Learning objectives
Knowledge and understanding: the course of Bioinorganic Chemistry has the aim of equipping the students with the fundamentals of inorganic chemistry in the biological systems. The course deals with the concepts of coordination chemistry associated to biology, with biocrystallography (including the capacity of describing the structure of metalloproteins and metalloenzymes) and with the role of the chemical elements in biological systems. Particular care will be given to the correct use of technical language of Bioinorganic Chemistry.
Knowledge application: the course equippes the students with the tools to study and understand the role of metals in biological systems. Students are encouraged to read scientific papers is stimulated and the reading comprehension is checked.
Communication skills: the course leads to the acquisition of a technical language that allows the students to communicate with specialists both in the field of chemistry and molecular biology using a formally correct language.
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
D. Rehder. 2014. Bioinorganic Chemistry, Oxford University Press, Oxford, UK
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
D.E. McRee. 1999. Practical Protein Crystallography. Academic Press. San
Diego
Teaching methods
Lectures supported by Power Point slides. Part of the course will be
devoted to the use of Chimera to display protein structures
Assessment methods and criteria
he exam is in two parts:
The oral communication skills are tested through a presentation of an article of bioinorganic chemistry. The other students are invited to pose questions at the end of the presentation. Also this activity is evaluated.
The written part is made up of ten questions divided in 3 sections: the first section regards the concepts of coordination chemistry applied to biological systems (2 questions, 3 points each), the second is about biocrystallography (2 questions, 3 points each ) and the last section concerns the strictly bioinorganic part (6 questions, 3 points each). The exam is passed only if the student has gathered at least 18 points and has obtained for each section at least half of the associated points).
Other information
The reference books are available in the department library. The software (Chimera) 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.
