Exam 2 Flashcards

1
Q

What does Cellular Respiration do?

A

turn FOOD energy into STORED energy

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2
Q

Kinetic energy is the energy of ___?

A

motion

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3
Q

Conservation of Energy

A

Energy cannot be created or destroyed, but is converted from one form to another

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4
Q

Chemical Energy is a form of __.

A

Stored energy

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5
Q

Products of Cellular Respiration:

A

Heat, Carbon Dioxide, Water

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6
Q

In the combustion of glucose with oxygen to form water and carbon dioxide (C6H12O6 + 6O2 –> 6CO2 + 6H2O), the entropy of products is ___ than the entropy of reactants.

A

greater

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7
Q

Facts about equilibrium:

A
  1. Lowest free energy state
  2. Most stable configuration for a reaction
  3. If a reaction is at equilibrium, it is not capable of doing work.
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8
Q

The Delta G for a reaction at equilibrium is __, so there is no ____ energy available to do any work.

A

Zero, free

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9
Q

When potential energy of products is less than that of reactants, heat ______

A

is released into the environment

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10
Q

Exergonic

A

Spontaneous, heat is released

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11
Q

Endergonic

A

Products have more potent energy, requires net input of energy from surroundings

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12
Q

What is usually the immediate source of energy for an endergonic reaction?

A

ATP. The hydrolysis of ATP provides the energy needed for an endergonic reaction

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13
Q

Equation with endergonic energy acquired:

A

ADP + P –> ATP

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14
Q

Where is one place that energy for endergonic reactions can come from?

A

Energy coupling, basically the exergonic reactions

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15
Q

What is the fate of phosphate group removed when ATP is converted to ADP?

A

It is acquired by a reactant in an endergonic reaction. By acquiring the phosphate group the reactant acquires energy.

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16
Q

Model of ATP (Adenosine triphosphate)

A

3P, Ribose, and Adenosine A group

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17
Q

What does hydrolysis do in terms of ATP

A

Hydrolysis breaks the bonds that join the phosphate groups in an ATP molecule.

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18
Q

Irreversible Inhibitors do what?

A

Permanently render an enzyme inactive. Example: Penicillin

19
Q

How to overcome competitive inhibitors

A

Add more Substrates

20
Q

A ___ inhibitor has a structure that is so similar to the substrate that it can bond to the enzyme just like the substrate

A

competitive

21
Q

A ___ inhibitor binds to a site on the enzyme that is not the active site.

A

non-competitive

22
Q

Usually, an ____ inhibitor forms a covalent bond with an amino acid side group within the active site, which prevents the substrate from entering the active site or prevents catalytic activity

A

irreversible

23
Q

The competitive inhibitor competes with the substrate for the ______ on the enzyme

A

active site

24
Q

When the noncompetitive inhibitor is bonded to the enzyme, the shape of the ___ is distorted

A

enzyme

25
Q

Enzyme inhibitors disrupt normal interactions between an enzyme and its ____

A

substrate

26
Q

An enzyme is ___ when it loses its native conformation and its biological activity

A

denatured

27
Q

An enzyme is considered a ___ because it speeds up chemical reactions without being used up

A

catalyst

28
Q

An enzyme is considered ___ because of its ability to recognize the shape of a particular molecule

A

specific

29
Q

A ____, such as a vitamin, binds to an enzyme and plays a role in catalysis.

A

Vitamin

30
Q

When properly aligned, the enzyme and substrate form an enzyme substrate ____

A

complex

31
Q

A substrate binds to an enzyme at the ______, where the reaction occurs

A

active site

32
Q

In a catalyzed reaction a reactant is often called a _____

A

substrate

33
Q

prefix: kin (kinet)

A

moving

34
Q

prefix: allo

A

other

35
Q

prefix: trans

A

across

36
Q

prefix: therm

A

heat

37
Q

prefix: ase

A

enzyme

38
Q

prefix: sub

A

under/below

39
Q

prefix: lac (lact)

A

milk

40
Q

prefix: glyc

A

sweet

41
Q

prefix: trop

A

change, turn, move

42
Q

prefix: extra

A

outside of

43
Q

What is glycolysis

A

the breakdown of glucose by enzymes, releasing energy and pyruvic acid.