- Docente: Francesco Capozzi
- Credits: 4
- SSD: CHIM/03
- Language: Italian
- Teaching Mode: Traditional lectures
- Campus: Cesena
- Corso: Second cycle degree programme (LM) in Food Science and Technology (cod. 8531)
Learning outcomes
At the end of the courses the student will get the theoretical
basis for understanding the relationship between the molecular
structure of enzymes and the biochemical reactions catalyzed by
them, particularly regarding the bioinorganic aspects of
metal-enzymes and metallo-proteins. He will be able to acquire
information, including those of spectroscopy nature, necessary to
evaluate the chemical changes in the structure of molecules within
the food.
Course contents
- Primary structure of proteins and chemical-physical properties of their constituting amino acids
- Secondary structure and Ramachandran plot
- Prosthetic groups, apo and holo-protein
- Sequence homology and maintenance of biological function
- Description and use of bioinformatics programs for validation of protein structures (molmol and CLUSTALX)
- NMR parameters and information on the chemical nature of biological systems
- RX crystallography and NMR spectroscopy for the elucidation of the structures
- Metal ions abundance in nature and in biological fluids
- Uptake of metal ions in the cells
- Transferrin, siderophores and Chaperones
- Enterobactin and competitive inhibition of ferric-MECAM
- Principles of chemical kinetics and Arrhenius law
- Michaelis-Menten kinetics and saturation
- Hints on Hard-Soft theory
- Dissociation constants and affinity
- Defining the catalytic site and mechanisms of enzymatic reactions
- Metal ions and effect of coordination on the acidic constant of water
- Role of metal ions in hydrolytic enzymes
- Mechanism of action of carboxy peptidase and carbonic anhydrase
- Conformational flexibility and stability
- Transduction of the chemical signal into mechanical energy: contractile proteins
- Structural differences between hemoglobin and myoglobin and their implications in their different physiological function
- Electronic state of iron ions in the high and low spin
- NMR of myoglobin and adducts with cyanide
- Paramagnetic effect on the chemical shift of NMR signals
- Nuclear relaxation of the water protons: interaction with paramagnetic ions
- Water redox properties: potential for oxygen reduction and of the H+ ion
- Role of the metal ion (Fe or Cu) and optimal coordination geometries in electronic transport
- Role of the geometry of the ligands on E0 of plastocyanin and azzurine
- Redox potential of the proteins and pathways of electron transfer
- Frank-Condon effect and Marcus theory
- Catalytic mechanism of superoxide dismutase
Readings/Bibliography
Scientific papers on authoritative journals
Bioinorganic Chemistry - I. Bertini, H.B. Gray, S.J. Lippard, J.S.
Valentine (Eds.) -University Science Books, Mill Valley, CA,
U.S.A., ISBN: 0935702571
Teaching methods
The
teaching consists of 4
ECTS. Each ECTS includes 6 hours of
lectures and 4
hours of practical work in class. The practical work
is carried out in the Computer Laboratory at the
Campus of Cesena (Villa Almerici) with
20 PC workstations with access to
the network. Students
will follow the operations conducted by the
teacher through the overhead screen projection. The objective of the practical
exercises is twofold:
- Have the
student familiar with the bioinformatic tools for the analysis of structural data
- To develop the
student's ability to independently develop hypotheses on the relationships between
structure and function of biological
molecules
Assessment methods
The examination at the end
of the course aims to assess the achievement
of learning
objectives:
- Using the information
provided in class to develop hypotheses
on the structural characteristics of macromolecules
- Describing,
with properties of language and scientific rigour, the
mechanisms of function for some emblematic enzymes
- Defining the
criteria by which the effects of the
chemical environment on the
function of biological
molecules can be
evaluated
For the examination, the
student could chose between either a
written test or the autonomous preparation of
a report accompanied by a PowerPoint presentation.
1) The written test
consists of answering questions concerning the
course program, through the description
of structural and
spectroscopic data which will be delivered to the
student during the exam. Subsequently, the student who passes the written test argues orally with the teacher the contents of the assignment in order to reach the final evaluation.
2) The report and the PowerPoint
presentation will be prepared at home by the student
on a topic of
her/his choice, among those
listed in the program, and based on the autonomous elaboration of literature data and on
the structural information acquired through the use of
the software taught in class.
Teaching tools
The didactic material projected during classes is made
available to the student in electronic format. To get educational
materials visit the website: http://www.francescocapozzi.it
The freeware softwares "ClustalX" and "MolMol" is available for
downloading from the teacher website.
Audio recordings of the lectures is permitted, provided that they
are made available to all students through the sharing of mp3
files into restricted areas of the above teacher's website.
Username and password are reserved for students enrolled in the
course and is released by the teacher, at the beginning of the
course, directly in class. Otherwise, they will be communicated by
subscribing to the corresponding mail distribution list.
Public databases for proteins are made accessible via
internet.
Office hours
See the website of Francesco Capozzi
SDGs
This teaching activity contributes to the achievement of the Sustainable Development Goals of the UN 2030 Agenda.