Bioinorganic Chemistry MCQ Quiz in తెలుగు - Objective Question with Answer for Bioinorganic Chemistry - ముఫ్త్ [PDF] డౌన్‌లోడ్ కరెన్

Explanation:

Metallobiomolecules is a generic term for a molecules that contains a metal ion cofactor.

→ Transferrin 

The molecule has a beta alpha structure of similar topology to human lactoferrin and is composed of two homologous lobes that each bind a single ferric ion. Each lobe is further divided into two dissimilar domains, and the iron-binding site is located within the interdomain cleft.

→ Siderophores 

It usually form a stable, hexadentate, octahedral complex preferentially with Fe³⁺ compared to other naturally occurring abundant metal ions, although if there are fewer than six donor atoms water can also coordinate.

→ Hydrogenases 

It catalyze the reversible conversion of molecular hydrogen to protons and electrons via a heterolytic splitting mechanism. The active sites of [NiFe] hydrogenases comprise a dinuclear Ni-Fe center carrying CO and CN^- ligands.

→ Hydroxylases

They are enzymes which add an hydroxyl group to organic compounds. This addition is the first step of aerobic oxidative degradation.

Secondary structure of Human phenylalanine hydroxylase catalytic domain. Fe⁺³ ion coordination site in Human phenylalanine hydroxylase catalytic domain 

→ Hameerythrin

The conformation of the hemerythrin subunit designated the hemerythrin fold, has four nearly parallel α-helical segments surrounding the pair of non-heme iron atoms, the oxygen binding site. These iron atoms are linked to the protein through specific histidine and tyrosine side chains

Conclusion: All the structures contains metal as co factor, so the correct answer is option 4.

Concept:

→ The main difference between oxyhemoglobin and deoxyhemoglobin is that the oxyhemoglobin is the form of haemoglobin loosely combined with oxygen whereas the deoxyhemoglobin is the form of hemoglobin that has released its bound oxygen. Furthermore, the oxyhemoglobin is bright red in color while the deoxyhemoglobin is purplish in color. 

→Oxyhemoglobin is the oxygen-bound form of hemoglobin. During respiration in the lungs, the hemoglobin component of the red blood cells is exposed to oxygen and loosely bound to it. The binding of oxygen into hemoglobin occurs at high pH, low carbon dioxide, and high-temperature conditions of the blood, which generally occurs inside the lungs. With the binding of the first oxygen molecule to the iron (II), the heme pulls the iron (II) into the porphyrin ring. This slight conformational shift encourages the binding of another three oxygen molecules to the hemoglobin. Ultimately, oxyhemoglobin contains four bound oxygen molecules in its fully saturated form. Therefore, oxyhemoglobin is considered to be in the relaxed (R) state of hemoglobin.  

→Deoxyhemoglobin is the hemoglobin that has released oxygen. The release of oxygen occurs at the metabolizing tissue due to the low pH, high carbon dioxide concentration, and low temperature. Deoxyhemoglobin is the tensed (T) state of hemoglobin due to the release of oxygen molecules.  

Explanation:

In ferrous hemoglobin and myoglobin, coordination numbers of five and six are associated with the high-spin (as in deoxy-hemoglobin) and low-spin (as in oxy-hemoglobin) states respectively.

In deoxyhemoglobin, the heme iron atom is in its high-spin paramagnetic form.

In oxyhemoglobin, the heme iron atom is in its low-spin diamagnetic form because oxygen molecules are bound to iron.

Conclusion: The correct answer is option 1.

Explanation:

Hemoglobin is responsible for the red color of blood. Hemes are the basic unit for building hemoglobin. Hemes have the capability of binding oxygen and iron molecules.

In oxyhaemoglobin, Fe²⁺=[Ar]3d⁶

The blood cells are red because of the binding of oxygen and iron molecules. When oxygen and Fe bind together they exchange their orbitals bond and energy. During binding, the Fe molecule changes its oxygen state from +2 to +3 and shows π – π* Interligand transition.

Interligand π – π* transition refers to an electronic transition that occurs between two adjacent ligands in a complex molecule. In such a transition, an electron from a π orbital of one ligand is excited to an empty π* orbital of another ligand.

The absorption spectrum of oxyhemoglobin shows a peak at around 415 nm, which corresponds to the Soret band, due to the π-π* transition of the porphyrin ring of the heme group. The Soret band is responsible for the blue-green color of oxyhemoglobin.

This type of transition is commonly observed in coordination complexes containing conjugated ligands, such as aromatic compounds. The transition is usually initiated by absorption of light, which excites the electrons from the π orbital of the donor ligand to the π* orbital of the acceptor ligand.

The sharp high energy transition between t_2g​ and e_g​ levels of the d-electrons is responsible for the bright red colour of oxyhaemoglobin.

Conclusion: The correct answer is option 3.

Concept:-

The structure of the oxymyoglobin complex is shown below:

Iron is in Fe⁺³ oxidation state, has \(t_2g^{5}\:eg^{0}\) configuration and one unpaired electron (n=1).

Explanation:-

[Fe(ox)3]3−

Fe³⁺(\(t_{2g}^{3}\:e_g^{2}\))=d⁵ high spin octahedral,

No. of unpaired electrons=5

[Fe(CN)6]3−      

Fe³⁺ \((t_{2g}^{5}\:e_g^{0})\) = d⁵ low spin octahedral 

No. of unpaired electrons=1

[NiCl4]2−     

Ni²⁺ \((e_{g}^{4}\:t_{2g}^{4})\)= d⁸ tetrahedral complex, \(eg^{4}\:t_2g^{4}\)

No. of unpaired electrons=2

[Cu(NH3)4]2+

Cu²⁺=d⁹ low spin, square planner

No. of unpaired electrons=1

• In case of complex(es) [Fe(CN)6]3− and [Cu(NH3)4]2+ has one unpaired electron. 
• That is exactly the same as the number of unpaired electron(s) present in the iron center in oxymyoglobin.

Conclusion:-

Therefore B and D is the correct one.

Concept:

• Carboxypeptidase A usually refers to the pancreatic exopeptidase that hydrolyzes peptide bonds of the C-terminal residues. This enzyme is referred to as CPA1.
• The oxygen-evolving complex (OEC), a water-splitting complex, is the portion of photosystem II where photo-oxidation of water occurs during the light reactions of photosynthesis at chlorophyll.
• Hemerythrin is a non-heme protein responsible for oxygen transport in the marine invertebrate.

Explanation:

• The metalloprotein Carboxypeptidase A or CPA1 contains a zinc (Zn²⁺) metal center in a tetrahedral geometry with amino acid residues in close proximity around the zinc metal ion to facilitate catalysis and binding. Thus, A - IV.
• The metalloprotein core of the oxygen-evolving complex (OEC) contains both manganese (Mn) and calcium ion. Thus, B - I.
• The metalloprotein hemerythrin involves Fe in the +2 oxidation state. The uptake of O₂ by hemerythrin involves the two-electron oxidation of the diferrous center to produce a hydroperoxide (OOH−) complex. Thus, C - II.
• The metalloprotein coenzyme F-430 is a nickel protein. Thus, D - III. 

Conclusion:

• Hence, the correct answer is A - IV, B - I, C - II, and D - III.

Concept:

Hemocyanin:

• From the name, it may suggest that Hemocyanin contains heme and cyanide, but it contains neither.
• The metal atom present in Hemocyanin is Copper and the meaning of Hemocyanin is 'Blue Blood'.
• Hemocyanin is a copper-containing protein that carries oxygen in some invertebrates such as snails, squids, etc.
• The deoxy form of hemocyanin contains Cu in a +1 oxidation state and is colourless.
• The oxy form of hemocyanin contains Cu in +2 form and is bridged to oxygen via an O22--Cu2+ LMCT.

Explanation:

• Hemocyanin molecule has several subunits and binds oxygen cooperatively. 
• The active sites contain two Cu (I) ions 360pm apart for binding of one dioxygen cooperatively.
• Each Cu(I) ion is bound by three histidine residues.
• The dioxygen molecule oxidizes each Cu(I) ion to Cu(II) ion and itself is reduced to the peroxide ion O₂^2-. 
• The peroxide ion bridges two Cu²⁺ ions in theμ−η2:η2−O2−" id="MathJax-Element-8-Frame" role="presentation" style="position: relative;" tabindex="0">μ−η2:η2−O−2μ−η2:η2−O2− $\mu-\eta^2:\eta^2-O_2^-$ mode. The resonance Raman spectroscopy reveals the formulation of Cu-O-O-Cu linkage.
• The 'O-O' stretching frequency in Raman is 745-750 cm^-1, which suggests that the peroxide is not in a free state.
• The UV stretching frequency is about 350-580nm, for the LMCT occurring in oxyhemocyanin imparting it a blue colour.
• The two Cu(II) ions are coupled antiferromagnetically with the μ-O₂^2- ion being involved in a superexchange mechanism.
• As the ions are coupled, there is no magnetic moment observed. The molecule is hence diamagnetic.
• Hemocyanin is colourless in deoxygenated state and blue in an oxygenated state.
• The two states are represented below:

• From the diagram above it is clear that the coordination number of hemocyanin is 5 in oxygenated form.
• Hence, in oxyhemocyanin, the coordination number, mode of oxygen binding, colour and the net magnetic behaviour of copper ions, respectively are five, \(\mu-\eta^2:\eta^2-O_2^-\) blue and diamagnetic.

Concept:

Role of Iron in Photosynthesis

• Iron plays a critical role in the electron transport chain during photosynthesis.
• It is a component of key proteins such as ferredoxin and cytochromes, which transfer electrons within the chloroplasts.
• Iron is essential for the synthesis of chlorophyll and for maintaining the overall efficiency of photosynthetic processes.

Explanation:

• Light absorption: Light absorption is primarily facilitated by chlorophyll pigments, not by iron, making this option incorrect.
• Electron transport: Iron is a crucial component of electron carriers like ferredoxin and cytochromes, enabling the transfer of electrons during the light-dependent reactions of photosynthesis. This makes the correct option.
• Carbon dioxide fixation: Carbon dioxide fixation occurs in the Calvin cycle, facilitated by the enzyme RuBisCO, and does not directly involve iron.
• Oxygen release: Oxygen release results from the splitting of water (photolysis) catalyzed by the oxygen-evolving complex, which does not directly depend on iron.

Therefore, the correct option is 2.

Concept:

Carbonic Anhydrase and Its Catalytic Mechanism

• Carbonic anhydrase is a zinc-containing metalloenzyme that catalyzes the reversible hydration of carbon dioxide (CO₂) to bicarbonate (HCO₃^-).
• The zinc ion in the active site is coordinated by three histidine residues and a water molecule. This arrangement polarizes the water molecule, facilitating its deprotonation to form a hydroxide ion (OH^-).

Explanation:

CO₂ acts as an electrophile and H₂O as a nucleophile which attacks CO₂. Hence, electrophilic addition takes place.

Therefore, the correct option is 1.

Concepts:

• Cytochrome Oxidase:
  • Cytochrome oxidase is the terminal enzyme in the electron transport chain, catalyzing the reduction of molecular oxygen to water.
  • It has the highest reduction potential among the cytochromes, enabling it to act as the final electron acceptor.
• Cytochrome c:
  • Cytochrome c is a small, heme-containing protein that transfers electrons between cytochrome b_c1 complex and cytochrome oxidase.
  • It has a moderate reduction potential, higher than cytochrome b but lower than cytochrome oxidase.
• Cytochrome b:
  • Cytochrome b is a component of the cytochrome b_c1 complex in the electron transport chain.
  • It has the lowest reduction potential among the cytochromes, enabling it to donate electrons to downstream components.

Explanation:

1. Reduction potential refers to the ability of a molecule to accept electrons; higher reduction potential means a stronger tendency to gain electrons.
2. In the electron transport chain, the reduction potential increases progressively from cytochrome b to cytochrome c and finally to cytochrome oxidase.
   • ​​
3. The correct order is: cytochrome c oxidase > cytochrome c > cytochrome b.

Conclusion:

The correct answer is Option 3, as the reduction potential increases in the order cytochrome c oxidase > cytochrome c > cytochrome b.

Concepts:

• Haemoglobin Structure: Haemoglobin is a complex protein containing an iron-bound heme group, critical for binding and transporting oxygen in the blood. The protein chain helps maintain the iron in the Fe²⁺ state, preventing uncontrolled reactions.
• Free Heme Reactivity: Without the stabilizing influence of the protein chain, free heme tends to react in an uncontrolled manner. The iron in the heme can undergo oxidation, resulting in different iron-oxygen complexes.
• Iron-Oxidation States: The iron in heme can exist in multiple oxidation states, primarily Fe²⁺ and Fe³⁺. The reactivity in the absence of the protein chain leads to specific iron-oxygen structures.

Explanation:

1. In the absence of the protein chain, the iron in the heme group can become oxidized from Fe²⁺ to Fe³⁺. This oxidation leads to the formation of a specific type of complex.
2. The absence of protein chain in haemoglobin leads the free haem to react in uncontrolled manner to form hematin which is an μ-oxo dimer Fe³⁺-O-Fe³⁺
3. This oxidation product is generated because Fe³⁺ is more stable under these conditions in the absence of the protein's protective environment.

Conclusion: 

The correct answer is Option 2: Fe³⁺-O-Fe³⁺, as it correctly represents the uncontrolled reaction product formed in the absence of the protein chain in haemoglobin.