D125 - Bioinorganic chemistry
| Course specification | ||||
|---|---|---|---|---|
| Course title | Bioinorganic chemistry | |||
| Acronym | D125 | |||
| Study programme | ||||
| Module | ||||
| Lecturer (for classes) | ||||
| Lecturer/Associate (for practice) | ||||
| Lecturer/Associate (for OTC) | ||||
| ESPB | 5.0 | Status | ||
| Condition | Облик условљености | |||
| The goal | To gain an understanding of a role of metal ions in biological systems; To learn about the structure and function of several enzymes that activate small molecules; To learn about the goals and methods of chemists that aim to mimic biological systems; To learn about selected organometallic and inorganic complexes that do a good job of mimicking biological catalysis. | |||
| The outcome | Upon successful completion of this course, the student should be able to: ; • Demonstrate proficiency in the basic principles of inorganic chemistry, biochemistry, and molecular biology that are necessary to approach the field of bioinorganic chemistry. ; • Identify the appropriate analytical techniques that are useful in characterizing transition-metal complexes in biological molecules. ; • Describe the different processes involved in the transport and storage of metal ions. ; • Describe the role of metal ions that are involved in electron-transfer reactions in biological systems. ; • Describe the most common metal centers for electron-transfer reactions—those based on copper and iron ions. ; • Summarize the role of metal centers in the enzymes that are involved in the nitrogen cycle. ; • Describe how oxygen is transported through the human body and transferred to each biological entity that requires it; identify which metal centers perform these tasks. ; • Describe the different metal-activation sites in enzymes that are involved in the incorporation of oxygen atoms into bio-organic molecules. | |||
| Contents | ||||
| Contents of lectures | Metals found in biological systems: structure and function; - Review of physical methods as applied to bioinorganic chemistry ; - Proteins as ligands: how the amino acids bind to metals ; - Zinc enzymes: carbonic anhydrase, carboxypeptidase A, phospotriesterase ; - Calcium binding proteins: Calmodulin ; - Hydrogenase and its mimics ; -Oxygen transport and activation: hemocyanin, methane monooxgenase ; - Non heme iron sites in enzymes: ribonucleotide reductase ; - Superoxide Dismutase (including the recently discovered Ni SOD ; - Nitrogenase and its mimics ; - Electron transport proteins: blue copper proteins, cytochrome P450 ; - The role of Co and Ni dependent enzymes in ancient life; Cobalamins: organometallic bonds in enzymes ; - Ni enzymes: Acetyl-CoA Synthase and CO dehydrogenase ; - Student presentations on selected topics ; - Metal containing drugs: cisplatin ; - Metal toxicity: lead and cadmium | |||
| Contents of exercises | ||||
| Literature | ||||
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| Number of hours per week during the semester/trimester/year | ||||
| Lectures | Exercises | OTC | Study and Research | Other classes |
| 2 | ||||
| Methods of teaching | Lectures, seminar, tests | |||
| Knowledge score (maximum points 100) | ||||
| Pre obligations | Points | Final exam | Points | |
| Activites during lectures | 20 | Test paper | ||
| Practical lessons | Oral examination | 50 | ||
| Projects | ||||
| Colloquia | ||||
| Seminars | 30 | |||