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Biochemistry > Enzymes, Mechanisms, Hemoglobin > Flashcards

Enzymes, Mechanisms, Hemoglobin Flashcards

1
Q

Tells us whether a reaction will occur spontaneously

System at equilibrium

A

Thermodynamics

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2
Q

Tells us what the speed (rate) of a reaction will be

System not at equilibrium

A

Kinetics

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3
Q

How does an enzyme increase the rate of a reaction?

A

They recognize a substrate S (the reactant) and speed up its conversion to product P

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4
Q

The standard free energy change under standard conditions

A

ΔG°

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5
Q

What is the equation for Keq?

A

A + B ↔ C + D.

K’eq = [C][D]

[A][B]

so ΔG°’ = -RT lnK’eq

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6
Q

What is the equation for Ka?

A

Ka = H+ [A −]

[HA]

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7
Q

What is the relationship between Ka and pKa?

A

pKa = -logKa

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8
Q

What is the equation for pH?

A

pH = pKa + log ([A −] / [HA])

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9
Q

What is the opposite of a log?

A

10log number

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10
Q

What additional equation is necessary for finding specific concentration of the acid?

A

[HA] = M – A

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11
Q

What will a Ka equation look like given only M?

A

Ka = (x)(x)

(M − x)

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12
Q

What two equations do you need when adding a strong base?

A

[A-] = Mof given base

[HA] = Mof solution − Mof given base

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13
Q

In physical terms, how do enzymes lower the activation energy?

A

All enzymes will lower the activation energy by providing energy derived from weak interactions (H-bonds, hydrophobic interactions, ionic interactions, and Van der Waals forces). This occurs through formation of the ES complex and is called binding energy.

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14
Q

An enzyme conforms to the shape of a substrate

A

Induced fit

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15
Q

Pocket or cleft on the enzyme where the catalytic reaction occurs

A

Active Site

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16
Q

Molecule that binds in the active site and is chemically transformed

A

Substrate

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17
Q

Catalytically active version of an enzyme

A

Holoenzyme

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18
Q

Catalytically inactive version of an enzyme

A

Apoenzyme

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19
Q

Affinity for processing S to P

A

larger kcat/Km

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20
Q

Affinity for binding

A

Small Km

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21
Q

Affinity for processing the fastest

A

large kcat

22
Q

Best overall substrate

A

large kcat/Km

23
Q

Change the equilibrium between the T and R states

A

Effector molecules

24
Q

The enzyme-substrate transition-state complex

Enzymes (typically proteins) are biological catalysts

A

[E] + [S] → [ES] → [E] + [P]

ES

25
Q

What is the y-intercept when looking at a Km Vmax graph?

A

1/Vmax

26
Q

Nucleophile in the active site temporarily forms a covalent bond

A

Covalent Catalysis

27
Q

An amino acid sidechain acts as a proton donor/acceptor

A

Acid-Base Catalysis

28
Q

Can work in multiple ways, electrophile, nucleophile, acid/base etc.

A

Metal ion catalysis

29
Q

Act of bringing two substrates into close proximity at a reactive surface

A

Catalysis by approximation

30
Q

Inhibitor resembles the substrate and binds to the active site thereby preventing binding of the substrate

A

Competitive

31
Q

Inhibitor binds to the enzyme substrate complex created only when substrate binds to enzyme

A

Uncompetitive

32
Q

Inhibitor binds at different site on enzyme (like allosterism).

A

Noncompetitive

33
Q

What type of inhibition is this?

A

Competitive

34
Q

What type of inhibition is this?

A

Uncompetitive

35
Q

What type of inhibition is this?

A

Noncompetitive

36
Q

What type of inhibition is this?

A

Competitive

37
Q

What type of inhibition is this?

A

Uncompetetive

38
Q

What type of inhibition is this?

A

Non-competitive

39
Q

Carries O2 from lungs to tissue Hb-O2 and CO2 and H+ from tissues to lungs HB-CO2/H+.

A

Hemoglobin

40
Q

Where is myoglobin found?

A

Muscles, not RBCs

41
Q

The low oxygen affinity state of the oxygen carrier

A

T-state

42
Q

The oxygen-bound state of the oxygen carrier

A

R-State

43
Q

An increase in blood CO2 concentration leads to a decrease in blood pH and will result in hemoglobin proteins releasing their load of oxygen. Conversely, a decrease in carbon dioxide provokes an increase in pH, which results in hemoglobin picking up more oxygen

A

The Bohr Effect

44
Q

What makes hemoglobin allosteric?

A

multimeric state, sigmoidal V vs S curve, cooperativity

45
Q

Hb can bind __ O2 while Myoglobin can bind __

A

4

1

46
Q

Found in RBCs

Active form is a tetramer

A

Hemogloblin

47
Q

Found in muscle tissue

Active form is a monomer

A

Myoglobin

48
Q

Would equilibrium would be shifted towards the T state or R state of hemoglobin with an increase in O2 concentration?

A

R-State

49
Q

Would equilibrium would be shifted towards the T state or R state of hemoglobin with an increase in CO2 concentration?

A

T-State

50
Q

Would equilibrium would be shifted towards the T state or R state of hemoglobin with a decrease in 2,3-DPG concentration?

A

R-State

51
Q

Would equilibrium would be shifted towards the T state or R state of hemoglobin with an increase in cellular pH (decrease in H+)?

A

R-State

Biochemistry (12 decks)

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