heamoproteins 1 Flashcards
—in the rbc responsible for 02 transport in higher animals and is — of iron in our body
- haemoglobin
- 65%
- RMM: 66000
— in muscles which stores and transports 02 across muscle cells and is — of the iron
- myoglobin
- 6%
- RMM: 17.8
myoglobin is a — and it consist of — which contains — and —-
- tertiary structure
- haem group of: iron II and protoprophryin IX
- globin chain that is secondary and primary and has 153-160 amino acid residues
—- refers to the linear sequence of amino acids in the polypeptide chain and are linked by — such as —
- primary structure
- covelant bond
- peptide bond
— 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
- secondary
- alpha helix , beta sheeted
- hydrogen bonding
— refers to the 3d structure of protein. The alpha helixes are beta sheetes are folded into — structure. The interactions include ——–
- tertiary structure
- globular
- salt bridges, disulfied, hydrogen bonds, and tightly packed side chains
— 3d structure of multi-subunit proteins and the subunits fit together. These structures are stabilised by —– and —–
- quantery
- non covalent binds
- disulfied interactions as tertiary structure
iron - protoprophryin IX is in — family and has —- atoms and is —- with — pyrrole like rings joined by — and is —–
- porphyrin , tetradentate, planer ligands
- 4N donor atoms
- hetroaromaric
- 4
- CH group
- peripheral substituents
— has a compact shape with protein chain folded about the haem group.
myoglobin
globin chain linked to the haem group through the histadine residue called
proximal histadine
myoglobin has — helical and —-
the interior is —-
exterior is —-
and only 2 —— and both are essential for —-
- 8 helical regions
- non helical regions and termini chain
- hydrophobic
- hydrophilic
- hydrophilic
-biological activituies
the fe II is — and the coordination number is — and has — amount of maximum coordination number and has a – coodrination site to complex with —
- unsaturated
- 5
- less
- vacant
- 02
the haem group is — or else it will be —- which can’t bind to 02
- non-polar , hydrophobic
- oxidised to fe III ( in the presence of 02 and h20 )
the forms of myoglobin:
- myoglobin is — + – and the color is —
- oxymyoglobin is — + — and the color is —
- metomyoglin is —- + — and the color is —
- fe II + histadine , purple red
- fe II + histadine +02 , bright red
- fe III + histadine + h20 , brownish red and can’t bind to 02
energies in the metal ion of – orbital in — and dependent on — and the two splits are — and — and the two possible configurations are
- d
- octahedral complex
- axial , inter axial
- high spin , low split ( paramagnetic, u fill singly )
- low spin , high split ( diamagnetic , u fill all down first)
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 —
- high spin , paramgantic , fe II
- out
- one empty
- 5
- low spin , diamagnetic , fe II
- smaller in size
- 3
- into
- saturated
- coordination number 6
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
- spherical
- non polar
- myoglobin
-identical
-24
4 subunits 2 alpha and 2 beta w/ salt bridges in between - myoglobin-like
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 —
- tetrametric
- 141
146 - both betas
- 2 alphas or 2 betas
the most important interactions between the subunits are
salt bridges linkages between oppositely charged amino acid side chains
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
- Mb-like
- unsaturated , 5
- 02
- high spin , 4 unpaired electrons
-out
true or false: when iron II enters the porphyrin plane it shrinks
true
the – structure of globin chain in haemoglobin is — from the myoglobin but the — and — are —. hemoglobins structure is — but myoglobin isn’t.
- primary
- different
- seoncdary and terirty
-quantery
when haemoglobin becomes oxyhemoglobin is called —
-formula:
-coordination number becomes:
- iron is – the plane
- – spin
- is the process reversible?
- oxygenation
- Hb + 402 –> <– ( aka equilibrium lol ) Hb(02)4
- 6 , saturated
- in
- low spin , diamagnetic
- yes
