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The designs are experimentally validated using various spectroscopic and kinetic techniques including circular dichroism, mass spectrometry, direct electrochemistry, and stopped-flow kinetics along with EPR and NMR techniques. In a Biomimetic approach towards the development of catalysts and sensors we carefully scrutinize coordination geometries of metal ions in metallo-enzymes and metallo-regulatory protein, to design selective ligands for metal ion complexation.
Students in the Bioinorganic program learn a confluence of techniques ranging from bio-engineering and synthesis, to spectroscopy, and develop a fundamental understanding on the crucial role of metal ions in biology. NaKATPase , vacuoles , siderophores , and other proteins and small molecules which control the concentration of metal ions in the cells. One issue is that many metals that are metabolically required are not readily available owing to solubility or scarcity.
Organisms have developed a number of strategies for collecting such elements and transporting them. Many reactions in life sciences involve water and metal ions are often at the catalytic centers active sites for these enzymes, i. Often the reacting water is a ligand see metal aquo complex.
Examples of hydrolase enzymes are carbonic anhydrase , metallo phosphatases , and metalloproteinases. Bioinorganic chemists seek to understand and replicate the function of these metalloproteins.
Markus Galanski. Prev Next Table of Contents. This, of course, led to some resentment 5 in the ranks of those interested in metal proteins with other functions such as transport, as e. Kennedy M. It has played the decisive role in the discovery of Fe-S proteins and the exploration of the electronic structure and other properties of these proteins Things were not as simple with iron, because there a new type of iron protein had to be discovered, the iron-sulfur Fe-S proteins. By the middle of that century, zinc and molybdenum were discovered in enzymes, and non-heme iron was recognized as a necessary component in mitochondrial preparations that are active in substrate oxidation.
Metal-containing electron transfer proteins are also common. They can be organized into three major classes: iron-sulfur proteins such as rubredoxins , ferredoxins , and Rieske proteins , blue copper proteins , and cytochromes. These electron transport proteins are complementary to the non-metal electron transporters nicotinamide adenine dinucleotide NAD and flavin adenine dinucleotide FAD. The nitrogen cycle make extensive use of metals for the redox interconversions.
Several metal ions are toxic to humans and other animals. The bioinorganic chemistry of lead in the context of its toxicity has been reviewed. Aerobic life make extensive use of metals such as iron, copper, and manganese. Heme is utilized by red blood cells in the form of hemoglobin for oxygen transport and is perhaps the most recognized metal system in biology.
Other oxygen transport systems include myoglobin , hemocyanin , and hemerythrin. Oxidases and oxygenases are metal systems found throughout nature that take advantage of oxygen to carry out important reactions such as energy generation in cytochrome c oxidase or small molecule oxidation in cytochrome P oxidases or methane monooxygenase.
Some metalloproteins are designed to protect a biological system from the potentially harmful effects of oxygen and other reactive oxygen-containing molecules such as hydrogen peroxide. These systems include peroxidases , catalases , and superoxide dismutases. A complementary metalloprotein to those that react with oxygen is the oxygen evolving complex present in plants.
This system is part of the complex protein machinery that produces oxygen as plants perform photosynthesis. Bioorganometallic systems feature metal-carbon bonds as structural elements or as intermediates. Bioorganometallic enzymes and proteins include the hydrogenases , FeMoco in nitrogenase, and methylcobalamin. These naturally occurring organometallic compounds.
This area is more focused on the utilization of metals by unicellular organisms. Bioorganometallic compounds are significant in environmental chemistry. A number of drugs contain metals. This theme relies on the study of the design and mechanism of action of metal-containing pharmaceuticals, and compounds that interact with endogenous metal ions in enzyme active sites. The most widely used anti-cancer drug is cisplatin.
MRI contrast agent commonly contain gadolinium. Lithium carbonate has been used to treat the manic phase of bipolar disorder.
Gold antiarthritic drugs, e. Carbon monoxide-releasing molecules are metal complexes have been developed to suppress inflammation by releasing small amounts of carbon monoxide.
The cardiovascular and neuronal importance of nitric oxide has been examined, including the enzyme nitric oxide synthase. See also: nitrogen assimilation. Besides, metallic transition complexes based on triazolopyrimidines have been tested against several parasite strains. Environmental chemistry traditionally emphasizes the interaction of heavy metals with organisms.
Methylmercury has caused major disaster called Minamata disease. Arsenic poisoning is a widespread problem owing largely to arsenic contamination of groundwater , which affects many millions of people in developing countries. The metabolism of mercury- and arsenic-containing compounds involves cobalamin -based enzymes. Research in Bioinorganic and Biomimectic chemistry at TIFR focuses on understanding the fundamental mechanisms underlying the role of metal ion cofactors in enzymes and developing metallo-enzyme inspired chemistry for applications in catalysis and sensing.
Studies in Bioinorganic Chemistry delineate the effects of active site amino acids on the structure, stability, electronic properties, and functions of metal ions in metalloproteins and metalloenzymes. Molecular modeling and docking analyses are used to rationally design novel mutant proteins with new functions of the metal center in a metalloenzyme.