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C H A P T E R 13 Bioinorganic Chemistry
Syllabus
Ion (Na+ and K+) transport, oxygen binding, transport and utilization, electron transfer reactions, nitrogen fixation,
­metalloenzymes containing magnesium, molybdenum, iron, cobalt, copper and zinc.

CHAPTER ANALYSIS
Topic GATE GATE GATE GATE GATE GATE GATE GATE GATE GATE GATE
2010 2011 2012 2013 2014 2015 2016 2017 2018 2019 2020
Ion (Na+ and K+)
transport
Oxygen binding, 1 1 2 1 1 1 1
transport and utilization
Electron transfer
reactions
Nitrogen fixation
Metalloenzymes 1 1 1 1 2 1 1 1 1
containing magnesium,
molybdenum, iron,
cobalt, copper and zinc

QUESTIONS

1. The metal ion present in carbonic anhydrase is 4. The correct match between Column I and Column II is:
(a) Mn (b) Zn Column I Column II
(c) Cu (d) Fe (P) Liver alcohol (I) Cu at the active site
(GATE 2001: 1 Mark) dehydrogenase
2. The metals involved in nitrogenase are (Q) Cytochrome C oxidase (II) Fe and Cu at the
active site
(a) Fe and Mg. (b) Mo and K.
(c) Mo and Fe. (d) Fe and K. (R) Hemocyanin (III) Zn at the active site
(GATE 2002: 2 Marks) (S) Myoglobin (IV) Fe at the active site
(V) Mo at the active site
3. Nature has chosen Zn(II) ion at the active site of many
hydrolytic enzymes because (VI) Cu and Zn at the
active site.
(a) Zn(II) is poor Lewis acid.
(a) P-VI; Q-II; R-I; S-IV
(b) Zn(II) does not have chemically accessible redox
states. (b) P-III; Q-II; R-I; S-IV
(c) Zn(II) forms both four and higher coordination (c) P-III; Q-II; R-IV; S-V
complexes. (d) P-V; Q-VI; R-I; S-II
(d) Zn(II) forms weak complexes with oxygen donor (GATE 2003: 2 Marks)
ligands.
(GATE 2003: 1 Mark)

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224 GATE chemistry Chapter-wise Solved Papers

5. The correct match between Column I and Column II is: 10. When a reduced cytochrome transfers an electron from
Column I Column II its Fe(II) to the bound O2
(P) Ferritin (I) Electron transport (a) the bond order of O2 is reduced by one and νO2
(Q) Vitamin B12 (II) Ionophore decreases.
(b) a metal bound superoxide is formed and νO2
(R) Cytochromes (III) Oxygen transport
decreases.
(S) Valinomycin (IV) Nitrogen fixation (c) a metal bound superoxide is formed and νO2
(V) Organometallic increases.
enzyme (d) the bond order of O2 is reduced by one and νO2
(VI) Iron storage. increases.
(a) P-VI; Q-IV; R-II; S-I (GATE 2006: 2 Marks)
(b) P-I; Q-III; R-VI; S-IV
11. In biological systems, the metal ion involved in the
(c) P-III; Q-V; R-IV; S-VI ­dioxygen transport besides Fe is
(d) P-VI; Q-V; R-I; S-II
(a) Co (b) Zn
(GATE 2004: 2 Marks) (c) Mg (d) Cu
6. The metal present at the active site of the protein (GATE 2006: 2 Marks)
­carboxypeptidase A is
12. In photosynthesis, the predominant metal present in the
(a) zinc. (b) molybdenum.
reaction centre of photosystem II is
(c) magnesium. (d) cobalt.
(a) Zn (b) Cu
(GATE 2005: 1 Mark)
(c) Mn (d) Fe
7. The correct match between the Column I and Column II is: (GATE 2007: 1 Mark)
Column I Column II
13. Zn in carbonic anhydrase is coordinated by three histi-
(P) Cytochrome (I) Molybdenum dine and one water molecule. The reaction of CO2 with
(Q) Calmodulin (II) Potassium this enzyme is an example of
(R) Chlorophyll (III) Magnesium (a) electrophilic addition.
(Q) Alcohol dehydrogenase (IV) Zinc (b) electron transfer.
(V) Iron (c) nucleophilic addition.
(VI) Calcium (d) electrophilic substitution.
(a) P-V; Q-VI; R-III; S-IV (GATE 2007: 1 Mark)
(b) P-II; Q-III; R-IV; S-VI
14. In biological systems, the metal ions involved in elec-
(c) P-III; Q-IV; R-VI; S-III tron transport are
(d) P-IV; Q-V; R-II; S-IV (a) Na+ and K + . (b) Zn2+ and Mg2+.
(GATE 2005: 2 Marks) (c) Ca2+ and Mg2+. (d) Cu2+ and Fe3+.
8. Iron-sulphur clusters in biological systems are involved in (GATE 2008: 2 Marks)
(a) proton transfer. (b) atom transfer.
15. In the transformation of oxyhaemoglobin to deoxyhae-
(c) group transfer. (d) electron transfer. moglobin
(GATE 2006: 1 Mark) (a) Fe2+ in the low spin state changes to Fe2+ in the high
9. The amino acid side chain high affinity for Ca2+ and Cu2+ spin state.
in metalloproteins is (b) Fe2+ in the low spin state changes to Fe3+ in the low
spin state.
(a) carboxylate in both the cases.
(c) Fe2+ in the high spin state changes to Fe2+ in the low
(b) imidazole in both the cases. spin state.
(c) caboxylate for Ca2+ and imidazole for Cu2+. (d) Fe2+ in the high spin state changes to Fe3+ in the
(d) imidazole for Ca2+ and caboxylate for Cu2+. high spin state.
(GATE 2006: 2 Marks) (GATE 2009: 1 Mark)

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Chapter 13 • Bioinorganic Chemistry 225

16. Among the following pair of metal ions present in nature, 23. Among the given pH values, the O2 binding efficiency of
the first one functions as an electron-transfer agent and hemoglobin is maximum at
the second one catalyzes the hydrolysis reactions. The (a) 6.8 (b) 7.0
correct pair is (c) 7.2 (d) 7.4
(a) Fe and Zn. (b) Mg and Fe. (GATE 2015: 1 Mark)
(c) Co and Mo. (d) Ca and Cu.
24. Identify the function of hemocyanin and the metal
(GATE 2010: 1 Mark)
responsible for it.
17. A well-known naturally occurring organometallic (a) O2 transport and Fe.
­compound is (b) O2 transport and Cu.
(a) vitamin B12 coenzyme. (b) chlorophyll. (c) electron transport and Fe.
(c) cytochrome P450. (d) myoglobin. (d) electron transport and Cu.
(GATE 2011: 1 Mark) (GATE 2015: 2 Marks)
18. The red color of oxyhaemoglobin is mainly due to the 25. During oxygen transport by hemerythrin, oxygen is
(a) d−d transition. bound as
(b) metal to ligand charge transfer transition. (a) O 2− to one Fe(III) only.
(c) ligand to metal charge transfer transition. (b) HO 2− to one Fe(III) only.
(d) intraligand π-π* transition. (c) O 2−
2 to one Fe(II) and one Fe(III).

(GATE 2011: 1 Mark) (d) O 2−

2 to two Fe(II).

19. Hemoglobin is an oxygen carrying protein. The correct (GATE 2016: 1 Mark)
statement about oxy-hemoglobin is that 26. At pH 7.2 and 10 torr oxygen partial pressure, the extent
(a) the metal is low spin in +3 oxidation state while of O2 binding is
dioxygen is in O 2− form. (a) high for both hemoglobin and myoglobin.
(b) the metal is high spin in +3 oxidation state while (b) high for hemoglobin and low for myoglobin.
dioxygen is in O 2− form. (c) high for myoglobin and low for hemoglobin.
(c) the metal is low spin in +3 oxidation state while (d) low for both hemoglobin and myoglobin.
dioxygen is in neutral form. (GATE 2016: 1 Mark)
(d) the metal is high spin in +3 oxidation state while
dioxygen is in neutral form. 27. Amongst the following, the group that is bound to the
metal ion in coenzyme B12 is
(GATE 2012: 2 Marks)
(a) methyl. (b) cyanide.
20. Oxymyoglobin Mb(O2) and oxyhemoglobin Hb(O2)4, (c) adenosyl. (d) hydroxyl.
respectively, are
(GATE 2016: 2 Marks)
(a) paramagnetic and paramagnetic.
(b) diamagnetic and diamagnetic. 28. The metal ion and the macrocyclic skeleton present in
the green pigment of plants, respectively, are
(c) paramagnetic and diamagnetic.
(a) Mg(II) and chlorin.
(d) diamagnetic and paramagnetic.
(b) Mg(II) and corrin.
(GATE 2013: 1 Mark)
(c) Mn(II) and chlorin.
21. The number of oxygen molecule(s) that a molecule of (d) Mg(II) and porphine.
hemerythrin can transport is _______.
(GATE 2017: 2 Marks)
(GATE 2013: 1 Mark)
29. The coordination geometries around the copper ion of
22. Mg2+ is preferred in photosynthesis by chlorophyll plastocyanin (a blue-copper protein) in oxidized and
because reduced form, respectively, are
(a) it has strong spin-orbit coupling. (a) tetrahedral and square-planar.
(b) it has weak spin-orbit coupling. (b) square-planar and tetrahedral.
(c) it is a heavy metal. (c) distorted tetrahedral for both.
(d) it binds strongly with chlorophyll. (d) ideal tetrahedral for both.
(GATE 2014: 2 Marks) (GATE 2018: 1 Mark)

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30. The O2 coordinated to metal ion centres in oxy-­myoglobin (a) P-III; Q-II; R-I; S-IV
and oxy-hemocyanin exists, respectively, as (b) P-III; Q-I; R-IV; S-II
(a) superoxide and peroxide. (c) P-IV; Q-I; R-III; S-II
(b) superoxide and superoxide. (d) P-IV; Q-II; R-I; S-III
(c) peroxide and peroxide. (GATE 2019: 2 Marks)
(d) superoxide and oxygen.
32. In oxyhemocyanin, the coordination number, mode of
(GATE 2018: 2 Marks) oxygen binding, color and the net magnetic behavior of
31. Match the Column I (metalloproteins) with Column II copper ions, respectively are
(their respective functions). (Given: Atomic number of Cu is 29)
Column I Column II (a) four, μ-η1 : η1 -O 2− , colorless and paramagnetic.
(P) Ferritin (I) Electron transfer (b) five, μ-η2 : η2 -O 2− , colorless and paramagnetic.
(Q) Rubredoxin (II) Acid-base catalysis (c) five, μ-η2 : η2 -O 22 − , blue and diamagnetic.
(R) Cobalamin (III) Metal storage (d) four, μ-η1 : η1 -O 22 − , blue and diamagnetic.
(S) Carbonic anhydrase (IV) Methyl transfer (GATE 2020: 1 Mark)
33. The following table Column I the reaction/conversion catalyzed by Column II metalloenzymes.
Column I (Reaction/Conversion) Column II (Metalloenzymes)
(P) R – H + O 2 + 2H + + 2e − → R – OH + H 2 O (I) Coenzyme B12
(Q) O 2 + 4e − + 8H + → 2H 2 O + 4 H + (II) Cytochrome P450
(R) 2H 2 O 2 → 2H 2 O + O 2 (III) Cytochrome c oxidase
(S) NH 2 – CH 2 – CO 2 H → NH 2 – CH(CH 2 OH) – CO 2 H (IV) Catalase
The correct combination is
(a) P-II; Q-I; R-III; S-IV (b) P-IV; Q-III; R-II; S-I
(c) P-II; Q-III; R-IV; S-I (d) P-I; Q-IV; R-III; S-II
(GATE 2020: 2 Marks)

Answer KeyS

1. (b) 2. (c) 3. (d) 4. (b) 5. (b) 6. (a) 7. (a) 8. (d) 9. (c) 10. (a)
11. (d) 12. (c) 13. (c) 14. (d) 15. (a) 16. (a) 17. (a) 18. (d) 19. (a) 20. (b)
21. (1) 22. (b) 23. (d) 24. (b) 25. (b) 26. (c) 27. (c) 28. (a) 29. (c) 30. (a)
31. (b) 32. (c) 33. (c)

HINTS AND Explanations

1. Concept: Metalloenzymes 4. Concept: Metalloenzymes

(b) Carbonic anhydrase is a metalloenzyme in which (b) The correct match is
Zn is present as a metal. (P) → (III): Liver alcohol dehydrogenase - Zn at the
active site
2. Concept: Metalloenzymes
(Q) → (II): Cytochrome C oxidase - Fe and Cu at the
(c) The metals involved in nitrogenase are Fe and Mo. active site
3. Concept: Metalloenzymes (R) → (I): Hemocyanin - Cu at active site
(d) Because Zn(II) forms weak complexes with (S) → (IV): Myoglobin - Fe at active site
­oxygen donor ligands as this will enable easy hydrolysis
5. Concept: Metalloenzymes
of Zn(II) complexes. In first three options, Zn(II) form
a very stable tetrahedral complex. (d) The correct match is
(P) → (VI): Ferritin - Iron storage

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Chapter 13 • Bioinorganic Chemistry 227

(Q) → (V): Vitamin B12 - Organometallic enzyme B −BH

+
2+ H
(R) → (I): Cytochromes - Electron transport (His)3 Zn O (His)3 Zn
+ –
OH
(S)→ (II): Valinomycin - Ionophore H
CO2 Nucleophilic
6. Concept: Metalloenzymes addition
–
(a) The metal present in carboxypeptidase A is Zn. O
2+ + H2O + +
(His)3 Zn OH2 (His)3 Zn O C
7. Concept: Metalloenzymes − H2CO3
+H2CO3 O
H
(a) The correct match between the pigments and the
metal ion present in them is:
(P) → (V): Cytochrome - C – Iron containing protein.
(Q) → (VI): Calmodulin – Calcium modulated protein. 14. Concept: Ion (Na+ and K+) Transport
(R) → (III): Chlorophyll – Magnesium. (d) Na+ and K+ are involved in Na-K pump in ion
exchange process and in electron transfer process Cu2+
(S) → (IV): Alcohol dehydrogenase – mammalian alco-
and Fe3+ are involved.
hol dehydrogenase contains Zn as a structural site.
15. Concept: Haemoglobin
8. Concept: Electron Transfer Reactions
(a) During the transformation of oxyhaemoglobin to
(d) Iron-sulphur clusters are involved in electron
deoxyhaemoglobin Fe(II) changes from low spin to high
transfer reactions mainly as ferredoxins.
spin Fe2+.
9. Concept: Metalloenzymes HbO 2  Hb + O 2
(c) Calcium ion shows a greater tendency to bind oxy- oxy Hb deoxy Hb
gen ligands so it will bind with carboxylate. However, Fe(II) L.S. Fe(II) H.S
Cu2+ ion has more tendency to bind with nitrogen donor
ligands, so it binds with imidazole. 16. Concept: Metalloenzymes
(a) Iron functions as an electron transport agent
10. Concept: Electron Transfer Reactions
and zinc catalysis the hydrolysis of peptide bond via
(a) Cytochrome C helps in redox reactions. In elec- ­carboxypeptidase enzyme.
tron transfer Fe(II) does not bind with O2. Thus, electron
donation will decreases and the bond order decreases by 17. Concept: Metalloenzymes Containing Mg, Mo, Fe,
one, hence, the νO2 will decrease. Co, Cu
(a) Vitamin B12 coenzyme is a naturally occurring
11. Concept: Oxygen Transport in Biological Systems
organometallic compound. In this metalloenzyme, there
(d) In biological systems oxygen transport is done is one metal and carbon bond, where Co binds with alkyl
by using metalloproteins containing iron and copper. group.
Hemocyanin is the copper containing metalloprotein
which is used for oxygen transport. 18. Concept: Oxygen Binding
(d) In hemoglobin, iron center is bind to four N-atoms
12. Concept: Metalloenzymes
of porphyrin ring which is a highly conjugated system.
(c) The metal ion present in reaction centre of photo- The π-π* transition of ligand is the main reason for red
system II is manganese (Mn). color of hemoglobin.
13. Concept: Metalloenzymes 19. Concept: Oxygen Binding
(c) Zn(II) ion promotes the ionization of bound H2O, (a) In oxyhemoglobin, the metal ion is low spin in +3
which leads to the formation of OH– and OH– attack the oxidation state which binds with superoxide ion (O 2− ).
carbon of CO2 via nucleophilic addition reaction. Thus, the oxy-form is considered as diamagnetic.

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20. Concept: Oxygen Binding 25. Concept: Metalloenzymes

(b) The Fe is present as Fe(II) in both oxymyoglobin (b) The structure of oxy-hemerythrin is;
and oxyhemoglobin, in low spin state. As O 2− is ­acting
as a π-acceptor ligand, so both oxyhemoglobin and HN O
H O
­myoglobin are diamagnetic in nature.
N
O N NH
21. Concept: Oxygen Transport N
(III) (III)
HN Fe Fe
(1) The protein contains one oxygen atom bridging O O
N O N
between two Fe atoms. O NH

HN N
H H
N +
N
O
N NH Thus, it has −OOH − linkage to one Fe(III) only.
HN Fe Fe
N N 26. Concept: Oxygen Binding
OO OO
N NH (c) The oxygen affinity of hemoglobin decreases as pH
H decreases from the value of 7.4. Thus, as hemoglobin
moves into a region of low pH, its tendency to release
oxygen increases. At pH = 7.4 and partial pressure of
O2
oxygen 10 torr, the binding tendency to oxygen is high
for myoglobin and low for hemoglobin.

HN 27. Concept: Metalloenzymes

H O
N +
(c) Adenosyl group bound to Co(II) metal ion in
O
N
O
N NH ­Vitamin B12.
HN Fe Fe
N HN CONH2
OO OO N
N NH CH2
H C
CH2 H3C H3C CH2 CONH2
H3C
22. Concept: Metalloenzymes Containing Magnesium CH2 CH2 CONH2
H2NOC CH2 N N
(b) Mg2+ is preferred in photosynthesis by chlorophyll
H3C Co+
because it has very weak spin-orbit coupling with the
H
excited state of porphyrin ring and hence, it does not N N CH3
quench the energy transfer.
H2NOC CH2 CH3
23. Concept: Oxygen Binding CH3 CH3 CH
CH2 2 CH2 CONH2
(d) The maximum binding of O2 to haemoglobin occur O CH2 N CH3
at physiological pH value 7.4. If pH value is gets lower C
than 7.4, hemoglobin does not bind to oxygen as well. NH N CH3
Because at lower pH, more of the H+ ions releases which H2C
−O HO
increases the CO2 level and the affinity of hemoglobin to C Adenosyl
H3C C C group
bind with O2 decreases. O P O H H O
H H C C
24. Concept: Metalloenzymes O
H CH2OH
(b) Hemocyanin are the metalloproteins which
­transport O2 throughout the body of some ­invertebrate Vitamin B12
animals. It contains two copper atoms (Cu) that
­
­reversibly binds a single O2 molecule.

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Chapter 13 • Bioinorganic Chemistry 229

28. Concept: Metalloenzymes Containing Magnesium 31. Concept: Metalloenzymes

(a) The metal ion and the macrocyclic ring present in (b) The function of the given metalloenzyme is given
chlorophyll (the green pigment of plants) are Mg(II) and below:
chlorin. (P) → (III): Ferritin – Metal storage
29. Concept: Metalloenzymes (Q) → (I): Rubredoxin – Electron transfer
(R) → (IV): Cobalamin – Methyl transfer
(c) Plastocyanin is a copper containing protein that
plays a vital role in electron transport process during the (S) → (II): Carbonic Anhydrase – Zn containing metal-
photosynthesis process. The geometry around copper ion loenzymes, which used in acid-base catalysis
in both oxidized and reduced form is distorted tetrahedral. 32. Concept: Oxygen Binding
S Methionine (c) Hemocyanin is a non-heme protein, it contains
copper metal and used for transport of dioxygen.
285 pm
210 The structure of oxyhemocyanin is
His pm
Cu 210 pm His His
O
– His Cu(II) Cu(II) His
S Cysteinate
His 210 pm His
His O

This is due to the three bond lengths are equal in length Thus, the coordination number of Cu(II) in this com-
plex is five, mode of oxygen binding is μ-η : η -O 2 , its
1 1 −
and one is larger than three, which makes it distorted
tetrahedral. color is blue and due to antiferromagnetic coupling is it
diamagnetic.
30. Concept: Oxygen Binding
33. Concept: Metalloenzyme
(a) The structure of oxy-myoglobin is:
(c) The correct match between the reaction and the
metalloenzyme involved is:
(P) → (II) : R − H + O 2 + 2H + + 2e − ⎯⎛⎯⎯⎯⎯
Cytochrome ⎞
→
R – ⎜ P 450 ⎟
O O Superoxide ⎜ Oxidation ⎟
⎝ ⎠

R − OH + H 2 O
R
N N (Q) → (III) : O 2 + 4e − + 8H + ⎯Cyclochrome
⎯⎯⎯
c − oxidase
→ 2H 2 O + 4 H +
Fe
(R) → (IV) : 2H 2 O 2 ⎯Catalase
⎯⎯→ 2H 2 O + O 2
R
N N

(S) → (I) : NH 2 − CH 2 − COOH ⎯⎯⎯⎯⎯ →

Coenzyme B12

R
CH 2 OH
|
N
NH 2 − CH − COOH
N
Me

In oxy-hemocyanin, O2 is present as a peroxide.

2Cu + + O 2  Cu 2 + − O 22 − − Cu 2 +
Cu (II) − O − O − Cu (II)
Peroxide

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