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Chronic Disease > Basic Metal Biochemistry > Flashcards

Basic Metal Biochemistry Flashcards

1
Q

Why are metals important for human function?

A

Nearly 50% of proteins require a metal for function.

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2
Q

How do metals exist within the body?

A

As a salt or bound up in protein but always containing a charge.

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3
Q

Which metallic form in the body releases the most energy?

A

The compound form

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4
Q

What is the amount of energy release by a metal directly proportional to?

A

The stability of the compound.

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5
Q

What happens when a protein forms around a metal?

A

Forms an exothermic stable lattice structure.

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6
Q

What does it mean if a metal-containing protein is very exothermic?

A

Very stable,

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7
Q

What things do we need to consider when testing the stability of a metal-containing compound?

A

Amount of energy to ionise the metal

Amount of energy released when the compound forms, as lattice energy (solids) or hydration enthalpy (solutions)

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8
Q

What kind of metallic reactions mostly do not occur in the body?

A

Large endothermic

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9
Q

What is metal centre geometry?

A

Arrangement of the protein primary and secondary coordination sphere around the metal.

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10
Q

What is important about the metal centre geometry?

A

Tune the properties of the metal to aid reactivity and selection.

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11
Q

How does haem attach to the RBC?

A

Attached to the unoccupied ligand.

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12
Q

Which residue binds to iron?

A

Cysteine

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13
Q

What are the functions of metals in the body?

A

Structural

Catalytic

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14
Q

How are metals used structually?

A

Can aid the correct folding of structures.

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15
Q

What deficiencies lead to Alzheimer’s?

A

Zn and Cu

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16
Q

What does zinc anaemia lead to?

A

Growth rertardation

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16
Q

What metal cluster does aconitase contain?

A

Iron

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16
Q

Which metal stabilizes DNA?

A

Zinc

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16
Q

What is the function of aconitase?

A

Responsible for the stereospecific isomerisation of citrate to isocitrate.

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17
Q

What is the function of superoxide dismutase (SOD)?

A

The disproportion of superoxides, this protects the cell from harm.

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17
Q

How does aconitase work?

A

Leave one iron solvent-exposed to bind to the reactant.

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17
Q

Which metals does SOD contain?

A

Copper and zinc

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17
Q

What is the function of zinc in SOD?

A

Structural element

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17
Q

Where are metals limited?

A

Oceans

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17
Q

What is the function of copper in SOD?

A

Catalytically active metal

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17
Q

Why does metal content differ between species?

A

Environment availablity

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17
Q

What is the reduction stratergy?

A

Reducing Fe3+ back down to 2+

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17
Q
A
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17
Q

What is chelation?

A

PS binds to Fe3+ allowing it to move back into the cell where it will be reduced.

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18
Q

What are the evolutionary mechanisms for acquiring iron?

A

Reduction strategy

Chelation

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18
Q

What evolutionary tactic is the last resort?

A

Changing the metal used or the amount required.

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18
Q

What is the Irving-Williams Series?

A

The order of metal strength.

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18
Q

Which is the weakest metal in the body?

A

Mg(II)

19
Q

What does it mean if a metal is weak?

A

Bound so can release copart easily.

19
Q

Which metal is the strongest?

A

Zn(II)

20
Q

What does it mean when a metal is strong?

A

More structural non-catalytic binding structure.

21
Q

What is the ligand -strong theory?

A

How closely bound the ligand is to the metal.

22
Q

How is metal binding controlled in the body?

A

Cells must have a mechanism to make sure the correct metal gets to the protein.

23
Q

What happens when spores enter an immunocompromised patient?

A

Spores can cross the blood-brain barrier due to urease activity.

Cobalt forces out urease.

24
Q

Why can metals lower (eg. Colbalt) displace metals higher on the Irving-Williams Series?

A

Larger concentrations can outcompete metals higher in the series.

25
Q

What is the effect of metals on oxidative stress?

A

Metals drive the transformation of hydrogen peroxide during the Fenton reaction causing oxidative stress.

26
Q

What are radicals?

A

Radicals can react with anything and cause damage.

27
Q

What are antioxidants?

A

We take them to remove radicals.

28
Q

How does the replacement of metals lead to the loss of activity or function?

A

Higher-function metals can have the same structural function but no catalytic function.

29
Q

What is the protoporphyrin example of metal replacement function loss?

A

Iron can be subbed with zinc, it is structural so there is no more catalytic function , this leads to anemia.

30
Q

Why is zinc protoporphyrin important?

A

Can be quantified to test for anaemia.

31
Q

How are metals transported into the cell?

A

By recycling or dietary uptake.

32
Q

What are the mechanisms needed for each biological metal?

A

Sensing how much is in the cell and how much is needed.

Distribute metal to the correct location.

Store, export or prevent uptake of excess metals.

33
Q

What distributes metals to the correct location?

A

Chaperones

34
Q

Why do we need to keep metals at homeostasis?

A

Ensure metal need is met and nay free cellular metal does not cause oxidative stress or inhibit protein function.

35
Q

Which transporters move Mg?

A

MgtA

CorA

36
Q

Which transporter moves manganese?

A

MntH (NRAMP)

37
Q

Which transporters move Iron?

A

FhuA-E

FepA-E

FecA-E

EfeU/O/B

FeoA/B

38
Q

Which transporters move nickle?

A

NikA-E

RcnA

39
Q

Which transporter moves colbalt?

A

RcnA

40
Q

Which transporters move zinc?

A

ZupT

ZnuA

ZntA

Yiip

ZitB

41
Q

What transporters move copper?

A

CopA

CusA-C

42
Q

What acts as sensors in metal homeostasis?

A

Transcription factors

43
Q

How does metal sensing work?

A

Metal binding causes an allosteric change,

44
Q

How does binding sensitivity change depending on the metal?

A

Increases moving up the Irving Williams series meaning the transcription factors are more sensitive.

45
Q

Which Transcription factors regulate iron concentration in the cells?

A

Aft1/2

46
Q

How do aft1/2 control the concentration of iron?

A

Fe-S signal relay caused by aft1/2 moves iron out of the nucleus.

When there is no Fe cluster, there is no signal relay and therefore concentration is maintained.

47
Q

What maintains the concentration of copper?

A

Apo Mac1

48
Q

How does Apo Mac1 control the concentration of Copper?

A

Apo Mac1 seeks out copper, the binding inactivates Mac1.

49
Q

Why does yeast need copper to survive?

A

To survive DNA damage.

50
Q

What is CTR1?

A

A copper transporter.

51
Q

How does copper prevent DNA damage in yeast?

A

MethylMethaneSulfonate (MMS) methylates N7-guanine residue.

When copper is complimented it binds to the damaging agent preventing the damage.

52
Q

What is MethylMethaneSulfonate (MMS)?

A

A DNA damaging agent.

53
Q

What is MTF1?

A

Human metal-responsive transcription factor

54
Q

What is Metallothionine (MT)?

A

Protectant against Cadmium.

55
Q

How does MT protect against Cadmium toxicity?

A

Cadmium displaces Zinc on MT, the zinc then binds to MTF1 activating the transcription of Metallothionine which removes more Cd.

56
Q

What is transporter degardation?

A

Turning off the import of metals.

57
Q

When are ZIP transporters present?

A

High concentrationsW

58
Q

When are transported degraded?

A

When the concentration drops the ZIP transporters are endocytosed and cleaved.

When the concentration is low the ZIP transporter is degraded.

59
Q

What is hepcidin?

A

Regulates Ferroportin (FPN) release and regulates iron in the cell.

60
Q

What is ferroportin?

A

An iron exporter.

61
Q

What are metal chaperones?

A

Involved in the delivery of the right metal to the protein.

62
Q

How to chaperones work?

A

Binding to the metal prevents it from binding else where until it is in the right place.

63
Q

How does compartmentalisation help metal homeostasis?

A

Keeps metals in their place and prevents travel to unnecessary places.

64
Q
A

Chronic Disease (15 decks)

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