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Biology 1001 > section 5 > Flashcards

section 5 Flashcards

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AP® Biology flashcards Biology 101 flashcards
1
Q

metabolism

A

all the life-sustaining reactions going on in an organism

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2
Q

anabolic reactions

A

simple to complex reactions. Biosynthetic. energy input required for this

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3
Q

how much energy is there for products compared to reactants in anabolic/ biosynthetic reactions

A

products have more energy than reactants in anabolic reactions

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4
Q

catabolic reactions

A

breakdown reactions. complex to simple. energy is released

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5
Q

what is an example of a catabolic reaction

A

hydrolytic reactions: breakdown of polymers into monomers

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6
Q

energy

A

the capacity to do work or cause change. rearranges collection of matter

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7
Q

heat energy

A

thermal energy released or transferred from one object to another

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8
Q

chemical energy

A

the potential energy stored in the chemical bonds of molecules (ATP)

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9
Q

radiant energy

A

light energy

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10
Q

nuclear energy

A

energy in atoms

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11
Q

The first law of thermodynamics

A

energy can be transferred and transformed but cannot be destroyed or created. living organisms are energy transformers but not energy creators

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12
Q

the second law of thermodynamics

A

energy transfers or transformations increase the entropy of the universe. in reactions in the body order will be increased locally but will be decreased in the universe

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13
Q

entropy

A

disorder

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14
Q

what happens to a small amount of heat during transfers and transformations

A

in every energy conversion, some energy becomes unusable and is no longer available to do works it is lost in form of heat and small molecules which dissipate

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15
Q

is a process that leads to increased entropy favourable or not favourable

A

it is favourable. proceeds without the input of energy. breakdown of things. they are spontaneous

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16
Q

Gibbs free energy

A

the energy available to do work

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17
Q

why is some energy unusable in molecules?

A

because there is an entropy requirement

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18
Q

exergonic

A

reactions, where the molecules produced, have less energy than the free energy in the reactants

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19
Q

what is an ERG

A

10 joules

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20
Q

are exergonic reactions spontaneous or not and are the produces less stable or more stable

A

they are spontaneous and catabolic. the products are more stable

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21
Q

the trend of G and the ability to do work

A

the less G is, the more stable the system is and the higher capacity to do work

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22
Q

what is the structure of ATP

A

ribose sugar
adenine
chain of three phosphate groups (triphosphate)

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23
Q

what is ATP broken down into during hydrolysis reactions?

A

ADP and inorganic phosphate

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24
Q

is the breakdown of ATP and H2O exergonic?

A

yessir

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25
Q

how do we deal with the loss of energy in the breakdown of ATP

A

the catabolic reaction is coupled with an anabolic reaction. the released energy of the catabolic reactions is captured by anabolic reactions.

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26
Q

what are the three types of work that need energy input from the hydrolysis of ATP?`

A
  1. chemical work
  2. transport work
  3. mechanical work
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27
Q

what is the delta G for ATP hydrolysis?`

A

-30.5kj/mol

28
Q

how can we do anabolic reactions and still follow the rules of thermodynamics?

A

by coupling anabolic reactions (building complex materials) with catabolic reactions (the breakdown of things)

29
Q

why don’t spontaneous reactions happen spontaneously in biological systems?

A

because chemical reactions involve the breaking of bonds and forming bonds. changing molecules involves contorting molecules into unstable formations so the bonds can be broken and configured into something new. This means that we need an initial input of energy to get bonds into this unstable form. This is the activation energy

30
Q

what is used for activation energy in non-biological systems and why is it inappropriate to use in biological systems

A

heat. it is inappropriate because
1. it’s indiscriminate: does not only affect the part you’re working on. it affects everything
2. damaging: organisms function within a preferred range of temp. higher temps denature proteins, destroy membranes, and the organism dies

31
Q

what enzyme is not a protein

A

riboenzymes

32
Q

does enzyme shape change after it catalyzes a reaction?

A

no, enzymes speed up a reaction without being changed or used up by the reaction

33
Q

how do enzymes work in reactions?

A

enzymes work to lower the activation energy barrier. this happens at the active site. reactants fit into the active site to form an enzyme-substrate complex and the enzyme closes upon the substrate.

  1. they line up reactants in the way that reactions are facilitated
  2. pull and contort substrates into their transition to destabilize them
  3. active site provides microenvironment good for reaction (pH etc)
  4. enzymes briefly covalently bond with parts of the reactants
34
Q

active site

A

a location on the enzyme that is a perfect structural fit for the reactant

35
Q

relation of AE and bond strength

A

activation energy is proportional to the difficulty in breaking bonds. stressing the bonds makes them easier to break and lowers the activation energy which is what enzymes do

36
Q

what is the rate of reaction a function of

A

the concentration of substrates and the number of enzymes. adding substrates increases reaction rate until a certain point when you will have to add more enzymes

37
Q

when is an enzyme denatured

A

when it has moved too far away from its optimal conditions.

38
Q

enzyme optimal conditions

A

the specific range of conditions when an enzyme is in its most active 3D configuration (pH, temp presence/ absence of cofactors)

39
Q

what is the ph that most enzymes work in

A

6-8

40
Q

the pH of pepsin- stomach

A

2

41
Q

the pH of trypsin- small intestine

A

8

42
Q

what are the two cofactors?

A
  1. inorganic cofactors (metal ions such as zinc)

2. organic coenzymes

43
Q

where are inorganic cofactors found on enzymes

A

might be permanently bound or reversibly bound along with the substrate

44
Q

what are coenzymes

A

vitamins

45
Q

enzyme inhibitors

A

molecules that prevent enzymes from working properly

  1. competitive inhibitors
  2. non-competitive inhibitors
46
Q

competitive inhibitors

A

bind reversibly onto the active site and can be dealt with by increasing the concentration of substrate so it can compete more effectively for the active site

47
Q

non-competitive inhibitors

A

bind somewhere other than the active site and distort the 3D shape of the enzyme, therefore, rendering the active site less effective or non-functional. maybe reversible. can be useful such as in the case of negative feedback

48
Q

example of non-competitive inhibitors

A

negative feedback things.

49
Q

irreversible inhibition

A

this is the case for poisons and toxins

50
Q

how can irreversible enzyme inhibitors work to our benefit

A

antibiotics alter or block active sites on the enzymes of bacteria. e.g. penicillin inhibit enzymes involved in bacterial cell wall production

51
Q

what are nerve agents and give an example

A

sarin gas: binds to R group on amino acid sarine (on active site of acetylcholinesterase) this leads to your nerves continuously firing and leads to loss of muscle control, paralysis, respiratory failure and death

52
Q

what is the principle process of regeneration

A

cellular respiration

53
Q

what are the three ways to regenerate ATP

A
  1. cellular respiraton
  2. anerobic respiration
  3. fermentation
54
Q

where do electrons go in redox reactions?

A

to the more electronegative atom

55
Q

what does the relocation of electrons do?

A

releases energy

56
Q

what are chemicals that get electrons called

A

oxidizing agents

57
Q

what are chemicals that give electrons called

A

reducing agents

58
Q

how much potential energy do electrons that are with less electronegative chemicals have

A

they have more potential energy since energy is required to be inputted to pull electrons away from strongly electronegative atoms

59
Q

is energy inputted or released when electrons go from less to more electronegative chemicals

A

the potential energy is released in a stepwise fashion by a series of controlled redox reactions with a bit of energy released at each step to work

60
Q

what does it mean to be an excellent source of hilltop molecules?

A

organic molecules that have an abundance of hydrogen are called hilltop molecules

61
Q

what are the three stages of cellular respiration?

A
  1. glycolysis
  2. oxidation of pyruvate followed by the citric acid cycle (Kreb’s cycle)
  3. oxidative phosphorylation electron transport and chemiosmosis
    the 2nd and 3rd parts take place in the mitochondria and the first part is in the cytosol
62
Q

where does glycolysis take place?

A

in the cytosol

63
Q

what are the reactants in glycolysis?

A

2NAD+ and 2ATP and glucose

64
Q

what are the products of glycolysis?

A

2ATP, 2NADH and 2Pyruvate and hydrogen ions

65
Q

what is substrate-level phosphorylation?

A

a process whereby a phosphate group is transferred to ADP from another molecule by an enzyme. a substrate carrying the phosphate group goes into an enzyme with an ADP molecule and the produce is ATP. 4 ATP are produced but two are used so the net gain is 2.

66
Q

where does the citric acid take place?

A

in the mitochondrion matrix

Biology 1001 (4 decks)

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