LS - 0 - 2 - 2d3125 - 024d2f3562799-Bioinorganic (Previous Year)

Download as pdf or txt
Download as pdf or txt
You are on page 1of 9

INORGANIC CHEMISTRY

Assignment

Bioinorganic (Previous Year)


1. The ligand system present in vitamin B12 is:
(a) Porphyrin (b) Corrin (c) Phthalocyanine (d) Crown ether
2. Carboxypeptidase contains :
(a) Zn(II) and hydrolyses CO2 (b) Zn(II) and hydrolyses peptide bonds
(c) Mg(II) and hydrolyses CO2 (d) Mg(II) and hydrolyses peptide bonds
3. Superoxide dismutase contains the metal ions
(a) Zn(II) and Ni(II) (b) Cu(II) and Zn(II) (c) Ni(II) and Co(III) (d) Cu(II) and Fe(III)
4. The reduction of nitrogen to ammonia, carried out by the enzyme nitrogenase, needs :
(a) 2 electrons (b) 4 electrons (c) 6 electrons (d) 8 electrons
5. A metal ion that replace maganese (II) ion in mangano-proteins without changing its function, is
(a) Fe(II) (b) Zn(II) (c) Mg(II) (d) Cu(II)
6. In bacterial rubredoxin, the number of iron atoms, sulfur bridges and cysteine ligands are

(a)
CHEM ACADEMY
Fe atom
4
Sulfur bridge
4
Cysteine
4
(b) 2 2 4
(c) 2 2 2
(d) 1 0 4
7. The oxidation state of iron in met-hemoglobin is:
(a) Three (b) two (c) four (d) zero
8. The changes (from a-d given below) which occur when O2 binds to hemerythrin are
(A) One iron atoms 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.
(a) B and C (b) B and D (c) A and D (d) A and C
9. In photosynthetic systems the redox metalloproteins involved in electron transfer are cytochrome
(cyt, b), cytochrome bf complex (cyt bf) and plastocyamin(PC). the pathway of electron flow is
(a) PC  cyt b  cyt bf (b) cyt bf  cyt b  PC
(c) cyt b  cyt bf  PC (d) PC  cyt bf  cyt b
10. The correct ser of the biologically essential elements is:
(a) Fe, Mo, Cu, Zn (b) Fe, Cu, Co, Ru (c) Cu, Mn, Zn, Ag (d) Fe, Ru, Zn, Mg

North Delhi: 72, Mall Road, G.T.B. Nagar, New Delhi - 110009
South Delhi: 28B/7, Jia Sarai, Near IIT, Hauz Khas, New Delhi - 110016. Mob.: 8860108204 1
Toll Free: 1800 120 5848, Ph.: 011-41415514, 09136597244, Web.: www.chemacademy.co.in
11. Based on the behaviour of the metalloenzymes, consider the following statements
(A) In the enzymes, the zinc activates O2 to form peroxide species
(B) In the enzymes, the zinc activates H2O and provides a zinc bound hydroxide.
(C) In the oxidases, the iron activates O2 to break the bonding between the two oxygens
(D) Zinc ion acts as a nucleophile and attacks at the peptide carbonyl
The set of correct statements is:
(a) A and B (b) B and C (c) C and D (d) A and D
2+
12. Fe -porphyrins fails to exhibit reversible oxygen transport and cannot differentiate CO from O2.
However, the hemoglobin is free from both these pit falls. Among the following :
(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+-porphy-
rins
(C) While Fe–Co is linear, Fe–O2 is beat and is recognized by hemoglobin
(D) The interlinked four monomeric units in the hemoglobin responsible to overcome the pitfalls.
The correct set of statements is:
(a) A and B (b) A and C (c) C and D (d) B and D
13. The metal ions present in the active site of nitrogenase enzyme co-factor are
(a) Fe, Mo (b) Fe, W (c) Fe, Cu (d) Fe, Ni
14. For the metalloprotein hemerythrin, the statement that is NOT TRUE is

CHEM ACADEMY
(a) Three are two ion centres per active site
(b) Both iron centres are hexacoordinated in the active site
(c) One iron is hexacoordinated while the other is pentacoordinated in the active state
(d) It is found in marine invertebrates
15. The coordination geometry of copper (II) in the type I copper protein plastocyanin is:
(a) Square planar (b) Tetrahedral (c) Octahedral (d) Distorted tetrahedral
16. High does of dietary supplement ZnSO4 for the cure of Zn deficiency
(a) Reduces myoglobin (b) Increases iron level in blood
(c) Increases copper level in brain (d) Reduces copper, iron and calcium levels in body
17. Molybdoenzymes can both oxidize as well as reduce the substrates, because
(a) Mo(VI) is more stable than Mo(IV)
(b) Mo(IV) can transfer oxygen atom to the substrate and Mo(IV) can abstract oxygen atom from
the substrate
(c) Conversion of Mo(VI) to Mo(IV) is not favoured
(d) Mo(VI) can transfer oxygen atom to the substrate and Mo(IV) can abstract oxygen atom from
the substrate.
18. The cooperative binding of O2 in hemoglobin is due to
(a) A decrease in size of iron followed by changes in the protein conformation
(b) An increase in size of iron followed by changes in the protein conformation
(c) A decrease in size of iron that is not accompanied by the protein conformational changes
(d) A increase in size of iron that is not accompanied by the protein conformational changes

North Delhi: 72, Mall Road, G.T.B. Nagar, New Delhi - 110009
South Delhi: 28B/7, Jia Sarai, Near IIT, Hauz Khas, New Delhi - 110016. Mob.: 8860108204 2
Toll Free: 1800 120 5848, Ph.: 011-41415514, 09136597244, Web.: www.chemacademy.co.in
19. If an enzyme fixes N2 in plants by evolving H2, the number of electrons and protons associated
with that, respectively are
(a) 6 and 6 (b) 8 and 8 (c) 6 and 8 (d) 8 and 6
20. The extent of p-electron conjugation in macrocyclic rings of (1) heme, (2) coenzyme B12 and (3)
chlorophyll follows the order
(a) 1 > 3 > 2 (b) 1 > 2 > 3 (c) 3 > 1 > 2 (d) 2  1  3
21. Under physiological condition, oxygen is binding to deoxyhemoglobin and deoxymyoglobin, the
binding curve and its pH dependence, respectively, are
(a) Sigmoidal and pH dependent; hyperbolic and pH independent
(b) Hyperbolic and pH independent; sigmoidal and pH dependent
(c) Sigmoidal and pH independent; hyperbolic and pH dependent
(d) Hyperbolic and pH dependent; sigmoidal and pH independent
22. Match the metalloproteins in Column-I with their function in column-II
Column-I Column-II
I. Oxygemocyanin P. Hydrolysis of C-terminal peptide bond
II. Carbonic anhydrase Q. Methylation
III. Cytochrome P450 R. Conversion of CO2 to H2CO3
IV. Carboxy-peptidase A S. Oxidation of alkene
T. Oxygen storage

CHEM ACADEMY
The correct answer is :
(a) I-U; II-R, III-S, IV-P
U. Oxygen transport

(b) I-T; II-R, III-P, IV-U


(c) I-U; II-Q, III-R, IV-P (d) I-T; II-S, III-U, IV-P
23. Identify correct statements for mercury as an environment pollutant
(A) Carbanionic biomethylation converts it to MeHg+
(B) Thiol group of cysteine has strong affinity for mercury
(C) Mercury containing industrial catalyst release caused Minamata disaster
The correct answer is :
(a) A and B (b) A and C (c) B and C (d) A, B and C
24. The Fe—Nporphyrin bond distances in the deoxy and oxy-hemoglobin, respectively, are
(a) ~2.1 and 2.0 Å (b) ~ 2.0 and 2.0 Å (c) ~ 2.2 and 2.3 Å (d) ~ 2.3 and 2.5 Å
25. The total number of metal ions and the number of coordinated imidazole units of histidine in the
active site of oxy-hemocyanin, respectively, are
(a) 2Cu2+ and 6 (b) 2Fe2+ and 5 (c) 2Cu– and 6 (d) Fe2+ and 3
26. The biological functions of cytochrome P450 and myoglobin are, respectively
(a) Oxidation of alekene and O2 storage (b) O2 transport and O2 storage
(c) O2 storage and electron carrier (d) Electron carrier and O2 transport
27. Deoxy-hemocyanin is
(a) Heme protein and paramagnetic (b) Colorless and diamagnetic
(c) O2 transporter and paramagnetic (d) Blue colored and diamagnetic

North Delhi: 72, Mall Road, G.T.B. Nagar, New Delhi - 110009
South Delhi: 28B/7, Jia Sarai, Near IIT, Hauz Khas, New Delhi - 110016. Mob.: 8860108204 3
Toll Free: 1800 120 5848, Ph.: 011-41415514, 09136597244, Web.: www.chemacademy.co.in
28. Match the metalloprotein in Column-I with the biological function and metal centre in Column-II
Column-I Column-II
I. Hemoglobin P. Electron carrier and iron
II. Cytochrome b Q. Electron carrier and copper
III. Vitamin B12 R. O2 transfer and copper
IV. Hemocyanin S. Group transfer reactions and cobalt
T. O2 storage and cobalt
U. O2 transport and iron
The correct match is :
(a) I-U, II-P, III-S, IV-R (b) I-T, II-P, III-S, IV-R
(c) I-U; II-T, III-P, IV-Q (d) I-T; II-U, III-Q, IV-S
29. In the absence of bound globin chain, heme group on exposure to O2 gives the iron-oxygen
species
O O
(a) (III)Fe Fe(III) (b) (III)Fe O

O Fe(III)
(c) (d) Fe(IV) = O
(III)Fe O
30. Match the metal given in Column-I with its medicinal use as a compound in Column-II.
Column-I Column-II
I. Gd
II. Au
III. Pt
CHEM ACADEMY P. Cancer
Q. Maniac depression
R. MRI contrast agent
IV. Li S. Arthritis
Correct match is:
(a) I-Q, II-R, III-S, IV-P (b) I-S, II-Q, III-P, IV-R
(c) I-R, II-S, III-P, IV-Q (d) I-P, II-Q, III-R, IV-S
31. Correct combination of number and size of rings present in a metal ion-porphine complex (in-
cluding metal ion bearing chelate rings) is:
(a) Four 5-membered and four-6-membered (b) Two 5-membered and six 6-membered
(c) Six 5-membered and two 6-membered (d) Five 5-membered and three 6-membered
32. In the catalytic hydration of CO2 by carbonic anhydrase, CO2 first interacts with
(a) OH group of the active site of the enzyme and then with zinc
(b) H2O of the active site of the enzyme and then the zinc
(c) Zinc of the active site of the enzyme and then with OH group
(d) Zinc of the active site of the enzyme and then with H2O
33. The number of inorganic sulphur (or sulphide) atoms present in the metalloprotein active sites of
rubredoxin, 2-iron ferredoxin and 4-iron ferredoxin, respectively, are
(a) 0, 2 and 4 (b) 2, 4 and 3 (c) 0, 4 and 2 (d) 0, 2 and 3

North Delhi: 72, Mall Road, G.T.B. Nagar, New Delhi - 110009
South Delhi: 28B/7, Jia Sarai, Near IIT, Hauz Khas, New Delhi - 110016. Mob.: 8860108204 4
Toll Free: 1800 120 5848, Ph.: 011-41415514, 09136597244, Web.: www.chemacademy.co.in
34. From the following transformations
(A) Epoxidation of alkenes (B) Diol dehydrase reaction
(C) Conversion of ribonucleotide-to-deoxyribonucleotide
(D) 1, 2-csarbon shift in organic substrates
Those promoted by coenzyme B12 are:
(a) A and B (b) B, C and D (c) A, B and D (d) A, B and C
35. Match the items of Column-I with the appropriate items in column II:
Column-I Column-II
I. Metallothioneins P. cis-[Pd(NH3)2Cl2]
II. Plastocyanin Q. Cysterine rich protein
III. Ferritin R. Electron transfer
IV. Chemotherapy S. Iron transport
T. Iron storage
U. Carboplatin
The correct answer is:
(a) I-Q, II-R, III-T, IV-S (b) I-Q, II-R, III-S, IV-P
(c) I-Q, II-R, III-T, IV-U (d) I-R, II-T, III-U, IV-Q
36. The resonance Raman stretching frequencies (in cm–1) of the bound O2 species in
oxyhemerythrin and oxy-hemoglobin, respectively, are:

37. CHEM ACADEMY


(a) ~850 and 1100 (b) ~750 and 850 (c) ~850 and 850 (d) ~1100 and 850
In vitro reaction of an excess of O2 with free heme B in aqueous medium the end product is :
(a) Hematin (b) [O2–-Fe(III)-Protoporphyrin-IX]
(c) Heme B(O)2 (d) Oxoferrylprotoporphyrin-IX cation radical
38. Consider the following statements for metallothioneins :
(I) They contain about 30% cysteine residues
(II) They prefer to bind soft metal ions such as Cd(II), Hg(II) and Zn (II)
(III) They are involved in electron transfer reactions
(IV) They are low molecular weight proteins
Correct statements are :
(a) I, II and III (b) I, II and IV (c) I, III and IV (d) II and III
39. Consider the following statements for deoxyhemerythrin and deoxy-hemocyanin :
(I) They are involved in O2 transport in biological systems
(II) They contain two metal ions in their active site
(III) Active site metal centres are bridged by amino acid residues
(IV) They prefer to bind only one O2 per active site
The correct statements are
(a) I, II and IV (b) I, III and IV (c) II, III and IV (d) I and III
40. The metal ion present in carbonic anhydrase is :
(a) Mn (b) Zn (c) Cu (d) Fe

North Delhi: 72, Mall Road, G.T.B. Nagar, New Delhi - 110009
South Delhi: 28B/7, Jia Sarai, Near IIT, Hauz Khas, New Delhi - 110016. Mob.: 8860108204 5
Toll Free: 1800 120 5848, Ph.: 011-41415514, 09136597244, Web.: www.chemacademy.co.in
41. The metals involved in nitrogenase are:
(a) Fe and Mg (b) Mo and K (c) Mo and Fe (d) Fe and K
42. Match the following :
Column-I Column-II
I. Liver alcohol dehydrogenase P. Cu at the active site
II. Cytochrome C oxidase Q. Fe and Cu at the active site
III. Hemocyanin R. Zn at the active site
IV. Myoglobin S. Fe at the active site
T. Mo at the active site
U. Cu and Zn at the active site
(a) I-U, II-Q, III-P, IV-S (b) I-R, II-Q, III-P, IV-S
(c) I-R, II-Q, III-S, IV-T (d) I-T, II-U, III-P, IV-Q
43. Nature has chosen Zn (II) ion at the active site of many hydrolytic enzymes because
(a) Zn(II) is poor Lewis acid
(b) Zn(II) does not have chemically accessible redox states
(c) Zn(II) forms both four and higher coordination complexes
(d) Zn(II) forms weak complexes with oxygen donor ligands.
44. Match the following :
Column-I Column-II

CHEM ACADEMY
I. Ferritin
II. Vitamin B12
III. Cytochromes
P. Electron transport
Q. Ionophore
R. Oxygen transport
IV. Valinomycin S. Nitrogen fixation
T. Organometallic enzyme
U. Iron storage
(a) I-U, II-S, III-Q, IV-P (b) I-P, II-R, III-U, IV-S
(c) I-R, II-V, III-S, IV-U (d) I-S, II-T, III-P, IV-Q
45. The metal present at the active site of the protein carboxypeptidase A is:
(a) Zinc (b) Molybdenum (c) Magnesium (d) Cobalt
46. Match the following :
Column-I Column-II
I. Cytochrome P. Molybdenum
II. Calmodulin Q. Potassium
III. Chlorophyll R. Magnesium
IV. Alcohol dehydrogenase S. zinc
T. Iron
U. Calcium
(a) I-T, II-U, III-R, II-T (b) II-Q, II-R, II-S, II-U
(c) III-R, III-S, III-U, III-R (d) IV-S, IV-T, IV-Q, IV-S

North Delhi: 72, Mall Road, G.T.B. Nagar, New Delhi - 110009
South Delhi: 28B/7, Jia Sarai, Near IIT, Hauz Khas, New Delhi - 110016. Mob.: 8860108204 6
Toll Free: 1800 120 5848, Ph.: 011-41415514, 09136597244, Web.: www.chemacademy.co.in
47. Iron-sulphur clusters in biological systems are involved in
(a) Proton transfer (b) Atom transfer (c) Group transfer (d) Electron transfer
48. When a reduced cytochrome transfers an electron from its Fe(II) to the bound O2.
(a) The bond order of O2 is reduced by one and v o2 decreases

(b) A metal bound superoxide is formed and v o2 decreases

(c) A metal bound superoxide is formed and v o2 increases

(d) The bond order of O2 is reduced by one and v o2 increases


49. In photosynthesis, the predominant metal present in the reaction centre of photosystem II is:
(a) Zn (b) Cu (c) Mn (d) Fe
50. Zn in carbonic anhydrase is co-ordinated by three histidine and one water molecule. The reaction
of CO2 with this enzyme is an example of:
(a) Electrophilic addition (b) Electron transfer
(c) Nucleophilic addition (d) Electrophilic substitution
51. In biological systems, the metal ions involved in electron transportare:
(a) Na+ and K+ (b) Zn2– and Mg2– (c) Ca2+ and Mg2+ (d) Cu2+ and Fe3–
52. In the transformation of oxyhaemoglobin to deoxyhaemoglobin
(a) Fe2+ in the low spin state changes to Fe2+ in the high spin state
(b) Fe2+ in the low spin state changes to Fe3+ in the low spin state
CHEM ACADEMY
(c) Fe2+ in the high spin state changes to Fe2+ in the low spin state
(d) Fe2+ in the high spin state changes to Fe3+ in the high spin state
53. Among 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:
(a) Fe and Zn (b) Mg and Fe (c) Co and Mo (d) Ca and Cu
54. A well known naturally occurring organometallic compound is :
(a) Vitamine B12 coenzyme (b) Chlorophyll
(c) Cytochrome P-450 (d) Myoglobin
55. Haemoglobin is an oxygen carrying protein. The correct statement about oxy-haemoglobin is that
(a) The metal is low spin in +3 oxidation state while dioxygen is in O2– form
(b) The metal is high spin in +3 oxidation state while dioxygen is in O2– form
(c) The metal is low spin in +3 oxidation state while dioxygen is in neutral form
(d) The metal is high-spin in +3 oxidation state while dioxygen is in neutral form
56. Oxymyoglobin Mb(O2) and oxhyhemoglobin Hb(O2)4, respectively, are:
(a) Paramagnetic and paramagnetic (b) Diamagnetic and diamagnetic
(c) Paramagnetic and diamagnetic (d) Diamagnetic and paramagnetic
57. Mg2+ is preferred in photosynthesis by chlorophyll because
(a) It has strong spin-orbit coupling (b) It has weak spin-orbit coupling
(c) It is a heavy metal (d) It binds strongly with chlorophyll

North Delhi: 72, Mall Road, G.T.B. Nagar, New Delhi - 110009
South Delhi: 28B/7, Jia Sarai, Near IIT, Hauz Khas, New Delhi - 110016. Mob.: 8860108204 7
Toll Free: 1800 120 5848, Ph.: 011-41415514, 09136597244, Web.: www.chemacademy.co.in
58. Among the given pH values, the O2 binding efficiency of hemoglobin is maximum at:
(a) 6.8 (b) 7.0 (c) 7.2 (d) 7.4
59. Identify the function of hemocyanin and the metal responsible for it
(a) O2 transport and Fe (b) O2 transport and Cu
(c) Electron transport and Fe (d) Electron transfer and Cu
60. During oxygen transport by hemerythrin, oxygen is bound as
(a) O 2 to one Fe(III) only (b) HO 2 to one Fe(III) only

(c) O 22  to one Fe(II) and one Fe(III) (d) O22  to two Fe(II)
61. At pH 7.2 and 10 Torr oxygen partial pressure, the extent of O2 binding is:
(a) High for both hemoglobin and myoglobin (b) High for hemoglobin and low for myoglobin
(c) High for myoglobin and low for hemoglobin (d) Low for both hemoglobin and myoglobin
62. Amongst the following, the group that is bound to the metal ion in coenzyme B12 is:
(a) Methyl (b) Cyanide (c) Adenosyl (d) Hydroxyl
63. The metal ion and the macrocyclic skeleton present in the green pigment of plants, respectively,
are:
(a) Mg(II) and chlorin (b) Mg(II) and corrin (c) Mn(II) and chlorin (d) Mg(II) and porphine
64. The vo–o resonance Raman stretching frequency (in cm–1) of the O2 coordinated to iron centre in
oxy-hemoglobin is nearly:
(a) 1100 (b) 850 (c) 1550 (d) 1950
65.
CHEM ACADEMY
Correct match for the coenzymes in list-I with their function in list-II is
List - I List - II
(a) NaDH (i) Oxidation
(b) FAD (ii) Acyl group transfer
(c) CoASH (iii) Reduction
Codes:
(a) (b) (c) (a) (b) (c)
(a) (i) (ii) (iii) (b) (iii) (i) (ii)
(c) (iii) (ii) (i) (d) (ii) (i) (iii)
66. For the catalytic activity of Cu and Zn containing enzyme, superoxide dismutase. What is/are the
correct statement(s)?
(A) Cu and Zn both are essential (B) Only Cu is essential
(C) Zn is essential and Cu may be replaced by any other divalent metal atom
(D) Zn may be replaced by any other divalent metal atom
(a) A only (b) C only (c) D only (d) B and D
67. Consider the following statements for the oxygenation of hemocyanin
(A) Oxidation state of both copper atoms changes by two
(B) It becomes intense blue from colourless
(C) Dioxygen is reduced to O2–2
(D) The   2 , 2 bond form between each oxygen and copper atoms

North Delhi: 72, Mall Road, G.T.B. Nagar, New Delhi - 110009
South Delhi: 28B/7, Jia Sarai, Near IIT, Hauz Khas, New Delhi - 110016. Mob.: 8860108204 8
Toll Free: 1800 120 5848, Ph.: 011-41415514, 09136597244, Web.: www.chemacademy.co.in
The correct statements are
(a) A & C (b) B & C (c) A, B and C (d) B, C & D
68. The chelate rings made by macrocyclic ligand in vitamin B12 are
(a) One five membered and three six membered
(b) Two five membered and two six membered
(c) Three five membered and one six membered
(d) Four six membered
69. Arrange the following molecules in order of increasing fundamental vibrational frequencies

(a) O 22  O 2  O 2  O 2 (b) O 2  O 2  O 2  O22

(c) O 22  O 2  O 2  O 2 (d) O 2  O 2  O 2  O22


70. Match the items given below in the three columns
Mettalloprotein Species coordinated Resonance Raman
to metal centre O-O stretching frequency (cm–1)
A. Oxymyoglobin I. n2, n2O2–2 X. 844
B. Oxyhemocyanin II. HO2– Y. 803

C. Oxyhemerythrin III. O2 Z. 1105
Correct matches
(a) A-III-Z, B-I-Y, C-II-X (b) A-II-Y, B-I-X, C-III-Z

CHEM ACADEMY
(c) A-III-Y, B-I-Z, C-II-X (d) A-I-X, B-II-Y, C-III-Z

ANSWER KEY
1. b 2. b 3. b 4. d 5. c 6. d 7. a
8. a 9. a 10. a 11. b 12. b 13. a 14. b
15. d 16. c 17. d 18. a 19. b 20. a 21. a
22. a 23. d 24. a 25. a 26. a 27. b 28. a
29. a 30. c 31. a 32. a 33. a 34. b 35. c
36. a 37. a 38. b 39. a 40. b 41. c 42. b
43. b 44. d 45. a 46. a 47. d 48. b 49. c
50. a 51. d 52. a 53. a 54. a 55. a 56. b
57. d 58. d 59. b 60. b 61. c 62. c 63. a
64. a 65. b 66. b 67. d 68. a 69. a 70. a

North Delhi: 72, Mall Road, G.T.B. Nagar, New Delhi - 110009
South Delhi: 28B/7, Jia Sarai, Near IIT, Hauz Khas, New Delhi - 110016. Mob.: 8860108204 9
Toll Free: 1800 120 5848, Ph.: 011-41415514, 09136597244, Web.: www.chemacademy.co.in

You might also like