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Bioinorganic Chemistry - Most Important Questions! (Download PDF)
1. In deoxyhaemoglobin
- 5th position is coordinated with O2
- 5th position is coordinated by porphyrin ring N-atom
- 5th position is occupied by N-atom of imidazole ligand of a histidine residue which couples’ heme to the protein
- None of the above
2. O2 binding in Hb is
- O2 binds at neutral pH
- None of these
3. Release of O2 from oxyhemoglobin is favoured by:
- high pH and low CO2 conc
- low pH and low CO2 conc
- high pH and high CO2 conc
- low pH and high conc. of CO2
4. Hemerythrin belongs to the group of
- Non-heme iron protein
- Binuclear copper protein
- Heme-iron protein
- Non-heme-iron protein
5. In oxy-haemoglobin, the iron centre is best described by which of the following?
- high-spin Fe(III)
- high-spin Fe(II)
- low-spin Fe(III)
- low-spin Fe(II)
6. Oxymyoglobin Mb(O2) is
- None of the above
7. The oxidation state of iron in methemoglobin is
8. The ligand system in vitamin B12 is:
9. Superoxide dismutase contains:
- Zn(II) and Ni(II)
- Cu(II) and Fe(II)
- Ni(II) and Co(II)
- Cu(II) and Zn(II)
10. What is the correct order of binding ability of zinc in carbonic anhydrase metalloenzyme towards halide ions?
The structure of deoxyhemoglobin is:
According to the structure, C is the correct option.
In Haemoglobin, oxygen binding affinity is inversely related to both acidity and the concentration of carbon dioxide. An increase in pH takes place as carbon dioxide decreases which result in haemoglobin picking up more oxygen.
The effect of carbon dioxide and acidity favours the formation of oxyhaemoglobin at low concentrations of CO2 and H+ ion which results in the dissociation of oxyhaemoglobin releasing O2 at a high concentration of both CO2 and H+ ion.
Hemerythrin is a non-heme protein that is used by two phyla of marine invertebrates for oxygen transport and for storage.
The active site of a protein contains a heme group which is coordinated with iron in a 6-coordinate, low spin state. A histidine and a cysteine are involved in axial coordination to the iron.
Oxymyoglobin has a zero magnetic moment which means it has no unpaired electrons. Each iron atom is attached with four porphyrin N atoms, the globin molecule, and the oxygen molecule through covalent bonds.
The formation of methemoglobin takes place by the reversible oxidation of heme iron to the ferric state that is Fe3+. Met haemoglobin cannot carry oxygen as oxidized iron cannot bind it.
Vitamin B12 is generally a collection of cobalt and corrin ring molecules. Corrin rings are like porphyrin rings. Out of the six coordinating sites, four of the ring coordinating sites are provided by corrin rings and fifth one is by dimethyl benzimidazole group. The sixth site which is the centre of reactivity is variable.
Based on protein fold and metal cofactor, there are three major classes of superoxide dismutase, and these are:
HSAB principle: According to this principle, hard acid tends to react with hard base while soft acid tends to react with soft base. The order of binding capability of Zn2+ with halide ions is F->Cl->Br->I- but in carbonic anhydrase enzyme, the order is reversed to I->Br->Cl->F- . Reason for the inversion is the presence of apoenzyme.
As Zn2+ belongs to category of borderline acids so, it tends to react with strong or borderline bases strongly in accordance with HSAB principle, but the presence of apoenzyme in the carbonic anhydrase enzyme makes the Zn as soft acid so, now Zn tends to bind strongly with weak base that is I- followed by Br-, Cl- and finally least binding with F-. So, the order of binding ability with Zn in carbonic anhydrase enzyme is:
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