Bioinorganic chemistry is a field that encompasses the intersection between inorganic chemistry and biochemistry. Inorganic molecules, including metal ions and coordination compounds, are necessary for life in many organisms, as they function in the transport of molecules and are a key component of enzymes.Inorganic molecules have also been used in compounds that have successfully treated cancer, pernicious anemia, and Alzheimer disease. Despite the importance of these molecules, transition metals, including cobalt, copper, nickel, molybdenum, and chromium, are found in the human body in only very small amounts. Of the transition metals found in human physiology, iron is the most abundant, adding up to as much as 5 g in the body of a healthy adult. Iron is of significant importance as it allows the transportation of oxygen throughout the body, and is stored within molecules for future use.

1. Title of the presentation:Bio InorganicChemistry
SubCode: 17KE6A
Presented by
Dr.A.Ramya, M.Sc., M.Phil., Ph.D.,
Assistant Professor of Chemistry
EMG Yadava Women’s College
Madurai-14
E.M.G YADAVA WOMEN’S COLLEGE, MADURAI - 625014
( An Autonomous Institution – Affiliated to Madurai Kamaraj University )
Re- accredited (3rd cycle) with Grade A+ & CGPA 3.51 by NAAC

2. Bio Inorganic Chemistry
Bioinorganic chemistry is a field that examines the role of metals in biology.
 Bioinorganic chemistry includes the study of both natural phenomena such as the
behavior of metalloproteins as well as artificially introduced metals, including those
that are non-essential, in medicine and toxicology.
 Many biological processes such as respiration depend upon molecules that fall
within the realm of inorganic chemistry.
 The discipline also includes the study of inorganic models or mimics that imitate
the behaviour of metalloproteins.

3. Evolution of life :Essential Elements
Earth solidified ~ 4 billion years ago 81 stable elements
Elements of the living organism:
1. Elements in large scale: 11 elements H, C, N, O, Na, Mg, P, S, Cl, K, Ca
2. Elements in small scale: 7 elements Mn, Fe, Co, Cu, Zn, I, Mo
3. Elements of a few species: 7 elements B, F, Si, V, Cr, Se, Sn

4. Role of metal Ions in biological system
1.Electron carriers. Fe: cytochrome, iron-sulfur protein. Cu : blue copper protein.
2.Metal storage compound. Fe : ferritin, transferrin. Zn : metallothionein.
3.Oxygen transportation agent. Fe: hemoglobin, myoglobin. Cu: hemocyanin.
4.Photosynthesis. Mg: chlorophyll.
5.Hydrolase. Zn: carboxypeptidase. Mg: aminopeptidase.
6.Oxidoreductase. Fe: oxygenase, hydrogenase. Fe, Mo: nitrogenase.
7.Isomerase. Fe: aconitase. Co: vitamin B12 coenzyme.
8.Cobalt: Unique biological role in cobaltamin (B12 Coenzymes) isomerization reactions

5. Role of metal Ions in biological system
9.Na and K Produces electrical and chemical gradient across a cell membrane.
It plays a very important role in nerve cell membranes.
Transmission of nerve impulses.
Channel = tunnel-like trans membrane protein: Na+-K+ ATPase
K+ inside a cell Na+ outside a cell
Cell surface membranes pump Na+ ions out of cell and K+ in.
10.The divalent cations Zn2+, Ca2+ and Mg2+ prevent cytotoxicity and in vivo antagonize
Cd-induced carcinogenesis.

6. Structure of metallophorphyrin
 The metalloporphyrins include two important categories: the chlorophyll
molecule and the molecules carrying the heme group.
The ability of chlorophyll to absorb light is related to the
conjugated polyene structure of the porphyrin ring.
 Magnesium ions that are coordinated to the nitrogen atoms of the four pyrrole
rings have at least two functions.

7. They provide the necessary structural rigidity and they Increase the
rate of conversion of the singlet-excited state resulting from photon
absorption into the triplet state that enables the transfer of the excitation
energy into the redox chain.
The two main functions of heme iron-containing proteins are the
transport of oxygen and the mediation of electron transfer reactions.
 The heme group is in all cases associated with a protein molecule, as in
hemoglobin, myoglobin, cytochromes, and enzymes such
as catalase and peroxidase.

8. Hemoglubin is are carrier protein for oxygen and CO2.
it a pigmented and globular protein present within the red blood Cell
its help to to carry out oxygen and other gases assistingthe respiratory system.
It buffers the blood pHand maintains it to tolerable limits.
Sources of physiological active catabolites.
Genetic resistance to malaria, etc.
Structure and function of Heamoglobin

9. Structure and function of Myoglobin
Myoglobin is a monomeric protein that has 153 amino acids
It has 8 α helices
Myoglobin= heme group (contains iron) + Globin protein
Have a linear chain of amino acids
It has a globular structure
Function as a reservoir of oxygen as an oxygen carrier
It increases the rate of transport of oxygen within muscle cell.

10. Structure and function of Chlorophyll
Chlorophyll is green pigment found in cyanobacteria and chloroplasts
of algea and plants
Chloroplast is another organelle found only in plant cells
The chloroplast is the structure that allows the plants to go through
Photosynthesis or make it own food and energy