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)