Bioenergetics & Kinetics Flashcards

1
Q

Define entropy

A

The degree of disorder in a system; ΔS = + in a favorable reaction

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2
Q

Define enthalpy

A

Pertains to the total heat content of the system (i.e. internal energy); ΔH = - in a favorable reaction (exothermic; heat is released)

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3
Q

Define free energy

A

Gibb’s free energy measures the favorability/usefulness of a reaction. ΔG = ΔH – TΔS. –ΔG = a favorable reaction that occurs spontaneously.

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4
Q

Define high-energy compounds

A

High-energy compounds generally contain thioester bonds or high-energy phosphate bonds. Energy is released by hydrolysis of high-energy bonds.

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5
Q

Define oxidation-reduction reactions

A

Involves an exchange of electrons. To be reduced is to gain electrons. Measured by reduction potential E, a measure of readiness of molecule to accept electrons. +E = readily accepts (favorable reactions have +E). –E = readily donates. ΔG = -nFΔE.

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6
Q

Define First Law of Thermodynamics

A

Energy can neither be created nor destroyed; it just changes form.

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7
Q

Define Second Law of Thermodynamics

A

The entropy of the universe is always increasing.

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8
Q

What are different forms of energy?

A

Kinetic (thermal, radiant, mechanical, electric) & Potential (stored in chemical bonds, concentration gradients, electric fields, and redox pairs)

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9
Q

What are ‘standard conditions?’

A

1atm, 298K, 1mmol Mg, aqueous environment, pH 7

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10
Q

What is the sign of standard free energy in a favorable reaction under standard conditions?

A

Negative

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11
Q

What are the major high-energy compounds used in biological systems?

A

ATP, acetyl CoA, phosphocreatine, phosphoenolpyruvate

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12
Q

What is the difference between coenzymes and cofactors?

A

Coenzymes are used up in an enzymatic reaction, while cofactors are not.

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13
Q

A coenzyme or cofactor tightly bound to an enzyme is called a ____________. The resulting complex is called a ____________. The protein in isolation is called a _____________.

A

Prosthetic group. Holoenzyme. Apoenzyme.

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14
Q

Are enzymes optimized to bind the substrate, transition state, or product?

A

Transition state

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15
Q

In the Michaelis-Menten equation, what is Km?

A

The substrate concentration at which enzyme velocity is half the maximal

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16
Q

In the Michaelis-Menten equation, what is Kcat?

A

The number of substrate molecules turned over into product per enzyme per second (aka how quickly the enzyme works)

17
Q

What does the value of kcat/km indicate about the efficiency of an enzyme?

A

The higher the value, the more efficient the enzyme

18
Q

What kind of enzyme usually recognizes palindromic DNA sequences?

A

Restriction enzyme

19
Q

Gel electrophoresis separates DNA on the basis of what characteristic?

A

Size

20
Q

SDS-PAGE separates proteins on which basis?

A

Size