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SAMBA (J&K) (NAAC Accredited B)

Recognized by J&K Govt. and Affiliated to the University of Jammu

Name: Ajay Kumar Class: B.Sc.-III Sec: Medical Roll No: 3

DISCUSSION

METALLOPORPHYRINS
HEMOGLOBIN MYOGLOBIN

STRUCTURE OF PORPHIN LIGAND


Porphines are macrocyclic tetradentate ligands made up of 4 pyrrole rings (C4H4NH) linked together through methene bridges(-CH=). This tetradentate ligand has a conjugated double bonded system with 4 nitrogen donor sites. 2 of the 4 Nitrogen are tertiary Nitrogen while the remaining 2 Nitrogen are secondary. The tert. Nitrogens donate pair of electrons form Coordinate bond()

Porphin Ligand

The Sec. Nitrogens loses proton and forms Covalent bond.

STRUCTURE OF HEMOGLOBIN

Occurs in the protein complex Hemoglobin

Schematic view of Oxygenated Heme in Hemoglobin

STRUCTURE OF MYOGLOBIN

An outline of the Structure of Myoglobin. The tubular structure represents the Polypeptide.

HEMOGLOBIN AND MYOGLOBIN


Basic Function: Hemoglobin and Myoglobin, carry and bind O2.. Hb is found in the blood and Mb is found in muscle tissue. They both metalloproteins, containing iron at the center of a heme group.

Hb can bind 4 molecules of O2 and Mb can bind only 1 molecule of O2.


Mb has much higher oxygen affinity at the low pO2(partial pressure of O2).

HEMOGLOBIN AND MYOGLOBIN


Basic Function:
Hb is pH-sensitive while Mb is not.
Hemoglobin picks up O2 in the lungs and transports it to the rest of the body. Myoglobin accepts O2 from the hemoglobin in the muscles and stores it until needed for energetic process. Deoxygenated hemoglobin uses some of its amino acids to fix up CO2 and then transport CO2 back to the lungs.

ROLE OF HEMOGLOBIN AND MYOGLOBIN

Ph Scale for Blood

Molecular Shift at the Heme Group after Oxygen Binding


Blue: deoxy Red: oxy

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