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Test: Bio Inorganic- 1 - Chemistry MCQ


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20 Questions MCQ Test - Test: Bio Inorganic- 1

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Test: Bio Inorganic- 1 - Question 1

The ligand system present in vitamin B12 is:

Detailed Solution for Test: Bio Inorganic- 1 - Question 1

Corrin is a heterocyclic compound. It is the parent macrocycle related to the substituted derivative that is found in vitamin B12. Its name reflects that it is the "core" of vitamin B12 (cobalamins)

Test: Bio Inorganic- 1 - Question 2

Superoxide dismutase contains the metal ions:

Detailed Solution for Test: Bio Inorganic- 1 - Question 2

Chemical Structure of Superoxide Dismutase:
Superoxide dismutase activity of a Cu–Zn complex—bare and immobilised - New  Journal of Chemistry (RSC Publishing) DOI:10.1039/B500579E

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Test: Bio Inorganic- 1 - Question 3

The oxidation state of iron in methemoglobin is:

Detailed Solution for Test: Bio Inorganic- 1 - Question 3
  • Methemoglobin is hemoglobin in the form of metalloprotein, in which the iron in the heme group is in the Fe³⁺ state, not the Fe²⁺ of normal hemoglobin.
  • Methemoglobin cannot bind oxygen, which means it cannot carry oxygen to tissues.
  • It is a bluish chocolate-brown in colour.
Test: Bio Inorganic- 1 - Question 4

The correct set of the biologically essential elements, is ______.

Detailed Solution for Test: Bio Inorganic- 1 - Question 4
  • An essential element is one that is required for life and whose absence results in death.
  • Because of the experimental difficulties involved in producing deficiencies severe enough to cause death, especially for elements that are required in very low concentrations in the diet.
  • An element is considered to be essential if a deficiency consistently causes abnormal development or functioning and if dietary supplementation of that element—and only that element—prevents this adverse effect.
  • The essential mineral elements are Nitrogen, phosphorus, potassium, calcium, magnesium, sulfur, boron, chlorine, iron, manganese, zinc, copper, molybdenum, and nickel.

Test: Bio Inorganic- 1 - Question 5

In metal ion catalysis, what is the primary function of the metal ion?

Detailed Solution for Test: Bio Inorganic- 1 - Question 5

 To stabilize negative charges on reaction intermediates

The primary function of the metal ion in metal ion catalysis is to stabilize negative charges on reaction intermediates.

Key Points

  • Stabilization of negative charges:
    • Metal ions in catalytic processes often stabilize negatively charged intermediates, which can be crucial for the reaction to proceed.
    • This stabilization lowers the activation energy, making the reaction more feasible.
  • Coordination chemistry:
    • Metal ions can coordinate with substrates to form more reactive complexes, facilitating the reaction.
Test: Bio Inorganic- 1 - Question 6

High dose of dietary supplement ZnSO4 for the cure of Zn deficiency:

Test: Bio Inorganic- 1 - Question 7

The extent of π electron conjugation in macrocyclic rings of (i) heme, (ii) coenzyme B12 and (iii) chlorophyll follows the order:

Detailed Solution for Test: Bio Inorganic- 1 - Question 7

Least conjugation is present in Vitamin B12 as one side of the corrin ring doesn’t have methylene linkages. In Heme, there is extensive conjugation of π electron (11 π ) as compared to that of chlorophyll.( 10π )


Test: Bio Inorganic- 1 - Question 8

The number of histidine amino acid nitrogen atoms coordinated to bimetallic active site of oxyhemocyanin and oxyhemerythrine, respectively, are:

Test: Bio Inorganic- 1 - Question 9

The biological functions of carbonic anhydrase and Carboxypeptidase A, respectively, are

Test: Bio Inorganic- 1 - Question 10

The Fe—Npprphyrin bond distances in the deoxy and oxy-hemoglobin, respectively are:

Test: Bio Inorganic- 1 - Question 11

The biological functions of the cytochrome P450 and myoglobin are, respectively:

Detailed Solution for Test: Bio Inorganic- 1 - Question 11
  • Cytochromes P450 (P450) are hemoproteins encoded by a superfamily of genes nearly ubiquitously distributed in different organisms from all biological kingdoms.
  • The reactions carried out by P450s are extremely diverse and contribute to the biotransformation of drugs, the bioconversion of xenobiotics, the bioactivation of chemical carcinogens, the biosynthesis of physiologically important compounds such as steroids, fatty acids, eicosanoids, fat-soluble vitamins and bile acids, the conversion of alkanes, terpenes and aromatic compounds as well as the degradation of herbicides and insecticides.
  • Cytochromes P450 belong to the group of external monooxygenases and thus receive the necessary electrons for oxygen cleavage and substrate hydroxylation from different redox partners. The classical as well as the recently discovered P450 redox systems.
  • Myoglobin contains a heme (prosthetic) group which is responsible for its main function (carrying of oxygen molecules to muscle tissues). Myoglobin can exist in the oxygen free form, deoxymyoglobin, or in a form in which the oxygen molecule is bound, called oxymyoglobin. Myoglobin is a protein found in muscles that binds oxygen with its heme group like haemoglobin.
  • Oxidation of the iron atom (Fe2+ -> Fe3+) is mainly responsible for the colour of muscle and blood.
Test: Bio Inorganic- 1 - Question 12

Deoxy-Hemocyanin is:

Detailed Solution for Test: Bio Inorganic- 1 - Question 12

Hemocyanin, a copper-containing protein chemically unlike haemoglobin, is found in some crustaceans.

Hemocyanin is blue in colour when oxygenated and colourless when oxygen is removed.

Test: Bio Inorganic- 1 - Question 13

Carboxypeptidase contains:

Test: Bio Inorganic- 1 - Question 14

The reduction of nitrogen to ammonia, carried out by the enzyme nitrogenase, needs:

Detailed Solution for Test: Bio Inorganic- 1 - Question 14
  • The reduction of nitrogen to ammonia, carried out by the enzyme nitrogenase is known as Nitrogen Fixation.
  • Biological nitrogen fixation (BNF) occurs when atmospheric nitrogen is converted to ammonia by an enzyme called nitrogenase.
  • The reaction for BNF is: N2 + 8H+ + 8 e- → 2NH3 + H2
  • This type of reaction results in N2 gaining electrons and is thus termed a reduction reaction.
Test: Bio Inorganic- 1 - Question 15

In bacterial ruberdoxin, the number of iron atoms, sulfur bridges and cysteine ligands are:

Test: Bio Inorganic- 1 - Question 16

A metal ion that replace manganese (II) ion in Mangano–proteins without changing its function, is:

Test: Bio Inorganic- 1 - Question 17

The changes (from A–D given below) which occur when O2 binds to hemerythrin are:
(A) One ion atom is oxidized.
(B) Both the iron atoms are oxidized.
(C) O2 binds to one iron atom and is also hydrogen bonds.
(D) O2 binds to both the iron atoms and is also hydrogen bonded.

Test: Bio Inorganic- 1 - Question 18

Amongst the following, the group that is bound to the metal ion in cenzyme B12 is:

Test: Bio Inorganic- 1 - Question 19

Based on the behavior of the metalloenzymes, consider the following statements:

(A) In the enzymes, the zinc act ivates O2 to form peroxide species.
(B) In the enzymes, the zinc activates H2O and provides a zinc bound hydroxide.
(C) In the enzymes, the zinc activates O2 to break the bounding between the two oxygens.
(D) Zincion acts as a nucleophile and attacks at the peptide carbonyl.

The set of correct statements is,

Test: Bio Inorganic- 1 - Question 20

Fe2+ -porphyrins fail to exhibit reversible oxygen transport and cannot differentiate CO from O2. However, the hemoglobin is free from both these pit falls. Among the following the correct set of statements is:

(A) Fe2+-porphyrins undergo μ-oxodimer formation and the same is prevented in case of the hemoglobin.
(B) Fe–CO bond strength is much low in case of hemoglobin when compared to the Fe2+ -porthyrins.
(C) While Fe–CO is linear, Fe–O2 is bent and is recognized by hemoglobin.
(D) The interlinked four monomeric units in the hemoglobin are responsible to overcome the pitfalls. 

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