protein hemoglobin and myoglobin part 1 Flashcards

1
Q

where is myoglobin located

A

in the muscle

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2
Q

where is hemoglobin located

A

in red blood cells

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3
Q

how many subunits does hemoglobin have

A

4 homologous Mb like subunits

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4
Q

what was the first protein whose 3d structure was determined by x ray crystallography

A

myoglobin

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5
Q

how many helices does myoglobin have

A

8 alpha helices labeled A through H

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6
Q

what is myolglobin

A

a monomer

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7
Q

what is hemoglobin

A

a tetramer

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8
Q

how many alpha and beta subunits does hemoglobin have

A

2 alpha and 2 beta

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9
Q

who solved Hb’s structure

A

Max perutz

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10
Q

what is a heme made of

A

protoporphyrin IX + Fe+2

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11
Q

what do Mb and Hb’s 4 subunits contain

A

a heme prosthetic group

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12
Q

what is heme prosthetic group

A

non amino acid portion of a protein that is required for biological activity

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13
Q

what is the octahedral coordination complex

A

the O2 binding pocket in heme

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14
Q

what amino acid is involved in the octahedral coordination complex

A

His F8

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15
Q

what does His E7 do in O2 binding pocket in heme

A

forces any ligand binding to Fe(II) to bind at a bent angle

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16
Q

what does the bent angle for His E7 allow

A

for O2 to bind Fe(II) on heme reversibily

17
Q

how is the heme held in place

A

hydrophobic interactions

18
Q

how is the heme held in place to each Hb subinit

A

coordinate covalend bond to His F8

19
Q

CO has a strong affinity for what

A

Fe+2

20
Q

CO2 binds to heme in a fashion

A

linearly and makes it 20,000 times stronger than O2

21
Q

what ligand helps prevent CO poisioning

A

His E7

22
Q

what other small molecules are positon becase they have a high affinity for Fe+2 in heme

A

Cn, N3, No, H2S

23
Q
A