Question

In: Biology

Describe the active (binding) sites of Hb, Hc and Hr.

Describe the active (binding) sites of Hb, Hc and Hr.

Solutions

Expert Solution

Hemoglobin, hemocyanin and hemoerythrin all three serve as oxygen transporter in various animal systems.

While hemoglobin is main oxygen binding molecule in higher vertebrates. Hemocyanin transports oxygen in invertebrates like Arthropods and molluscs. whereas hemoerythrin transports oxygen in several marine invertebrates.

The active site is different in all three.

Hemoglobin (Hb). Hemoglobin is a tetramer. It contains 4 subunit ( 2 alpha and 2 beta in case of human adult). It is found inside red blood cells in most vertebrates.

So,active site contains 4 heme groups as prosthetic group in each monomer. A heme is iron bound with porphyrin (heterocyclic). Porphyrin contains 4 pyrrole rings where i ion remain complexed in the centre of pyrrole rings by binding with N atoms. Iron binds covalently to N of proximal histidine residue (F8) covalently hence strongly. The 6 th position can attach oxygen by forming a covalent coordinate bond. The binding of oxygen shows cooperativity. It means that binding of oxygen to one iron makes oxygen binding at other 3 binding sites easier.

Hemocyanin (Hc)- In case of Hc the molecule which binds to oxygen is Cu. Cu remains as prosthetic group in the active site and forms coordination complex with histidine residues.

The active site therefore is composed of 2 copper (I) cations which form coordination complex with 6 histidine residue's imidazole ring.

Unlike hemoglobin the hemocyanin is not found in any blood cell but remains a part of hemolymph. Oxygenation converts Cu (I) colorless form to Cu (II) blue color form. It also does not show cooperative binding mostly as happens in case of hemoglobin

Hemoerythrin. (Hr)- it is an oligomer protein. Active site contains 2 iron centre. iron centres form coordination complex with 5 histidine residues as well as carboxyl side chain of glutamic amino and aspartic amino acid.

Oxygen transport by hemoerythrin is most unusual in terms of formation of hydroperoxide intermediate while in hemoglobin oxygen forms di oxygen complex.


Related Solutions

What features of the binding site hinder oxygen binding to Hb? What feature of the binding...
What features of the binding site hinder oxygen binding to Hb? What feature of the binding site facilitates oxygen binding to Hb? Explain the Bohr effect using the theory of allosteric modulation of oxygen binding to hemoglobin.
How do Hemogloblin's amino acids dictate the structure & function of the protein? (using binding/active sites,...
How do Hemogloblin's amino acids dictate the structure & function of the protein? (using binding/active sites, polar/non-polar residues & catalytic mechanisms)
Describe how antigen binding sites of BCRs or TCRs are formed, how they are similar and...
Describe how antigen binding sites of BCRs or TCRs are formed, how they are similar and how they differ.
Describe why Histidine is often found in active sites and is involved in the catalytic mechanisms...
Describe why Histidine is often found in active sites and is involved in the catalytic mechanisms of enzymes. What role does it generally play in catalytic mechanisms? Draw an example of a catalytic mechanism that involves Histidine as a critical amino acid residue.
BIOCHEM: How are the three active sites of PDH linked?
BIOCHEM: How are the three active sites of PDH linked?
Explain why BPG, even at higher concentration, does not affect O2 binding to Hb in the...
Explain why BPG, even at higher concentration, does not affect O2 binding to Hb in the lungs?
The Hb O2 binding curve provides an excellent example of the principle that living systems operate...
The Hb O2 binding curve provides an excellent example of the principle that living systems operate on the basis of weak non covalent interactions. Starting with the curve itself, explain how processes involving weak non covalent interactions within the structure of Hb are responsible for the sigmoid O2 binding curve.
biochem question: At the pO2 in ACTIVE muscle tissue, would Mb or Hb be predicted to...
biochem question: At the pO2 in ACTIVE muscle tissue, would Mb or Hb be predicted to have the higher Kd value? Explain, correlating with function of the protein. Would a protein with only tertiary structure ever display cooperative binding?
What is the basic structure of an antibody? What are the antigen‐binding sites? What are the...
What is the basic structure of an antibody? What are the antigen‐binding sites? What are the types of immunoglobins? How do antibody isotypes differ from antibody idiotypes? Describe the functions of each immunoglobins type.
Which of the following best describes the tRNA binding sites of the ribosome? Group of answer...
Which of the following best describes the tRNA binding sites of the ribosome? Group of answer choices A. The P site contains the tRNA molecule covalently bound to the growing chain of amino acids. B. All tRNAs leave the ribosome through the A site. C. Only one of the three sites can be occupied by a tRNA molecule at any given time. D. Each tRNA that associates with the ribosome must first bind in the P site and then moved...
ADVERTISEMENT
ADVERTISEMENT
ADVERTISEMENT