heamoproteins 1 Flashcards

1
Q

—in the rbc responsible for 02 transport in higher animals and is — of iron in our body

A
  • haemoglobin
  • 65%
  • RMM: 66000
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2
Q

— in muscles which stores and transports 02 across muscle cells and is — of the iron

A
  • myoglobin
  • 6%
  • RMM: 17.8
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3
Q

myoglobin is a — and it consist of — which contains — and —-

A
  • tertiary structure
  • haem group of: iron II and protoprophryin IX
  • globin chain that is secondary and primary and has 153-160 amino acid residues
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4
Q

—- refers to the linear sequence of amino acids in the polypeptide chain and are linked by — such as —

A
  • primary structure
  • covelant bond
  • peptide bond
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5
Q

— refers to highly regular local sub structure and consist of two main types — and —. These structures are defined by patterns of —- between the main-chain peptide groups

A
  • secondary
  • alpha helix , beta sheeted
  • hydrogen bonding
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6
Q

— refers to the 3d structure of protein. The alpha helixes are beta sheetes are folded into — structure. The interactions include ——–

A
  • tertiary structure
  • globular
  • salt bridges, disulfied, hydrogen bonds, and tightly packed side chains
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7
Q

— 3d structure of multi-subunit proteins and the subunits fit together. These structures are stabilised by —– and —–

A
  • quantery
  • non covalent binds
  • disulfied interactions as tertiary structure
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8
Q

iron - protoprophryin IX is in — family and has —- atoms and is —- with — pyrrole like rings joined by — and is —–

A
  • porphyrin , tetradentate, planer ligands
  • 4N donor atoms
  • hetroaromaric
  • 4
  • CH group
  • peripheral substituents
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9
Q

— has a compact shape with protein chain folded about the haem group.

A

myoglobin

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10
Q

globin chain linked to the haem group through the histadine residue called

A

proximal histadine

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11
Q

myoglobin has — helical and —-
the interior is —-
exterior is —-
and only 2 —— and both are essential for —-

A
  • 8 helical regions
  • non helical regions and termini chain
  • hydrophobic
  • hydrophilic
  • hydrophilic
    -biological activituies
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12
Q

the fe II is — and the coordination number is — and has — amount of maximum coordination number and has a – coodrination site to complex with —

A
  • unsaturated
  • 5
  • less
  • vacant
  • 02
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13
Q

the haem group is — or else it will be —- which can’t bind to 02

A
  • non-polar , hydrophobic
  • oxidised to fe III ( in the presence of 02 and h20 )
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14
Q

the forms of myoglobin:
- myoglobin is — + – and the color is —
- oxymyoglobin is — + — and the color is —
- metomyoglin is —- + — and the color is —

A
  • fe II + histadine , purple red
  • fe II + histadine +02 , bright red
  • fe III + histadine + h20 , brownish red and can’t bind to 02
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15
Q

energies in the metal ion of – orbital in — and dependent on — and the two splits are — and — and the two possible configurations are

A
  • d
  • octahedral complex
  • axial , inter axial
  • high spin , low split ( paramagnetic, u fill singly )
  • low spin , high split ( diamagnetic , u fill all down first)
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16
Q

myoglobin has — spin and lies – of the prophrin plane and has – coordiantion side and coordination number is —
oxymyoghobin has — and is — in size and electrons are concentrated into – orbitals and they fit – the porphyrin plane and is — with coordination number —

A
  • high spin , paramgantic , fe II
  • out
  • one empty
  • 5
  • low spin , diamagnetic , fe II
  • smaller in size
  • 3
  • into
  • saturated
  • coordination number 6
17
Q

haemoglobin has – shape and is — the 3D structure of globin chain in Hb is similar to — although the amino acids are — at — position
consist of — subunits and are —like

A
  • spherical
  • non polar
  • myoglobin
    -identical
    -24
    4 subunits 2 alpha and 2 beta w/ salt bridges in between
  • myoglobin-like
18
Q

The adult human hemaoglobin (HBA ) is a — protein
- alpha has – amino acids
- beta has — amino acids
- each alpha is in contact w — beta
- very few interactions between — or —

A
  • tetrametric
  • 141
    146
  • both betas
  • 2 alphas or 2 betas
19
Q

the most important interactions between the subunits are

A

salt bridges linkages between oppositely charged amino acid side chains

20
Q

subunit in the haem group:
- each haem group is —
- fe II is — and the coordination number is —
- vacant coordination site to complex with —
- has – spin with – unpaired electrons
- Fe II is – of the plan

A
  • Mb-like
  • unsaturated , 5
  • 02
  • high spin , 4 unpaired electrons
    -out
21
Q

true or false: when iron II enters the porphyrin plane it shrinks

A

true

22
Q

the – structure of globin chain in haemoglobin is — from the myoglobin but the — and — are —. hemoglobins structure is — but myoglobin isn’t.

A
  • primary
  • different
  • seoncdary and terirty
    -quantery
23
Q

when haemoglobin becomes oxyhemoglobin is called —
-formula:
-coordination number becomes:
- iron is – the plane
- – spin
- is the process reversible?

A
  • oxygenation
  • Hb + 402 –> <– ( aka equilibrium lol ) Hb(02)4
  • 6 , saturated
  • in
  • low spin , diamagnetic
  • yes