Inorganic chemistry B.Sc III Bioinorganic chemistry

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<ul><li> Slide 1 </li> <li> Inorganic chemistry B.Sc III Bioinorganic chemistry </li> <li> Slide 2 </li> <li> Bulk Elements: O, C, H, N, Ca, S, P, Na, K, Cl, Mg, etc. Trace Elements: Mo, Mn, Fe, Co, Cu, Zn, I, Si, etc. Ultra-trace Elements: V, Cr, Se, Br, Sn, F, etc. Inorganic Elements in Biological Systems </li> <li> Slide 3 </li> <li> Porphyrins and Related Complexes in Bioinorganic Molecules A porphine ring has a square planar geometry with a pocket in the center. A metalloporphyrin complex can result by incorporating a metal atom into the pocket (look at heme from Rasmol). Axial sites are available for other ligands. Structure, specificity, and reactivity are changed by differing the side chains, metal ions, and surrounding species. </li> <li> Slide 4 </li> <li> Porphyrins </li> <li> Slide 5 </li> <li> Metalloporphyrin complex Heme B group of hemoglobin. An iron (Fe) atom in the middle is shown in red, complexed to four interior nitrogen atoms shown in blue. </li> <li> Slide 6 </li> <li> Hemoglobin and Myoglobin Oxygen transfer and storage agents in the blood and muscle tissue. Hemoglobin transports oxygen (O 2 ) from the lungs/gills to tissues and muscles. Myoglobin stores oxygen (O 2 ) in the muscles and tissues. Oxygen commonly transfers from the hemoglobin to the myoglobin for later use. </li> <li> Slide 7 </li> <li> Hemoglobin (I) Made up of four globin protein subunits ( and ). Each protein partially encloses a heme group. Each heme group is in a porphyrin pocket. One axial position of the iron is bound to an imidazole nitrogen from the protein. One axial position is available/vacant or has H 2 O bound to it. Dissolved O 2 can bind reversibly to this axial position. http://www.umass.edu/microbio/chime/hemoglob/ </li> <li> Slide 8 </li> <li> Hemoglobin (II) In hemoglobin, the Fe(II) does not become oxidized to Fe(III) or Fe(IV). Occurs readily in simpler systems (see Figure on the next page). There needs to be reversible binding of the O 2 without oxidation. A free heme also oxidizes in an aqueous environment. Why doesnt oxidation occur in hemoglobin by O 2 or H 2 O? </li> <li> Slide 9 </li> <li> Hemoglobin (Figures) </li> <li> Slide 10 </li> <li> Hemoglobin (III) In nonoxygenated hemoglobin, the Fe(II) is about 70 pm out of the plane of the porphyrin nitrogens (show with Chime). Bonding O 2 or CO in the sixth position causes the iron to be come planar. Fe(II) becomes diamagnetic Oxygen bonds at an angle of ~130 degrees (show with Chime). Explain these structural changes upon bonding. </li> <li> Slide 11 </li> <li> Hemoglobin (IV) There is a considerable amount of backbonding from the metal to the O 2. Can be described as Fe(III)-O 2 - Why is the O 2 bent? The energy changes very little with this angle. suggestions </li> <li> Slide 12 </li> <li> Hemoglobin (V) Cooperativity The function of hemoglobin is to bind O 2 at high oxygen pressure and carry it through the blood to needed areas (and myoglobin for storage). Hb + 4O 2 Hb(O 2 ) 4 Hb(O 2 ) 4 + 4Mb 4Mb(O 2 ) + Hb As one iron binds an oxygen molecule in Hb, the molecular shape changes to make binding of additional oxygen molecules easier. In a similar fashion, initial removal of oxygen triggers the release of the remaining oxygens. </li> <li> Slide 13 </li> <li> Hemoglobin At low partial pressures of O 2, Mb has a much greater affinity for O 2. The Bohr effect. Increased acidity favors the release of O 2 from Hb(O 2 ) 4 </li> <li> Slide 14 </li> <li> Sodium is important in the body, as it helps maintain body fluid homeostasis. People with disorders that do not have enough sodium in the body can take medication such as serum sodium in order to maintain a healthy amount of sodium in the body. Sodium is also crucial in osmotic pressure, as the body adjusts to when there is too little or too much sodium in the body. Sodium is also the main cation in outside cells containing fluid in mammalian bodies, and very little sodium inside the cells, consisting of approximately 90% of the body's total sodium content. Biological Role of Sodium </li> <li> Slide 15 </li> <li> Magnesium and calcium are ubiquitous and essential to all known living organisms. They are involved in more than one role, with, for example, Mg/Ca ion pumps playing a role in some cellular processes, magnesium functioning as the active center in some enzymes, and calcium salts taking a structural roleion pumpsenzymes Biological Role of Magnesium and calcium </li> <li> Slide 16 </li> <li> Nitrogen Fixation The growth of all organisms depend on the availability of Nitrogen (e.g. amino acids) Nitrogen in the form of Dinitrogen (N 2 ) makes up 80% of the air we breathe but is essentially inert due to the triple bond (N N) In order for nitrogen to be used for growth it must be "fixed" (combined) in the form of ammonium (NH 4 ) or nitrate (NO 3 ) ions. </li> <li> Slide 17 </li> <li> Nitrogen Fixation The nitrogen molecule (N 2 ) is quite inert. To break it apart so that its atoms can combine with other atoms requires the input of substantial amounts of energy. Three processes are responsible for most of the nitrogen fixation in the biosphere: atmospheric fixation biological fixation industrial fixation </li> <li> Slide 18 </li> <li> Biological Fixation cont. Biological nitrogen fixation requires a complex set of enzymes and a huge expenditure of ATP. Although the first stable product of the process is ammonia, this is quickly incorporated into protein and other organic nitrogen compounds. Scientist estimate that biological fixation globally adds approximately 140 million metric tons of nitrogen to ecosystems every year. </li> <li> Slide 19 </li> <li> Some nitrogen fixing organisms Free living aerobic bacteria Azotobacter Beijerinckia Klebsiella Cyanobacteria (lichens) Free living anaerobic bacteria Clostridium Desulfovibrio Purple sulphur bacteria Purple non-sulphur bacteria Green sulphur bacteria Free living associative bacteria Azospirillum Symbionts Rhizobium (legumes) Frankia (alden trees) </li> <li> Slide 20 </li> <li> Some nitrogen fixing organisms </li> <li> Slide 21 </li> <li> Nitrogen Fixation All nitrogen fixing bacteria use highly conserved enzyme complex called Nitrogenase Nitrogenase is composed of of two subunits: an iron-sulfur protein and a molybdenum-iron-sulfur protein Aerobic organisms face special challenges to nitrogen fixation because nitrogenase is inactivated when oxygen reacts with the iron component of the proteins </li> <li> Slide 22 </li> <li> Nitrogenase FeMo Cofactor N 2 + 8H + 2NH 3 + H 2 8e-8e- 4C 2 H 2 + 8H + 4C 2 H 2 Dinitrogenase reductase Fd(red) Fd(ox) nMgATP nMgADP + nP i N 2 + 8H + + 8e - + 16 MgATP 2NH 3 + H 2 + 16MgADP </li> <li> Slide 23 </li> <li> Nitrogenase </li> <li> Slide 24 </li> <li> Types of Biological Nitrogen Fixation Free-living (asymbiotic) Cyanobacteria Azotobacter Associative RhizosphereAzospirillum Lichenscyanobacteria Leaf nodules Symbiotic Legume-rhizobia Actinorhizal-Frankia </li> </ul>