Bioenergetics & Enzymes Unit 4 Flashcards

1
Q

Define metabolism.

A

Consists of all the chemical reactions by which organisms transform matter & energy

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2
Q

What two(2) metabolic pathways are there?

A

Catabolic pathways, and Anabolic pathways

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3
Q

Define catabolic pathways.

A

The release of energy by breaking down complex molecules into simpler molecules (cellular respiration)

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4
Q

Define anabolic pathways.

A

The consumption of energy by using simple molecules to build more complex molecules (photosynthesis)

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5
Q

What is free energy?

A

Any available energy to do work

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6
Q

What is work?

A

Any change in motion or position, other than the change of random motions of particles (heat)

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7
Q

What are the two(2) chemical reactions that have a characteristic ‘free energy change’?

A

Exergonic & endergonic

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8
Q

Define Exergonic free energy change.

A

Reactions that release free energy, these occur spontaneously, w/o a source of free energy outside the system

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9
Q

Define Endergonic free energy change.

A

Reactions that absorb free energy, but do not occur spontaneously. They must be coupled w/ a exergonic reaction, or process outside of the system

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10
Q

What three(3) characteristics need to be known for a reaction?

A

Temperature, Heat released or absorbed, and the entropy change (increase or decrease of disorder)

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11
Q

What are the two(2) different types of physical work in cells w/ definition?

A

Transport work, & mechanical work (both require a free energy source)

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12
Q

What is an example of chemical work?

A

Linking glucose molecules together

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13
Q

What is ATP?

A

(adenosine triphosphate, one of the four ribonucleotides) is used as one of the monomers in the synthesis of RNA, but also used as an energy carrier in cells, picking up energy from exergonic reactions and processes, and giving up some energy to endergonic reactions and processes to make them go.

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14
Q

What type of reaction is the hydrolysis of ATP?

A

An exergonic reaction

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15
Q

What does the hydrolysis reaction of ATP look like?

A

ATP + H2O–>ADP + Pi G’o= -30.5 kJ/mol

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16
Q

Although the hydrolysis of ATP is exergonic, and therefore is a spontaneous reaction, the reaction has a high activation energy and will not happen without being catalysed by an enzyme. What is the name of this enzyme?

A

ATPases (speeds up reaction)

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17
Q

What is the opposite reaction of ATP hydrolysis?

A

ATP synthesis

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18
Q

What type of reaction is ATP synthesis?

A

Endergonic reaction

19
Q

What is the ATP cycle?

A

The linking of cellular exergonic and endergonic processes by ATP hydrolysis and ATP synthesis

20
Q

What kind of reaction can happen when an endergonic reaction is coupled w/ ATP hydrolysis?

A

An exergonic reaction

21
Q

What are enzymes, what do they do, and give an example.

A

Enzymes are proteins that catalyse biochemical reactions, increasing the reaction rate enormously. RNA molecules: ribozymes

22
Q

How do enzymes work to increase reaction time?

A

They lower the activation energy of the reaction

23
Q

Although enzymes do speed up reactions, what do they not affect?

A

The deltaG of reactions whether exergonic or endergonic

24
Q

Why are enzymes so important?

A

Cells can control what reactions happen and their rate by altering the identity and amount of the enzymes they produce

25
Q

Are enzymes selective of where they bind?

A

Yes, very, as they only bind with one or a few different substrates (active sites) where catalysis takes place

26
Q

What happens to the active site shape upon substrate binding w/ the enzyme?

A

It changes its shape, induced fit (conformational change)

27
Q

What happens to the enzyme and substrate post reaction?

A

They regenerate with no net change, further ready for more catalytic cycles

28
Q

What factors effect enzyme activity? (5)

A

Substrate concentration, pH, temperature, cofactors, & inhibitors/activators

29
Q

Are enzymes saturable? Explain why?

A

There are finite locations of active sites on an enzyme, they have a maximum rate of processing substrates

30
Q

Why is temperature so important to enzyme activity?

A

There is an optimal, to low and the reaction cannot happen or is slow. To high and the enzyme may not be able to react at all

31
Q

Why is pH important to enzyme activity?

A

There is an optimal pH, to low and its slow or doesn’t occur, to high and it also cannot take place

32
Q

What are enzyme cofactors?

A

Small non-proteinaceous molecules required by some enzymes for their catalytic activity (non-active alone)

33
Q

What are the molecules called that can turn down, or turn up enzyme activity?

A

Inhibitors & activators (competitive and non-competitive inhibitors for active site location)

34
Q

What is an allosteric enzyme?

A

An enzyme w/ four active sites

35
Q

Enzyme Info.

A

Enzymes act sequentially in regulated metabolic pathways. An example of a control circuit: the product of a pathway inhibits the first enzyme of the pathway (feedback inhibition).

36
Q

What are oxidation and reduction reactions?

A

Oxidation- the loss of electrons (either entire, or shares)

Reduction- the gain of electrons (either entire, or shares)

37
Q

How electrons often transferred?

A

Via H atoms (1 proton, 1 electron), least electronegative atom

38
Q

What compounds are common electron carriers?

A

NADH, NADPH, & FADH^2

39
Q

Why is electron transfer important in energy economy of the cell?

A

B/C electron transfer may absorb or release free energy during oxidation & reduction reactions

40
Q

What is the difference between energy transfer in the form of heat, and energy transfer in the form of work?

A

Energy transfer in the form of heat increases the random motion of particles such as molecules and atoms. Work, however, brings about any other kind of change, such as chemical work, transport work, and mechanical work.

41
Q

Thermodynamically speaking, how can ATP hydrolysis drive reactions that would not otherwise happen? How, in specific molecular terms, is this often done?

A

ATP hydrolysis is an exergonic process. When it is coupled with an endergonic process, the combined 􏰂G might be negative, and so the combined reaction would be thermodynamically favourable.

42
Q

Why do enzymes have saturation kinetics?

A

A given quantity of enzyme will have a finite number of active sites, each taking a certain amount of time to process substrates. When the substrate concentration reaches a high enough value that a new substrate molecule diffuses to the active site the moment the products from the previous catalytic cycle are ejected, further increases in substrate concentration will have no effect on the rate of reaction.

43
Q

a) Why does the rate of an enzyme-catalyzed reaction increase with increasing temperature up to the optimum temperature? b) Why does the rate of reaction fall when the optimum temperature is exceeded?

A

a) As the temperature rises, substrates diffuse into active sites more quickly, and the collisions of molecules are more violent; the activation
Bioenergetics and Enzymes - 10
energy is reached by a greater proportion of molecules at a given moment, so the reaction rate increases.
b) The enzyme denatures.

44
Q

What are the enzymes that catalyze ATP hydrolysis?

A

ATPases