BIOINORGANIC CHEMISTRY
cod. 1005297

Academic year 2012/13
1° year of course - Second semester
Professor
Academic discipline
Chimica generale e inorganica (CHIM/03)
Field
Discipline chimiche inorganiche e chimico-fisiche
Type of training activity
Characterising
48 hours
of face-to-face activities
6 credits
hub: PARMA
course unit
in - - -

Learning objectives

This course has the purpose to provide the students with the knowledge
that will allow them to read critically papers concerning bioinorganic
issues and to join with little difficulties research groups dealing with
bioinorganic chemistry.

Prerequisites

Basic knowledge of coordination chemistry and biochemistry

Course unit content

The cycles of the main elements involved in the functioning of living
organisms – Summary of the main metalloenzymes and metalloproteins
studied in the course – Proteins and nucleic acids from a structural
perspective – Protein crystallography: preparing crystals, preliminary
characterization, reciprocal lattice, data collection, solution of the phase
problem, refinement and structure - Protein data bank and use of
RASMOL to display proteins - Roles of metalloproteins in cells: choice,
uptake and assembly of metal containing units in biology – Control and
use of of ion concentration in the cell - Influence of metals in folding and
cross linking in biomolecules – Interactions between metal ions and
complexes in biomolecules – Electron transport proteins _ Nonredox
activation mechanisms and interactions with substrates – Atom and atom
groups transfer chemistry – Tuning of metal properties by proteins to
obtain specific functions Metal protein analysis according to the metal:
Iron, Copper, Molybdenum, Cobalt, Zinc and other metals. Metals in
medicine.

Full programme

Development of Bioinorganic Chemistry

Thermodynamic and kinetic concenpts and models of coordination chemistry used in bioinorganic chemistry

Protein crystallography: preparations of the crystals, preliminary analysis, reciprocal lattice, data collection, phase problem, refinement and structure, Protein Data bank

Roles of metalloproteins in cells: choice, uptake and assembly of metal containing units in Biology

Control and use of metal ion concentrations in cells

Influence of metals on folding and cross linking of biomolecules

Interactions between metal ions and complexes in the active sites of biomolecules

Electron transport proteins

Non redox mechanisms of activation and interactions with substrates

Transfer chemistry of atoms and atom groups. Metals in Medicine.

Bibliography

H. B. Gray, E. I. Stiefel, J. S. Valentine, I. Bertini. Biological Inorganic
Chemistry: Structure and Reactivity . University Science Book. Mill Valley,
California
S J Lippard, J M Berg. 1994. Principles of Bioinorganic Chemistry.
University Science Books Mill Valley, California
R. M. Roat-Malone. 2002. Bioinorganic Chemistry: A Short Course. John
Wiley & Sons, New Jersey, USA.
W Kaim, B Schwederski. 1995. Bioinorganic Chemistry. John Wiley &
Sons, New York

Teaching methods

Lectures supported by Power Point slides. Part of the course will be
devoted to the use of RasTop to display protein structures

Assessment methods and criteria

Written test

Other information

The reference books are available in the department library. The software (Rastop 2.2) used for the visualization of proteins and also the Protein Data Bank files are free and can be downloaded from the internet.

The teaching material used during the lectures is also downloadable from the course website.