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CHEM F343: Inorganic Chemistry III: Pilani
CHEM F343: Inorganic Chemistry III: Pilani
CHEM F343: Inorganic Chemistry III: Pilani
Pilani Campus
1/24/2019
BITSPilani, Pilani Campus
Bioinorganic Chemistry
Structure similarity of Hb and Mb
1/24/2019
BITSPilani, Pilani Campus
Hemerythrin
O2 Fe(III) results in a peak at 844 cm-1 indicating
peroxide type binding
Blue
1/24/2019
BITSPilani, Pilani Campus
Enzymes: 6 types
• Oxidoreductase: Oxidation/ reduction
• Transferase: Transfers the group from one compound to
another
•Hydrolase: hydrolysis
• Isomerase: converts substrate into it’s isomeric form
• Lyase: non hydrolytic addition or removal of group
• Ligase: Synthesis of a large molecules from two smaller ones
Zn—OH2 Zn—OH- + H+ pKa = 8.8
Mg—OH2 Mg—OH- + H+ pKa = 11.4
Carboxypeptidase A
• Catalyzes the hydrolysis of C-terminal amino acid of any
polypeptide and prefers for substrate with aromatic side
chain
• Active site possesses hydrophobic pocket to recognize
such side chain
• Bovine Carboxypeptidase A has been extensively
explored
1/24/2019 BITSPilani, Pilani Campus
Carboxypeptidase A
• Zn(II)---Zn(II) = 4 Å
• One Mg (II) ion is
located at 5-7 Å away
from both the Zn(II)
ion
• Zn(II) ions are bound
with His and Asp
• One Zn(II) is close to
Ser-OH, which acts as
nucleophile to attack
the phosphate ester
• TBP geometry about
Zn(II)
Dimer of 94 kDa
1/24/2019 BITSPilani, Pilani Campus
Alkaline Phosphatase
• Optimum activity at pH 8
• One Zn(II) is closely
associated with Ser while
other is with water
• Water coordinated Zn(II)
stabilizes the -ve charge
developed on alkoxide group
produced
• The pKa of aquated
Zn(II) is 8.8, which yields
R-OH and displaces the
phosphoryl group from the
phosphoserin intermediate
1/24/2019 BITSPilani, Pilani Campus
Alkaline Phosphatase
• K3 is the
slowest step
• ROH is rapidly
produced
• Burst kinetics:
Due to an initial
high velocity of
enzymatic
turnover when
adding enzyme
to substrate.
1/24/2019
BITSPilani, Pilani Campus