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Bio Inorganic 1 PPT Chemistry
Bio Inorganic 1 PPT Chemistry
By
Dr. Harekrishna Bar
Sabang Sajanikanta Mahavidyalaya
Elements in the living systems
❖Essential elements
The elements which have specific essential
role to sustain life.
Elements:
Na K Mg Ca V CrMn
Fe Co Ni Cu Zn Mo Cd
Elements in the living systems
❖Beneficial elements
The elements that are not required by all
plants but can promote plants growth; and
may be essential for a perticular taxa.
Elements:
Li CrNi Sn V W
Elements in the living systems
❖ Trace elements
The elements that are present in trace amount ranging from 10-1
to 10-4 gm/molein 75 kg adult human body.
Elements:
Mo Mn Fe Co Cu Zn I
❖ Ultra-trace elements
The elements that are present in trace amount ranging lower
than 10-4 gm/mole in 75 kg adult human body.
Elements:
Li Cr Si Sn V W Br Se
Recommended daily dose for ~70 kg
adult human body
Elements Intake (per day)
Fe 10 mg (Male)
18 mg (Female)
Zn 15 mg
Mn 2.5-5 mg
Cu 2-3 mg
F 1.5-4 mg
Mo 150-500 µg
I 150 µg
Cr 50-200 µg
Se 50-200 µg
Function Deficiency
Major constituent of bone Ca: Rickets, steomalacia,
and teeth. Osteoporosis
Blood coagulation
Function
Constitutional element as prosthetic
group in chlorophyll.
Activator of enzyme which utilize ATP Deficiency
Control muscle contraction, acts as co Mg: Convulsion &
factor
neuromuacular irritation,
Intracelluler Mg2+ keeps ribosomes
intact ; stabilizing DNA and RNA
Tremors and spasm
structure
Role of metals in biological systems
Function
O2 transport/storage protein
Hb, Mb, Hemoerythrin
Iron storage protein
Ferritin
e transfer protein Deficiency
Ferredoxins, cytochrome Fe: Anemia
Enzyme
Cytocrome c oxidase,
catalase, peroxidase, aconitase,
nitrogenase
Function
Enzyme
Carbonic anhydrases,
carboxyl peptidases, alkaline Deficiency
phosphatage Zn: Dwarfism,
Enzyme activator hypogonadism
Enolage, Peptidase, arginase,
histidine deaminases
Role of metals in biological systems
Function
Deficiency
Vitamin B12 co-enzymes
Co: Pernicious Anemia
Required in enzyme as glutamate
mutase, ribonucleotide reductase
Function
Enzyme Deficiency
Nitrogenases, hydrogenase, Mo: Plant growth
Nitrate reductase, xanthine disorder
oxidase, sulphite oxidase
Function Deficiency
O2 transport/storage protein Cu: Anemia, Menke’s
Hemocyanin disease, demineralization
Cu storage protein of boanes, decolouration
Ceruloplasm of skin & boan
Enzyme
Cytocrome c oxidase,
Ascorbic acid oxidase
Role of metals in biological systems
Function
Plant growth factor Deficiency
O2 transport in some lower form V: increase blood fat
of life; hemovanadins and colesterol level
Function Deficiency
Glucose tolerence factor Cr: Suspected to
cause Diabetes
Function
Deficiency
Enzyme
Ni: whole leaf chlorosis
Urease, methanogenic bacteria
along with necrotic leaf
factor F430
tips (accumulation of
toxic levels of urea)
Function
Metalloenzyme Deficiency
Pyruvate kinase, pyruvate carboxylase Mn: impaired ,reproductive
Enzyme activator function, skeletal
Phosphoenol pyruvate, photosynthetic abnormalities, impaired glucos
system tolerance
Toxic elements
⚫ Most common toxic elements are
Arsenic(As)
Lead(Pb),
Mercury(Hg),
Cadmium(Cd)
Copper (Cu)
Beryllium (Be)
Manganese (Mn)
Selenium (Se)
Tin(Sn)
Antimony (Sb)
⚫ They are mainly produced by industrial activities, and deposit slowly in the
surrounding water and soil
Effect of toxic elements
Toxic effects of As
⚫ Birth defects
⚫ Carcinogen:
Lung cancer results from the inhalation of arsenic
and probably also from its ingestion. Skin and liver
cancer, and perhaps cancers of the bladder and
kidneys, arise from ingested arsenic
⚫ Gastrointestinal damage
⚫ Severe vomiting
⚫ Diarrhea
⚫ Death
Toxic effects of Hg
βPleated
βsheet
Prosthetic
groups
Porphyrins with
different metals at its
centre are a common
prosthetic group in
bioinorganic chemistry
Coenzyme B12
Cytochrome C
Chlorophyll
Hemocyanin Myoglobin
Protoporphyrin IX and Heme
Present in
Vertebrates
Present in
molluscs
Present in some
sea worms
Hemoglobin Hb
Four units of Hb
3 major types of Hb
Hb A (Adult)
Hb F ( Fetal)
Hb is tetramaric protein
Hb S (Sickle cell) M.W = 64500 Dalton
α Chain = 141 amino acid
β Chain = 146 amino acid
Hb is not an exact
tetramer of Mb
Mw = 17000 Daltons
Active Sites of Hemoglobin & Myoglobin
Protein chain
hydrophobically
shield
Non polar
Reversible
Active Sites of Hemoglobin & Myoglobin
OH2
Irreversible
Hematin
Non polar Readily binds with
O2,CO etc polar Cl-, CN-, S2- etc
•Rupture of other
peptide chain
•Hb tetramer
Relaxed
+ O2 •exposed for O2
0.8A°
Co-operative Interaction
•Rupture of other
peptide chain
•Hb tetramer
Relaxed
•exposed 4 Fe (II)
for O2
K1
Hb + O2 HbO2
K2
HbO2 + O2 (HbO2)2
Hb(O2)2 + O2 K3 (HbO2)3
Mb has no Co-operative interaction Hb(O2)3 + O2 K4 (HbO2)4
K4 (Hb) ~ K (Mb) K1 < K2 < K3< K4
Trigger Mechanism
Co-operative
Interaction
+ O2
Blood O2
O2 O2
O2 O2
O2 Hb carry O2 O2
O2
In muscle
Hb(O2)4 + 4Mb 4 Mb(O2) + Hb
Mb + O2 Mb(O2)
Hb + nO2 Hb4(O2)n
f = fraction of Hb bearing O2
pO2 = equilibrium partial pressure of O2
n = Hill exponent
Mb
Total transport
Hb + O2 = Hb(O2)4 Acidic condition
Acidic Hb(O2)4 = Hb + O2
Hb carry O2
At high O2 pressure + Mb
produce H2CO3,
High O2 affinity of Hb
ng s w ith CO 2 pH independe
Hb release CO2 CO2, lactic acid
se b ac k to lu
er
Acidic condition etc. Hb rev
Mb(O2)
CO2 transported to lungs
Store for
respiration
Hemocyanin (Hc)
metaquohemerythrin
The uptake of O2 by hemerythrin is accompanied by two-electron oxidation of
the di ferrous centre to produce a hydroperoxide (OOH−) complex.
Thank you