Hemoglobin and Myoglobin Flashcards

1
Q

Why is hemoglobin needed?

A

Oxygen has poor solubility in blood

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2
Q

What occurs to iron in free heme when oxygen binds?

A

Oxygen oxidizes it from Fe2+ to Fe3+

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3
Q

What is methemoglobin (metHb)?

A

Hemoglobin that contains oxidized iron (Fe3+)

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4
Q

What reduces metHb to Hb?

A

Cytochrome b5 reductase (methemoglobin reductase); needs to stop metHb from accumulating

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5
Q

What is methemoglobinemia?

A

When methemoglobin rises higher than 20% in the blood (normally 1%)

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6
Q

What are the two types of inherited methemoglobinemia?

A

Type 1: Defective reductase (recessive)
Type 2: Hemoglobin M; defective hemoglobin (dominant)
Vitamin C is preventative of this disease

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7
Q

How can methemoglobinemia be acquired?

A

Anesthetics
Nitrites (infants consume too many)
Antibodies

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8
Q

What is the Bohr Effect on hemoglobin?

A

Decreasing of local pH decreases the binding of hemoglobin so that oxygen can be released to the cells that need it

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9
Q

What is the Bohr effect on myoglobin?

A

Decreased local pH increases the amount of oxygen transferred to myoglobin

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10
Q

What is the effect of CO2?

A

It decreases pH and forms carbaminohemoglobin stabilizing the T state

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11
Q

What is the effect of 2,3-BPG on hemoglobin?

A

Decreases affinity for oxygen

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12
Q

Where does 2,3-BPG come from?

A

It is an intermediate in glycolysis; increased exercise increases levels of 2,3-BPG causing more oxygen to be released

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13
Q

What is the importance of His E7?

A

Interacts with oxygen to stop it from reacting with the iron; without E7 CO has much higher affinity than O2

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14
Q

Why is important to note about methemoglobin?

A

It cannot bind oxygen

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15
Q

What does hemoglobin do with iron?

A

Doesn’t allow oxygen to oxidize it

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16
Q

What is the importance of His E8?

A

Binds with iron changing conformation from T to R state

17
Q

What does carbonic anhydrase do?

A

CO2 + H2O -> HCO3-