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- Question 1 of 45
1. Question
Category: Bio-Inorganic ChemistryPatients suffering from Wilson’s disease have:
CorrectIncorrect - Question 2 of 45
2. Question
Category: Bio-Inorganic ChemistryMg2+ is preferred in photosynthesis by chlorophyll because-
CorrectIncorrect - Question 3 of 45
3. Question
Category: Bio-Inorganic ChemistryThe ligand system present in vitamin B12 is,
CorrectCorrin 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)
IncorrectCorrin 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)
- Question 4 of 45
4. Question
Category: Bio-Inorganic ChemistrySuperoxide dismutase contains the metal ions:
CorrectIncorrect - Question 5 of 45
5. Question
Category: Bio-Inorganic ChemistryThe oxidation state of iron in methemoglobin is:
CorrectIncorrect - Question 6 of 45
6. Question
Category: Bio-Inorganic ChemistryThe cooperative binding Of O2 in hemoglobin is due to:
CorrectIncorrect - Question 7 of 45
7. Question
Category: Bio-Inorganic ChemistryThe correct set of the biologically essential elements, is
CorrectIncorrect - Question 8 of 45
8. Question
Category: Bio-Inorganic ChemistryMolybdoenzymes can both oxidize as well as reduce the substrates, because
CorrectIncorrect - Question 9 of 45
9. Question
Category: Bio-Inorganic ChemistryUnder physiological condition, oxygen is binding to deoxyhemoglobin and deoxymyoglobin, the binding curve and its pH dependence respectively, are
CorrectIncorrect - Question 10 of 45
10. Question
Category: Bio-Inorganic ChemistryHigh dose of dietary supplement ZnSO4 for the cure of Zn deficiency,
CorrectIncorrect - Question 11 of 45
11. Question
Category: Bio-Inorganic ChemistryThe total number of metal ion and the number of coordinated imidazole units of histidine in the active site of oxy-hemocyanin, respectively are-
CorrectIncorrect - Question 12 of 45
12. Question
Category: Bio-Inorganic ChemistryThe extent of π electron conjugation in macrocyclic rings of (i) heme, (ii) coenzyme B12 and (iii) chlorophyll follows the order,
CorrectLeast 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 )
IncorrectLeast 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 )
- Question 13 of 45
13. Question
Category: Bio-Inorganic ChemistryThe changes (from A-D given below) which occur when O2 binds to hemerythrin are
(A) One iron atom is oxidized
(B) Both the iron atoms are oxidized
(C) O2 binds to one iron atom and is also hydrogen-bonded.
(D) O2 binds to both the iron atoms and is also hydrogen-bonded.
CorrectIncorrect - Question 14 of 45
14. Question
Category: Bio-Inorganic ChemistryThe number of histidine amino acid nitrogen atoms coordinated to bimetallic active site of oxyhemocyanin and oxyhemerythrine, respectively are,
CorrectIncorrect - Question 15 of 45
15. Question
Category: Bio-Inorganic ChemistryThe resonance Raman stetching frequency (V0-0 in cm-1) of O2 is 1580. The V0-0 for O2 in bound oxy-hemoglobin is close to:
CorrectOxyhemogolbin is Fe(¡¡¡)O2(-1) …and 1100 cm-1 is v(o-o) for O2(-1)
in case of oxygen bound to hemerythin the stretching frequency is around 850 and when oxygen is blund to hemocyanin the stretching frequency is around 780
IncorrectOxyhemogolbin is Fe(¡¡¡)O2(-1) …and 1100 cm-1 is v(o-o) for O2(-1)
in case of oxygen bound to hemerythin the stretching frequency is around 850 and when oxygen is blund to hemocyanin the stretching frequency is around 780
- Question 16 of 45
16. Question
Category: Bio-Inorganic ChemistryThe Fe—Nporphyrin bond distances in the deOxy and Oxy-hemoglobin, respectively are
CorrectThe Fe-O-O angle is 152 degrees, as in human hemoglobin. The oxygen is hydrogen-bonded to the distal histidine at N epsilon 2-O1 and N epsilon 2-O2 distance of 2.95 A and 2.68 A, respectively.
IncorrectThe Fe-O-O angle is 152 degrees, as in human hemoglobin. The oxygen is hydrogen-bonded to the distal histidine at N epsilon 2-O1 and N epsilon 2-O2 distance of 2.95 A and 2.68 A, respectively.
- Question 17 of 45
17. Question
Category: Bio-Inorganic ChemistryThe metal present at the active site of the protein Carboxypept idase A is,
CorrectIncorrect - Question 18 of 45
18. Question
Category: Bio-Inorganic ChemistryThe biological functions of the cytochrome P450 and myoglobin are respectively,
CorrectIncorrect - Question 19 of 45
19. Question
Category: Bio-Inorganic ChemistryIn biological systems, the metal ion involved in the Dioxygen transport besides Fe is,
CorrectIncorrect - Question 20 of 45
20. Question
Category: Bio-Inorganic ChemistryDeoxy-Hemocyanin is,
Correct<div> <p><strong>Hemocyanin</strong>, a copper-containing protein chemically unlike hemoglobin, is found in some crustaceans.</p> <p><strong>Hemocyanin</strong> is B<strong>lue</strong> in <strong>colour</strong> when oxygenated and colourless when oxygen is removed.</p> </div> <div></div>
Incorrect<div> <p><strong>Hemocyanin</strong>, a copper-containing protein chemically unlike hemoglobin, is found in some crustaceans.</p> <p><strong>Hemocyanin</strong> is B<strong>lue</strong> in <strong>colour</strong> when oxygenated and colourless when oxygen is removed.</p> </div> <div></div>
- Question 21 of 45
21. Question
Category: Bio-Inorganic ChemistryCarboxypeptidase contains
CorrectIncorrect - Question 22 of 45
22. Question
Category: Bio-Inorganic ChemistryIron–sulphur clusters in bio logical systems are involved in,
CorrectIncorrect - Question 23 of 45
23. Question
Category: Bio-Inorganic ChemistryThe reduction of nitrogen to ammonia, carried out by the enzyme nitrogenase, needs
CorrectIncorrect - Question 24 of 45
24. Question
Category: Bio-Inorganic ChemistryThe amino acid side chain high affinity for Ca2+ and Cu2+ in metallo–proteins is,
CorrectIncorrect - Question 25 of 45
25. Question
Category: Bio-Inorganic ChemistryIn bacterial ruberdoxin, the number of iron atoms, sulfur bridges and cysteine ligands are:
Fe atoms S-bridges Cysteine ligands A 4 4 4 B 2 2 4 C 2 2 2 D 1 0 4 CorrectIncorrect - Question 26 of 45
26. Question
Category: Bio-Inorganic ChemistryWhen a reduced cytochrome transfers an electron from its Fe(II) to the bound O2
CorrectIncorrect - Question 27 of 45
27. Question
Category: Bio-Inorganic ChemistryA metal ion that replace manganese (II) ion in Mangano–proteins without changing its function, is
CorrectIncorrect - Question 28 of 45
28. Question
Category: Bio-Inorganic ChemistryIn photosynthesis, the predominant metal present in the reaction centre of photo –system II is,
CorrectIncorrect - Question 29 of 45
29. Question
Category: Bio-Inorganic ChemistryZn in carbonic anhydrase is coordinated by three hist idine and one water molecule. The reaction of CO2 with this enzyme is an example of,
CorrectIncorrect - Question 30 of 45
30. Question
Category: Bio-Inorganic ChemistryThe 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.CorrectIncorrect - Question 31 of 45
31. Question
Category: Bio-Inorganic ChemistryAmongst the following, the group that is bound to the metal ion in coenzyme B12 is,
CorrectIncorrect - Question 32 of 45
32. Question
Category: Bio-Inorganic ChemistryIn biological systems, the metal ions involved in electron transport are,
CorrectIncorrect - Question 33 of 45
33. Question
Category: Bio-Inorganic ChemistryBased 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,
CorrectIncorrect - Question 34 of 45
34. Question
Category: Bio-Inorganic ChemistryIn the transformation of oxyhaemoglobin to deoxyhaemoglobin,
CorrectIncorrect - Question 35 of 45
35. Question
Category: Bio-Inorganic ChemistryAmong the following pair of metal ions present in Nature. The first one functions as an electron transfer agent and the second one catalyzes the hydrolysis reactions. The correct pair is,
CorrectIncorrect - Question 36 of 45
36. Question
Category: Bio-Inorganic ChemistryFe2+ -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+ -porphyrins.
(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.CorrectIncorrect - Question 37 of 45
37. Question
Category: Bio-Inorganic ChemistryA well known naturally occurring organometallic compound is,
CorrectIncorrect - Question 38 of 45
38. Question
Category: Bio-Inorganic ChemistryThe red color of oxyhaemoglobin is mainly due to the
CorrectEach hemoglobin protein is made up subunits called Hemes, which are what give blood its red color. More specifically, the hemes can bind iron molecules, and these iron molecules bind oxygen.
The blood cells are red because of the interaction between iron and oxygen i.e. intra ligand π–π* transition.
When the iron is oxygenated(Fe+3), it becomes red. When the iron is deoxygenated(Fe+2), it becomes blue. This is why your veins are blue.
IncorrectEach hemoglobin protein is made up subunits called Hemes, which are what give blood its red color. More specifically, the hemes can bind iron molecules, and these iron molecules bind oxygen.
The blood cells are red because of the interaction between iron and oxygen i.e. intra ligand π–π* transition.
When the iron is oxygenated(Fe+3), it becomes red. When the iron is deoxygenated(Fe+2), it becomes blue. This is why your veins are blue.
- Question 39 of 45
39. Question
Category: Bio-Inorganic ChemistryHemoglobin is an oxygen carrying. The correct statement about oxy–hemoglobin is that,
CorrectIncorrect - Question 40 of 45
40. Question
Category: Bio-Inorganic ChemistryOxymyoglobin Mb(O2) and oxyhaemoglobin Hb(O2)4, respectively, are
CorrectIncorrect - Question 41 of 45
41. Question
Category: Bio-Inorganic ChemistryAmong the given pH values, the O2 binding efficiency of hemoglobin is maximum at,
CorrectIncorrect - Question 42 of 45
42. Question
Category: Bio-Inorganic ChemistryIdentify the function of Hemocyanin and the Metal responsible for it,
CorrectIncorrect - Question 43 of 45
43. Question
Category: Bio-Inorganic ChemistryDuring Oxygen Transport by Hemerythrin, Oxygen is bound as,
CorrectThe mechanism of dioxygen binding is unusual. Most O2 carriers operate via formation of dioxygen complexes, but hemerythrin holds the O2 as a hydroperoxide (HO2, or -OOH−). The site that binds O2 consists of a pair of iron centres. The iron atoms are bound to the protein through the carboxylate side chains of a glutamate and aspartates as well as through five histidine residues. Hemerythrin and myohemerythrin are often described according to oxidation and ligation states of the iron center:
Fe2+—OH—Fe2+deoxy (reduced)
Fe2+—OH—Fe3+semi-met
Fe3+—O—Fe3+—OOH−oxy (oxidized)
Fe3+—OH—Fe3+— (any other ligand)met (oxidized)
The uptake of O2 by hemerythrin is accompanied by two-electron oxidation of the diferrous centre to produce a hydroperoxide (OOH−) complex.
IncorrectThe mechanism of dioxygen binding is unusual. Most O2 carriers operate via formation of dioxygen complexes, but hemerythrin holds the O2 as a hydroperoxide (HO2, or -OOH−). The site that binds O2 consists of a pair of iron centres. The iron atoms are bound to the protein through the carboxylate side chains of a glutamate and aspartates as well as through five histidine residues. Hemerythrin and myohemerythrin are often described according to oxidation and ligation states of the iron center:
Fe2+—OH—Fe2+deoxy (reduced)
Fe2+—OH—Fe3+semi-met
Fe3+—O—Fe3+—OOH−oxy (oxidized)
Fe3+—OH—Fe3+— (any other ligand)met (oxidized)
The uptake of O2 by hemerythrin is accompanied by two-electron oxidation of the diferrous centre to produce a hydroperoxide (OOH−) complex.
- Question 44 of 45
44. Question
Category: Bio-Inorganic ChemistryAt pH 7.2 and 10 Torr oxygen partial pressure, the extent of O2 binding is,
CorrectIncorrect - Question 45 of 45
45. Question
Which statement are incorrect for L to Metal Charge Transfer,
Incorrect
Free Bio-Inorganic Chemistry Practice Mock Test is for CSIR UGC NET, GATE & JAM students so can practice before exams and get involved the right way to handle exam time pressure.
This quiz contains 45 questions related to Bio inorganic chemistry.Chemistry free Mock Test To prepare for these exams, it is important to give mock tests as it helps the students learn from their mistakes.
Mock tests are considered as practice exams before you appear for the final Exam. While you attempting these Mock tests, it help boost your confidence and overcome minor and major mistakes
The Gibbs free energy of activation ∆GŦis represented by the following equation:
ΔG∓=ΔwG∓+ΔoG∓+ΔsG∓+RTln(k′T/hZ)
T = temperature in K
R = molar gas constant
k’ = Boltzman constant
h = Plancks constant
Z = effective frequency collision in solution ~ 1011 dm3 mol-1 s-1
∆wGŦ = the energy associated with bringing the reactants together, includes the work done to counter any repulsion
∆0GŦ = energy associated with bond distance changes
∆s ∆GŦ= energy associated with the rearrangements taking place in the solvent spheres
ln ( k’T / hZ) = accounts for the energy lost in the formation of the encounter complex