synthetic models for enzymes

1. Department Of Chemistry
Dr B R Ambedkar
National Institute Of Technology
Jalandhar,Punjab (144011)
AMAN KUMAR
Roll No.-19311103
M.Sc Chemistry(4th Sem)
Submitted to:
Dr Vimal Kumar Bhardwaj
Water-Soluble Polymer-Bound Biomimetic Analogues of Cytochrome c Oxidase
Catalyze 4e- Reduction of O2 to Water

2. This Talk Consist
• Introduction
• Cytochrome C Oxidase
• Biomimetic Chemistry
• Biomimetic of Enzymes
• O2 Reduction
• Coclusion

3. Introduction
• Enzymes are biological catalysts that speed up the rate of the
biochemical reaction.These act as Catalyst to accelerates a reaction.
• Enzymes are specific for what they catalyze.
• Most enzymes are three dimensional globular proteins.
• The Synthetic enzyme is an artificial, organic molecule that recreate
some function of an enzyme.
• These enzymes have shown faster reaction rate in comparison with
natural enzymes.These are designed to achieve some desirable features
of enzymes.

4. Cytochrome C Oxidase (COX)
• The complex is a large integral membrane
protein composed of several metal prosthetic
sites and protein subunits in mammals.
• It is the last enzyme in the respiratory
electron transport chain of cells located in
the membrane. It receives an electron from
each of four cytochrome c molecules, and
transfers them to one dioxygen molecule,
converting the molecular oxygen to two
molecules of water

5. Biomimetic Chemistry
• Biomimetic Chemistry is defined as ‘‘a method of scientific
enquiry that involves mimicking the laws of nature to
create new synthetic compounds’’.
• Biomimetic Compound: A compound that mimics a
biological material in its structure or function.
• Biomimetic process: A laboratory procedure designed to
imitate a natural chemical process

6. Biomimetic of Enzymes

7. Structures of the Porphyrin Monomers and Their
Copolymers

8. • The synthesis of three artificial copolymerized CcO
models (Scheme 1) and their catalytic O2 reduction
behavior is discussed in following slides

9. O2 Reduction
• O2 reduction catalyzed by biomimetic
CcO analogues in polymers in an air-
saturated aqueous pH ) 49 buffer
containing 0.1 M KNO3 as the
supporting electrolyte.10 Electrode
rotation rate: 200 revolutions per
minute; collection efficiency: 15%.
Note the different scales for the disk
and ring currents

10. Conclusion
• Here we have shown that polymeric matrixes can be used to tune
predictably catalytic properties of biomimetic Fe porphyrins toward
reduction of O2 by affecting the microenvironment around the catalytic
sites.
• This approach usefu in preparation of more faithful analogues of the
heme/Cu site for further biomimetic studies.