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Biochemistry > Biologic Oxidation > Flashcards

Biologic Oxidation Flashcards

1
Q

Oxidation-reduction taking place in the cell

A

Biologic oxidation

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2
Q

Energy producing reaction in living cells involving transfer of H atoms

A

Biologic oxidation

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3
Q

In 2H2+O2 —> 2H2O + heat, which is oxidized and reduced?

A

H2 is oxidized

O2 is reduced

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4
Q

Controlled reaction of hydrogen with oxygen to form energy and water

A

Respiration

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5
Q

The cell stores energy instead of dissipating heat in the form of…

A

ATP

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6
Q

Product of oxidation-reduction reaction

A

Redox potential (E’o)

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7
Q

This is the tendency of reactants in redox reaction to donate or accept electrons

A

Redox potential (E’o)

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8
Q

Form electrical energy due to movement of electron

A

Redox potential (E’o) - volts

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9
Q

Pairs of redox potentials

A

Oxidized form and reduced form

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10
Q

True or false. Heat energy (kJ) —> electric energy (volts) in redox potential which is consistent with the first law of thermodynamics

A

True

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11
Q

Enzyme responsible for movement of electron from one substrate to another

A

Oxidoreductases (class 1)

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12
Q

The prediction of the direction of flow of electrons

A

Relative position of the redox systems

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13
Q

True of false. The more negative the redox potential, the lesser the capacity to donate an electron

A

False

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14
Q

Enzymes of biological oxidation

A 
Oxidases
Dehydrogenases
Hydroperoxidases
Oxygenases
Superoxide dismutase
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15
Q

Catalyze the removal of hydrogen from substrate using oxygen as hydrogen acceptor

A

Oxidases

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16
Q

Product of oxidase reaction

A

Water or hydrogen peroxide

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17
Q

Last enzyme in ETC

A

Cytochrome oxidase

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18
Q

Enzyme with two atoms of Cu oresent, each associated with a heme unit

A

Cytochrome oxidase

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19
Q

Terminal component of the chain of respiratory carriers found in mitochondria

A

Cytochrome oxidase

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20
Q

Cytochrom oxidase is poisoned by..

A

Carbon monoxide
Cyanid
Hydrogen sulfide

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21
Q

Give examples of Flavoproteins

A

L-amino oxidase
Xanthine oxidase
Aldehyde dehydrogenase

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22
Q

FMN-linked enzyme found in the kidney

A

L-amino oxidase

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23
Q

For oxidative deamination of naturally occurring L-amino acids

A

L-amino oxidase

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24
Q

Contains molybdenum

A

Xanthine oxidase

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25
Q

Plays an important role in the conversion of purine bases to uric acid

A

Xanthine oxidases

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26
Q

FAD-linked enzyme present in mammalian livers which contains molybdenum and nonheme iron protein

A

Aldehyde dehydrogenase

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27
Q

Acts upon aldehyde and N-heterocyclic substrate

A

Aldehyde dehydrogenase

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28
Q

Catalyze the transfer of hydrogen from one substrate to another in a coupled oxidation-reduction reaction

A

Dehydrogenases

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29
Q

Cannot use oxygen as hydrogen acceptor

A

Dehydrogenases

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30
Q

In dehydrogenases, what acts as hydrogen acceptor by acting as an intermediate carrier of electrons

A

Coenzymes

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31
Q

2 types of dehydrogenases

A

NAD-linked

NADP-linked

32
Q

Difference between NAD-linked and NADP-linked

A

NAD-linked is oxidative patway

NADP-linked is reductive synthesis

33
Q

Dehydrogenases found characteristically in biosynthetic pathways

A

NADP-linked dehydrogenases

34
Q

Main pathway for the generation of reducing equivalents, in the form of NADPH

A

Pentose phosphate pathway (PPP)

35
Q

Active in liver, adipose tissue. Adrenal cortex, thyroid, erythrocytes, testis, lactating mammary gland

A

PPP

36
Q

True or false. NADP is utilized by tissues in reductive synthesis (PPP)

A

False

NADPH

37
Q

Pathways utilizing NADPH

A

Fatty acid synthesis

Steroid synthesis

38
Q

In fatty acid synthesis, which are reduced by NADPH

A

3 ketoacyl

2,3 unsaturated acyl derivatives

39
Q

In steroid synthesis, what enzyme utilizes NADPH as reducing equivalents

A

Steroid reductases

40
Q

This riboflavin linked dehydrogenase has a systematic name of NADH-Q oxidoreductase in complex 1 of ETC

A

NADH dehydrogenase

41
Q

Catalyzes electron transfer from NADH to Q, coupled with the transfer of four H+ across the membrane

A

NADH dehydrogenase

42
Q

Acts as carrier of electrons between NADH and the components of higher redox potential

A

NADH dehydrogenase

43
Q

Riboflavin linked dehydrogenases that transfer reducing equivalents directly from the substrate to the ETC

A

Succinate dehydrogenase
Acyl-coA dehydrogenase
Mitochondria glycerol-3 phosphate dehydrogenase

44
Q

Dehydrogenation of reduced lipoate, an intermediate on the oxidative carboxylation of pyruvate and alpha keto glutarate

A

Dihydrolipoyl dehydrogenase

45
Q

Intermediate carrier of electrons between acyl coA dehydrogenase and ETC

A

Electron transferring flavoprotein

46
Q

Iron containing hemoproteins involved as carriers of electrons from flavoproteins to cytochrome oxidase

A

Cytochromes

47
Q

2 enzymes of hydroperoxidases

A

Peroxidases

Catalases

48
Q

Plays an important role in protecting the body against harmful effects of reactive oxygen species (ROS)

A

Hydroperoxidases

49
Q

Highly reactive oxygen containing molecules like peroxides which are formed during normal metabolism

A

Reactive oxygen species

50
Q

A hydroperoxidase found in milk and in leukocytes, platelets, and other tissues involved in eicosanoid metabolism

A

Peroxidases

51
Q

Prosthetic group of peroxidases

A

Protoheme

52
Q

Electron acceptor of peroxidases (eg. Vitamin C, quinones, cytochrome c)

A

Hydrogen peroxide

53
Q

Dependent on the supply of NADPH which in erythrocytes are formed via the PPP

A

Glutathione peroxidase

54
Q

Prostehetic group of glutathione peroxidase

A

Selenium (contains selenocysteine in active site)

55
Q

A hemoprotein containing four heme groups

A

Catalase

56
Q

Catalyzes the breakdown of H2O2 formed by the actionof oxygenases to water and oxygen

A

Catalases

57
Q

Electron acceptor and donor of catalases

A

H2O2

58
Q

Catalyzes the incorporation of oxygen into a substrate molecule

A

Oxygenases

59
Q

2 groups of oxygenases

A

Monooxygenase

Dioxygenase

60
Q

Oxygenase that utilizes both O2

A

Dioxygenase

61
Q

Enzymes of dioxygenases

A

Homigentisate dioxygenase
3 hydroxyanthranilate dioxygenase
L-tryptophan dioxygenase

62
Q

Oxygenase where only one atom of O2 is utilized and the other becomes water

A

Monooxygenase

63
Q

Participate in ETC where alectrons are passed in two types of reaction involving FAD or FMN

A

Cytochrome P450

64
Q

Hydroxylation reaction by cytochrome p450 is re oxidized through…

A

Hydroxylase cycle

65
Q

Anion free radical that resulted from transfer of a single electron to oxygen

A

Superoxide

66
Q

Formed when reduced flavins are reoxidized by molecular oxygen

A

Superoxide

67
Q

Enzyme used to ease the formation of superoxide from oxygen in tissues

A

Superoxide dismutase

68
Q

Enzyme responsible for the removal of superoxide anion free radical

A

Superoxide dismutase

69
Q

Chain breaking antioxidant in vivo

A

Superoxide dismutase

70
Q

Acts in aqueous phase to trap super oxide free radicals

A

Superoxide dismutase

71
Q

Acts in the lipid phase to trap ROO- radicals

A

Urate and vitamin e

72
Q

Can reduce oxidized cytochrome c or be removed by superoxide dismutase

A

Superoxide

73
Q

Enzymes in ETC

A

NADH dehydrogenase
Succinate dehydrogenase
Q-cyt, oxidoreductases & Q cycle
Cytochrome dehydrogenases & cytochrome oxidase

74
Q

NADH + H+ + Q ———————> NAD + QH2

A

NADH dehydrogenase

75
Q

SUCCINATE ————————>FUMARATE

A

Succinate dehydrogenase

76
Q

QH2 + 2Cyt c(oxidized) ———-> Q + 2Cyt c(reduced)

A

Q-cyt oxidoreductases and q cycle

77
Q

4Cyt c (reduced) + O2 —–> 4Cyt c (oxidized) + 2H2O

A

Cytochrome dehydrogenases and cytochrome oxidase

Biochemistry (2 decks)

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