SOLUTIONS TO PREVIOUS YEARS QUESTIONS

FROM BIO-INORGANIC CHEMISTRY

B.Sc VI SEMESTER
Solution:
Vitamin B12 is the only, metal-containing water-soluble
vitamin that is stored in the liver and must come from the
diet.Vitamin B12 is a collective term for a group of cobalt-
containing compounds known as corrinoids which when
assembled with 5th and 6th position ligands are known as
cobalamins.
Cobalt is an integral part of vitamin B12 and therefore essential for
the function of cells. Cobalt is also involved in the production of
red blood cells and the production of antibacterial and antiviral
compounds that prevent infections. It also plays a key role in the
metabolism of fats and carbohydrates as well as the synthesis of
proteins and conversion of folate in their active form. Cobalt in
vitamin B12 is needed to maintain normal bone marrow function for
producing erythrocytes. Consequently a deficiency of cobalt results
in limitation of vitamin B12 supply which may lead to nutritional
type of anaemia, whereas an excess of cobalt results in over
production of erythrocytes causing polycythemia (High Red Blood
Cell Count). The polycythemia effect may be pharmacological one
due to the action of cobalt inhibiting certain respiratory enzymes
e.g., cytochrome oxidase succinate dehydrogenase etc.
Solution:

The elements which are absolutely necessary for life

process and are found in low concentration are called
essential trace elements .

Essential elements from p-block: B, Si, I2, Se

Essential elements from d-block: Fe, Cu, Zn, V

Solution:
The structural isomer of a platinum complex that
exhibits anti-cancer activity is cis- platin (cis-
diamminedichloroplatinum(II)) known as cis-DDP
Solution:
Mercury Neurological diseases and kidneys problem
Lead Anaemia
Beryllium Lung cancer
Aluminium Central nervous system
Solution:
The two alkali metals, sodium, and potassium are very important
and play a vital role in biological systems, These are highly mobile
unipositive cations forming soluble salts. They are strongly
solvated in water. Our bodies obtain them from plants. i.e. from
fruits and vegetables, common salt is the most important source of
sodium in the diet. Potassium is present in coffee, tea, cocoa, dried
beans, molasses, green leafy vegetables, milk, fish, bananas,
oranges, pineapples, potatoes etc. Daily requirements of NaCl is
minimum 5-10 gm. and of potassium is 4 gm approximately. Since
the average intake is much above these values, deficiencies of these
ions are rarely observed.
Functions: Sodium is a major cation in blood plasma of vertebrates
i.e. outside the cells while potassium is a major cation in cytoplasm
i.e., inside the cells. The difference in Na+ and K+ concentration
inside and outside the cell creates a potential difference across the
cell membrane. This allows nerve fibers to conduct impulses and the
muscles to contract. Both ions are used to maintain constant osmotic
pressures on either side of the cell wall. Both are the part of the
regulatory system of acid-base balance. Both the ions are needed for
the smooth working of muscles and the nervous system i.e., they
maintain the sensitivity of nerves and control the muscles.
For e.g., Na+ ions depresses the activity of muscle enzyme and are
required for muscle contraction. K+ ions permit the heart muscles
to relax between the beats. They are charge carriers. Na+ and K+
are structure promoters for both protein and polynucleic acid, K+
especially is an enzyme activator. In the form of compounds, they
help in various activities for example. NaCl is a source of HCl for
gastric juices and bicarbonate generally is a buffer in maintaining
acid-base balance of body fluids and in the transportation of CO2

Deficiency or excess of sodium and potassium: Sodium

deficiency shows a reduction in fat deposit, atrophy of muscle and
testis, lung infection, retarded bone growth and reduction in
osteoid tissue. Deficiency of sodium also reduces blood pressure
and causes circulatory failure. Excess of sodium increases blood
pressure i.e., hypertension. Deficiency of potassium reduces
heartbeats, causes scarring of the heart muscle, hypertrophy of
kidneys and paralysis of muscles.
Solution:
Definition of Cooperativity : Deoxy-hemoglobin (deoxy-
Hb) has relatively low affinity for oxygen, but when one
molecule of oxygen binds to a single heme, the oxygen
affinity increases, allowing the second molecule to bind
more easily, and the third and fourth even more easily. This
phenomenon of increasing oxygen affinity at second, third
and fourth sites in Hb is known as Cooperativity.

Refer solution (alternate answer) to Question No 10

for structural changes
Q7.

Solution:
 Q8.

Solution:
1. Metalloprotein is a generic term for a protein that contains a metal ion
cofactor. Metalloproteins have many different functions in cells, such as in
enzymes, transport and storage proteins, and signal transduction proteins.
The metal ion is usually coordinated by nitrogen, oxygen or sulfur atoms
belonging to amino acids in the polypeptide chain and/or a macro cyclic
ligand incorporated into the protein. The presence of the metal ion allows
metalloenzymes to perform functions such as redox reactions that cannot
easily be performed by the limited set of functional groups found in amino
acids.
2. The various modes of metal-protein interaction include metal-, ligand-, and
enzyme-bridge complexes. Metals can serve as electron donors or
acceptors, Lewis acids or structural regulators. Those that participate
directly in the catalytic mechanism usually exhibit anomalous
physicochemical characteristics reflecting their entatic state.
Solution:
There are around twenty five elements that are required
by most biological systems, including an important
number of metal ions. However, for humans, there are
ten essential metal ions. Of these, four: sodium,
potassium, calcium and magnesium, can be considered
as ‘bulk elements’, and together constitute approximately
99% of the metal ion content of the human body. The
other five transition metals manganese, iron, cobalt,
copper, zinc and molybdenum, are known as ‘trace
elements’, with much lower dietary requirements than
the bulk elements; they are nonetheless indispensable for
human life.
Solution:
Myoglobin and hemoglobin are hemeproteins whose physiological
importance is principally related to their ability to bind molecular
oxygen. Hemoglobin is a heterotetrameric oxygen transport protein
found in red blood cells (erythrocytes), whereas myoglobin is a
monomeric protein found mainly in muscle tissue where it serves as
an intracellular storage site for oxygen. Hb binds and transports
oxygen from the lungs to Myoglobin in tissues. Myoglobin is
oxygen storage protein
Mb facilitates & enhances oxygen diffusion within the cell.
When hemoglobin takes up one oxygen , the oxygenated heme
assumes a planar configuration, and the central iron atom occupies a
space in the plane of the heme group .The shape change in the heme
group has important implications for the rest of the hemoglobin
protein, as well. When the iron atom moves into the porphyrin plane
upon oxygenation, the histidine residue to which the iron atom is
attached is drawn closer to the heme group. This movement of the
histidine residue then shifts the position of other amino acids that are
near the histidine . When the amino acids in a protein are shifted in
this manner (by the oxygenation of one of the heme groups in the
protein), the structure of the interfaces between the four subunits is
altered. Hence, when a single heme group in the hemoglobin protein
becomes oxygenated, the whole protein changes its shape. In the new
shape, it is easier for the other three heme groups to become
oxygenated. Thus, the binding of one molecule of O2 to hemoglobin
enhances the ability of hemoglobin to bind more O2molecules. This
property of hemoglobin is known as "cooperative binding."
 Deoxygenated hemoglobin Oxygenated hemoglobin

In Deoxy-Hb, Fe(II) is In Oxy-Hb, Fe(II) is

in high spin state in low spin state
paramagnetic diamagnetic
bigger in size (0.78 A0) smaller in size (0.61 A0)
t2g4eg2 i.e e gorbital is filled t2g6eg0 i.e. eg orbital is empty
situated above the plane of the situated in the plane of the porphyring ring.
porphyring ring.
It is also referred to as T-state (Tensed) It is also referred to as R-state (relaxed)

Low-oxygen-affinity form High-oxygen-affinity form

Alternate answer to structural change that takes place when hemoglobin takes up one
oxygen
The heme group is nonplanar when it is not bound to oxygen; the iron
atom is pulled out of the plane of the porphyrin, towards the histidine
residue to which it is attached. This non-planar configuration is
characteristic of the deoxygenated heme group, and is commonly
referred to as a "domed" shape. The valence electrons in the atoms
surrounding iron in the heme group and the valence electrons in the
histidine residue form "clouds" of electron density. (Electron density
refers to the probability of finding an electron in a region of space.)
Because electrons repel one another, the regions occupied by the
valence electrons in the heme group and the histidine residue are
pushed apart. Hence, the porphyrin adopts the domed (nonplanar)
configuration and the Fe is out of the plane of the porphyrin ring
(Figure 1, left). However, when the Fe in the heme group binds to an
oxygen molecule, the porphyrin ring adopts a planar configuration
and hence the Fe lies in the plane of the porphyrin ring (Figure 1,
right).
 Fig. 1 left Fig.1 right
On the left is a schematic diagram showing representations of electron-density
clouds of the deoxygenated heme group (pink) and the attached histidine residue
(light blue). These regions of electron density push one another apart, and the iron
atom in the center is drawn out of the plane. (The nonplanar shape of the heme
group is represented by the bent line.)

On the right is a schematic diagram showing representations of electron-density

clouds of the oxygenated heme group (pink), the attached histidine residue (light
blue), and the attached oxygen molecule (gray). The oxygenated heme assumes a
planar configuration, and the central iron atom occupies a space in the plane of the
heme group (depicted by a straight red line).
The shape change in the heme group has important implications for
the rest of the hemoglobin protein, as well. When the iron atom
moves into the porphyrin plane upon oxygenation, the histidine
residue to which the iron atom is attached is drawn closer to the
heme group. This movement of the histidine residue then shifts the
position of other amino acids that are near the histidine . When the
amino acids in a protein are shifted in this manner (by the
oxygenation of one of the heme groups in the protein), the structure
of the interfaces between the four subunits is altered. Hence, when a
single heme group in the hemoglobin protein becomes oxygenated,
the whole protein changes its shape. In the new shape, it is easier for
the other three heme groups to become oxygenated. Thus, the
binding of one molecule of O2 to hemoglobin enhances the ability of
hemoglobin to bind more O2 molecules. This property of
hemoglobin is known as "cooperative binding."
Q11.

Solution:
(i) Deficiency of calcium causes osteoporosis
(ii) Excess of iron causes hemosiderosis
(iii) Deficiency of iodine causes Hypothyroidism
(iv) Excess of copper causes Wilson’s disease
Solution:
An interesting example of active transport in biological system
Na+/K+ pump present in animal cells. This pumps Na+and K+
out of and into the cell respectively using energy released by
hydrolysis of ATP. In order to maintain the cell potential, cells must
keep a low concentration of sodium ions and high levels of potassium
ions within the cell (intracellular).
Whereas in outside cells (extracellular), there are high concentrations
of sodium and low concentrations of potassium, so diffusion occurs
through ion channels in the plasma membrane. In order to keep the
appropriate concentrations, the sodium-potassium pump pumps
sodium out and potassium in through active transport.
Mechanism of Sodium-Potassium Pump:

1)After binding with ATP (Adenosine triphosphate), the pump

binds three intracellular Na+ ions and stimulates phosphorylation
by ATP with release of ADP (Adenosine diphosphate).
2)Phosphorylation causes the enzyme (protein) to change its
conformation
3)The phosphorylated form of the pump has a low affinity for Na+
ions, so they are released and pump further binds two extracellular
K+ ions
4)K+ binding triggers (activates) release of a phosphate group
5)Loss of phosphate restores original conformation The
unphosphorylated form of the pump has a higher affinity for Na+
ions than K+ ions, so the two bound K+ ions are released and Na+
sites are receptive again.
ATP binds again and the cycle repeats as shown in the
following fig.
The net result is that hydrolysis of ATP pumps Na+ out and K+
in. The ratio is 3Na+ ions out and two K+ ions in . The overall
equation can be represented by

(Pi = Inorganic phosphate)

Solution:

Both essential and non-essential metal ions can cause toxicity. The essential metal
ions for humans are the bulk metals sodium, potassium, calcium and magnesium
and the trace metals manganese, iron, cobalt, copper, zinc and molybdenum. Let
us try to summarise the circumstances in which certain metal ions can be toxic. A
number of non-essential metals, like cadmium, lead and mercury are not at all
necessary for life but, when introduced into the human environment, they pose
serious problems on account of their toxicity. Essential metal ion toxicity can be
attributed to accumulation of excessive concentrations of the metal ion, often in
specific tissues or organs. The toxicity of non-essential metal ions is a
consequence of environmental exposure leading to their accumulation within the
body, where they interfere with the functions of the essential metal ions. Both
types of metal toxicity can, in principle, be treated by the use of appropriate metal
ion chelators.
Exposure to heavy metals such as mercury, lead, iron, and arsenic
is harmful to the human body and can potentially cause both acute
symptoms (e.g., local irritation, gastroenteritis, and pneumonia) and
long term effects (e.g., abnormal physical development, cancer,
damage to the central nervous system, and kidney). Toxic metals
have many industrial purposes and therefore represent occupational
hazards for a number of professions. Industrial pollution
with heavy metals can affect the wider population through the
contamination of food (e.g., mercury in fish) and water (e.g., lead,
arsenic.
Solution:
1. Magnesium (Mg) is needed by all crops to help capture the sun's
energy for growth and production through photosynthesis.
Photosynthesis takes place in chlorophyll, the green pigment in
plants, and magnesium is the central atom of the chlorophyll
molecule, with each molecule containing 6.7% magnesium.

Magnesium plays an important role in activating enzymes involved

in respiration, photosynthesis and nucleic acid synthesis. It aids in
phosphate metabolism, serving as a carrier of phosphate compounds
through the plant. Magnesium facilitates translocation of
carbohydrates (sugars and starches) and enhances the production of
oils and fats.
2. The choice of Mg(II) in chlorophyll is really unique. In fact
without magnesium the chlorin ring is flourescent (i.e the absorbed
light energy is emitted back immediately). But after incorporation
of Mg(II), chlorophyll becomes phosphorescent. This change due to
metal incorporation i.e fluorescent to phosphorescent is biologically
very important. If the fluorescence occurs exclusively, the absorbed
light energy is lost immediately and will not be available for
chemical transformation in a chemical reaction. Hence the absorbed
light energy must be stored for some while so that it can be utilised
in a chemical reaction for the conversiton of light energy to
chemical energy. For this phosphorescence behaviour, there must
be an excited state of finite life-time. Probably, mixing of the
excited singlet and triplet states through spin orbit coupling of
magnesium gives a relatively stable triplet excited state. In fact ,
triplet to singlet transition is not allowed and it makes the triplet
excited state stable.
3.Stacking of chlorophylls i.e polymerisation in antennae
chlorophyll is attained through the bridging action of Mg(II) ion
between the adjacent chlorophyll molecules.

4.The water molecule coordinated to the Mg(II) centre in the

axial position of chlorophyll of active reaction centre helps the
photoinduced splitting to generate the hydrogen atom that
provides the electron for the photosynthetic process.
Q15.

Solution:
(a). Criteria for an element to be considered as an essential element
are:
i)A physiological deficiency that appears when the element is
removed from the diet
ii)The deficiency is relieved by the addition of that specific
element to the diet .
iii) A specific biological function is associated with the element.
(b)

Element Diseases due to deficiency Diseases due to excess

accumulation

Iron Anemia Hemochromatosis (bronze diabetes),

hemosiderosis, leisons in
gastrointestinal tract, liver damage
Calcium Abnormalities in bone for Cataracts; stones in gall bladder and
example rickets, osteomalacia kidney; calcification of tissues;
and osteoporosis, nerve inhibits the absorption of other
function, muscle contraction, essential metals; hypercalcemia
blood clotting; retarted
growth; hypocalcemia
Iodine Hypothyroidism; goiter Hyperthyrodism
(c).

Figure. General structutre of Chlorophyll

( R = CH3 in chlorophyll a & R = CHO in chlorophyll b)
The basic structure of chlorophyll molecule is a porphyrin
system in which four pyrrole rings are linked together by
methine groups forming a ring system. The centre of the
complex is occupied by a divalent magnesium (Mg2+)
which is bonded to the nitrogen atoms of the four pyrrole
rings. Cyclopentanone ring is fused with one pyrrole ring
and both the acid side chains are esterified .One of side
chain attached to the cyclopentanone ring is a methyl ester
while the other chanin attached is an ester of phytol
(C20H39OH, a tetraisoprenoid alcohol). The presence of this
phytol chain makes chlorophyll highly hydrophobic and
soluble in nonplar meda. The most abundant chlorophyll is
chlorophyll-a which was first synthesised by Woodward in
1960.
The process of photosynthesis involves the following two
steps:
1.Light reactions or light dependent reactions: In
these reactions the energy from the sun is absorbed and
converted in to chemical energy . The chemical energy is
stored in ATP and NADPH( reduced nicotimanide adenine
dinucleotide phosphate)
2.Dark reactions or light independent reactions : In
this stage of the reaction carbohydrates are synthesized
from CO2 using the energy stored in ATP and NADPH
during the light reactions.
Figure 1
Figure 1.
(Pi = inorganic phosphate)
Dark reactions (The Calvin Cycle): After the energy
from the sun is converted and packaged into ATP and
NADPH, the cell has the fuel needed to build food in the
form of carbohydrate molecules. The carbohydrate
molecules made will have a backbone of carbon atoms.
The Calvin cycle is the term used for the reactions of
photosynthesis that use the energy stored by the light-
dependent reactions to form glucose and other
carbohydrate molecules. In plants, carbon dioxide (CO2)
enters the chloroplast through the stomata and diffuses
into the stroma of the chloroplast.
The Calvin cycle reactions (Figure 3) can be organized into three
basic stages: fixation, reduction, and regeneration. In the stroma, in
addition to CO2, two other chemicals are present to initiate the Calvin
cycle: an enzyme abbreviated RuBisCO, and the molecule ribulose-
1,5-bisphosphate (RuBP). RuBP has five atoms of carbon and a
phosphate group on each end.
The enzyme, RuBisCO catalyzes a reaction between CO2 and RuBP
in the stroma, which forms a six-carbon compound that is
immediately converted into two three-carbon compounds in a process
called carbon fixation.
ATP and NADPH use their stored energy to convert the three-carbon
compound, 3-PGA(3-phosphoglyceric acid ) , into another three-
carbon compound called G3P (glyceraldehyde-3-phosphate ). This
type of reaction is called a reduction reaction, because it involves the
gain of electrons. The molecules of ADP and NAD+, resulting from
the reduction reaction, return to the light-dependent reactions to be
re-energized.
Overall, it takes six turns of the Calvin cycle to fix six
carbon atoms from CO2. These six turns require energy
input from 12 ATP molecules and 12 NADPH molecules
in the reduction step and 6 ATP molecules in the
regeneration step.
Figure 3. The Calvin cycle has three stages. In stage 1, the enzyme RuBisCO
incorporates carbon dioxide into an organic molecule. In stage 2, the organic
molecule is reduced. In stage 3, RuBP, the molecule that starts the cycle, is
regenerated so that the cycle can continue.
Q16.
Solution(a).
The cobalt centre in vitamin B12 can exist in +1, +2 or +3
oxidation states depending on the situation. Cobalt exhibits
+3 oxidation states in cyanocobalamin represented as
Vitamin B12 ,aquacobalamin represented as B12a and
hydroxocobalamin represented as B12b. However cobalt
centre can be reduced to +2 represented as B12r which can
be further reduced to Cobalt in +1 oxidation state
represented as B12s.
Vitamin B12 is a collective term for a group of cobalt-
containing compounds known as corrinoids which when
assembled with 5th and 6th position ligands are known as
cobalamins. The cobalt centre lies approximately in the
plane of the corrin ring. Four nitrogen atoms from the
pyrrole rings is coordinated to the central Co(III) ion.
The 5th coordination site of the cobalt centre is occupied
by the nitrogen of the 5,6-dimethylbenzimidazole. The
sixth octahedral position can be occupied either by
(R=CN) as in cyanocobalamin, (R = H2O ) as in
aquacobalamin , (R = OH) as in hydroxycobalamin etc.
Methylation of Vitamin B12:
Methylation or biomethylation is the process of controlled transfer of
a methyl group onto amino acids, proteins, enzymes and DNA.
Methylation process for the synthesis of methionine involves vitamin
B12. Vitamin B12 is involved directly in the transfer of the methyl
group to homocysteine. In turn, methionine and ATP are required in
the synthesis of S-adenosyl methionine (SAM). SAM transfer its
methyl group and is rapidly converted to S-adenosyl homocysteine
(SAH) and subsequently hydrolysed to homocysteine and adenosine.
This hydrolysis is a reversible reaction that favours SAH synthesis.
Fig. Methylation of methionine involving vitamin B12
(b).Carbonic anhydrase is a metalloenzyme containing
Zn2+. This enzyme catalyses the hydration of CO2 and
dehydration of carbonic acid ( HCO 3-) to be more
precise). This enzyme occurs in animals as well as in
plants. The molar mass of this enzyme is about 30,000
and it contains a single protein unit of 260 amino acids
and the active site contains a Zn2+ ion coordinated
tetrahedrally to three histidine imidazole nitrogen atoms
and water molecule or hydroxide ion. This enzyme can
hydrate 106 molecules of carbon dioxide at 37 °C and is
about 107 times faster than the uncatalysed rate of
hydration of CO2 .
The Lewis acidity of Zn2+ ion in carbonic anhydrase
polarizes the coordinated H2O molecule to lose H+ ion to
form Zn-OH-. It is the hydroxy form of the enzyme which
is believed to reversibly hydrate CO2 to HCO 3-. The
nucleophilic OH- bonded to Zn2+ in the enzyme then
attacks on the carbon atom of CO2 to form a transient five
coordinate Zn2+ ion. In which a cabonato oxygen from
HCO3- coordinates to the Zn2+. After rearrangement, the
HCO3- ligand is replaced by H 2O. The deprotonation of
H2O ligand coordinated to Zn2+ ion then regenerate the
species Zn-OH- which then attacks another CO2 and the
catalytic cycle continues. A probable mechanism for the
catalytic cycle (reversible hydration )of CO2 by carbonic
anhydrase is shown below.
Fig. A probable mechanism for the catalytic cycle (reversible hydration ) of CO2
by carbonic anhydrase.
(C).

Be: The most commonly known effect of beryllium is called berylliosis, a

dangerous and persistent lung disorder that can also damage other organs.

Al: Long lasting uptakes of significant

concentrations of aluminum can lead to serious health effects, such as:
- Damage to the central nervous system
- Dementia
- Loss of memory
- Listlessness
- Severe trembling.
- Inhalation of finely divided aluminum and aluminum oxide powder
- has been reported as a cause of pulmonary fibrosis and lung
- damage. This effect, known as Shaver’s Disease, is complicated by
- the presence in the inhaled air of silica and oxides of iron.
- Aluminum may also be considered a Primary Etiological Factor in
- Alzheimer’s Disease
Pb: Lead can cause several unwanted effects, such as:
- Disruption of the biosynthesis of haemoglobin and anaemia
- A rise in blood pressure
- Kidney damage
- Miscarriages and subtle abortions
- Disruption of nervous systems
- Brain damage
- Declined fertility of men through sperm damage
- Diminished learning abilities of children.
-Behavioural disruptions of children, such as aggression, impulsive
behavior and hyperactivit.

Hg: Mercury has a number of effects on humans, and can be

simplified into the following main effects:
- Disruption of the nervous system
- Damage to brain functions
- DNA damage and chromosomal damage
- Allergic reactions, resulting in skin rashes, tiredness and headaches
- Negative reproductive effects, such as sperm damage,
birth defects and miscarriages. Damaged brain functions can cause degradation of
learning abilities, personality changes, tremors, vision changes, deafness, muscle
incoordination and memoryloss. Chromosomal damage is known to cause mongolis
17.
(2022)

Solution:
(a) Refer to solution for question No. 12

(b) Refer to solution for question No. 16(c)

( c). cis- platin(cis- diamminedichloroplatinum(II)) also
known as cis-DDP is a platinum complex that exhibits
anti-cancer activity.
(d). Myoglobin (Mb) is an iron-containing heme protein that is present
predominantly in the muscles. Myoglobin is a monomeric protein, consisting of a
single polypeptide chain with a heme group. This heme group is where oxygen
binds. Structurally, myoglobin is similar to a single subunit of hemoglobin, the
oxygen-carrying protein in blood. Myoglobin's tertiary structure enables it to
bind oxygen more strongly than hemoglobin, which is crucial for its role in
muscle tissue where oxygen concentration is lower than in blood.
Myoglobin's primary role is to serve as an oxygen reservoir within muscle cells.
When muscles are at rest, myoglobin binds to oxygen, storing it for later use.
This stored oxygen can be crucial during periods of increased physical activity
when muscles require an immediate supply of oxygen to support energy
production.
Myoglobin facilitates the transport of oxygen from the bloodstream to the
mitochondria within muscle cells. Mitochondria are the cellular powerhouses
responsible for converting oxygen and nutrients into energy through a process
called oxidative phosphorylation. Myoglobin ensures that the oxygen needed for
this energy production is readily available within muscle fibres.
18. (2022)
Solution:
(a) Refer to solution for question No. 15(a)

(b) Iron is an essential element for blood production. About 70 percent of your
body's iron is found in the red blood cells of your blood called hemoglobin and
in muscle cells called myoglobin. The key function of iron is to facilitate
oxygen transport by haemoglobin, the oxygen-carrying pigment of the
erythrocytes (red blood cells).
The heme group contains an iron (ferrous ion, Fe+2) held in the center of
a porphyrin ring binding with the nitrogen atoms of the ring. The Fe+2 ion is
bound to the pocket of the globin subunit with a histidine residue. Each
Fe+2 ion can bind with one oxygen (O2) molecule or one carbon dioxide (CO2)
molecule. Fe+2 ion of a heme group can bind one O2 molecule; hence, a total of
4 O2 molecules can be carried by one hemoglobin. When O2 is bound with
hemoglobin, it is called oxyhemoglobin and hemoglobin without bound O2 is
called deoxyhemoglobin. About 98% of oxygen in the blood is carried by
oxyhemoglobin.
The catalytic zinc ion in carbonic anhydrase serves as a Lewis acid;
its primary role is to lower the pKa of the Zn-bound water from 10 to
7, allowing the formation of a zinc-bound hydroxide ion at
physiological pH.

For function of carbonic anhydrase as a metalloenzyme Refer to

solution for Question No. 16 (b)
(d)
Deficiency of iron causes Anaemia.
Deficiency of calcium causes rickets, osteomalacia and
osteoporosis.
Deficiency of iodine causes Hypothyroidism, goiter.
19.

(2023)
Solution:
(a) Refer to solution for question No. 2
Iron:
Most abundant metal in biology, used by all plants and animals
including bacteria. It is an important component of may
metalloproteins like hemoglobin, myoglobin, transferrin, ferritin
etc.The two main functions of iron in biological system is (i)
transport of oxygen and (ii) mediation in electron transfer chains.
Zinc:
Major concentration of Zn is found in metallothionein (which
also serves as a reservoir for other metals, e.g. Cd, Cu, Hg)
and in the enzymes like carbonic anhydrase and carboxy
peptidase. Zn is needed for the body's defensive (immune)
system to properly work. It plays a role in cell division, cell
growth, wound healing, and the breakdown of carbohydrates.
Zinc is also needed for the senses of smell and taste.
(b) Heme is a porphyrin ring system made up of four pyrrole rings
with an Fe(II) ion coordinated to nitrogens of pyrrole rings.

Fig. Structure of heme group present in hemoglobin and myoglobin

Hemoglobin and myoglobin are two types of oxygen-binding

proteins in the human body. Both play critical roles in transporting
oxygen and storing oxygen. Myoglobin consists of a single
polypeptide chain and so contains a single heme group. On the
other hand, hemoglobin consists of four polypeptide chains and so
contains four heme groups.
Hemoglobin is an oxygen-carrier protein present in the blood,
specifically in the red blood cells, of humans and other animals. It is
a globular protein that binds to oxygen molecules and transports
them from the lungs to other organs throughout the body. Cells in
the human body need oxygen to produce energy; therefore,
hemoglobin performs a vital function by transporting oxygen.
Hemoglobin also carries carbon dioxide from the cells throughout
the body to the lungs to be expelled.

Myoglobin is a globin protein that stores oxygen. It is present in

muscle cells, including skeletal muscles (which attach to tendons
and bones) and heart muscle tissue. Myoglobin binds oxygen very
efficiently and stores oxygen until muscle tissues need it. Skeletal
muscles and heart muscle cells have a high demand for oxygen due
to their constant use. Therefore, myoglobin is an important muscle
protein that contains stored oxygen.
(c)
Cisplatin exerts anticancer activity via multiple mechanisms but its most
acceptable mechanism involves generation of DNA lesions by interacting with
purine bases on DNA followed by activation of several signal transduction
pathways to form 1,2-intrastand which finally lead to apoptosis (programmed
cell death).
The structure of cis-platin and trans-platin are shown below:

The anti-cancer activity of cis-platin is attributed to the

formation of 1,2-intrastand which finally lead to apoptosis.
Note: Apoptosis is the process of programmed cell death.
However, in case of trans-platin, the distance between the two chlorine atoms is longer
than that in cis-platin resulting in trans-platin being unable to form 1,2-intrastand DNA
adducts similar to cis- platin which from 1,2-intrastand (cis-platin-DNA complxes) and
is believed to shield the DNA from intracellular repair leading to apoptosis.

OR

In cis-platin both of its chlorine atoms are on the same side of platinum and this allows
the formation of a complex compound with guanine base of DNA to stop cell division. In
case of trans-platin only one chlorine atom is there on each side and hence it is more
easily removed from the DNA strand. This is why cisplatin is more effective as an
anticancer drug.
20.
(2023)
Solution:
(a) Refer to solution for question No. 12
(b) Refer to solution for question No. 16
The stereochemistry of active zinc site (Zn2+ ) in carbonic anhydrase
is tetrahedral. The zinc ion is tetrahedrally coordinated to protein by
the imidazole nitrogen atoms of three histidine residues and a water
molecule.
(c )
(i) Anaemia: Iron deficiency
(ii)Hypothyroidism: Iodine deficiency
(iii)Tenany: Calcium deficiency
(iv)Diabetes: Magnesium deficiency
******END*****