

A

extract usable energy, release useless energy, and increase entropy in the universe

27
Q

What do all reactions go towards?

A

equilibrium

28
Q

What is ΔG at equilibrium?

A

0

29
Q

What can ΔG tell us about a reaction?

A

which direction the reaction will go as it reaches equilibrium

30
Q

Can ΔG tell us how fast a reaction will proceed?

A

No!

31
Q

What is ΔG(knot)?

A

ΔG at standard conditions of 1 M reactions and products, 25°C, 1 atm, and pH 0

32
Q

What are some things that you can do to speed up a reaction?

A

increase temperature, increase reactant, decrease product, lower activation barrier, couple the reaction to a fast one

33
Q

What is used instead of ΔG(knot) in biochemistry?

A

ΔG(knot)(prime)

34
Q

What does ΔG(knot)(prime) indicate?

A

that the reaction is at the biochemical standard state of pH 7, [H2O] = 55 M

35
Q

What does it mean if the Keq is above 1.0?

A

ΔG is negative and the reaction proceeds forward

36
Q

What does it mean is the Keq is 1.0?

A

ΔG is zero and the reaction is at equilibrium

37
Q

What does it mean if the Keq is below 1.0?

A

ΔG is positive and the reaction proceeds in reverse

38
Q

Why can individual steps in a pathway not be favorable, but the overall pathway is?

A

ΔGs are additive in multistep pathways, the overall pathway must have a -ΔG

39
Q

What can enzymes not do?

A

alter ΔG or go against equilibrium

40
Q

What are the advantages of an enzymatic catalyst?

A

acceleration under mild conditions, high specificity, possibility for regulation, coupling reactions to ATP hydrolysis, avoids side reactions, substrate channeling

41
Q

Why are chemical couplings so important?

A

they allow for otherwise unfavorable reactions by making the overall ΔG negative

42
Q

What are the two steps of ATP group transfer?

A

1) ATP transfers phosphate to substrate, raising its energy (group transfer)
2) the phosphate leaves the substrate, making it go back to a lower energy state

43
Q

What is a metabolic pathway?

A

a pathway that produces energy or valuable materials

44
Q

What is a signal transduction pathway?

A

a pathway that transmits information

45
Q

Where is the most common point of regulation?

A

at the first enzyme in a pathway

BCH451 (3 decks)

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