Molybdenum is a chemical element atomic number 42, it does not occur naturally as a free metal but is found only in various oxidation states in minerals. Molybdenum forms a complex with many different biomolecules, including a cofactor for some enzymes. It is an essential component in nitrogenase, a nitrogen-fixing protein found soil bacteria, as well as in other proteins important for sulfur and nitrogen cycles and for chemical reactions of small metabolites (Leimkühler & Iobbi-Nivol, 2015). Life, in general, shares many similarities and characteristics among organisms. These similarities consist of: cell structure, organelles, and macromolecules such as carbohydrates, proteins, lipids, and nucleic acids. Observations between two separate organisms can show the utilization of specific proteins with similar, if not the same, functional conformation, or residue sequence. The use of protein signature sequences can show evolutionary relationships that organisms share. In environments rich in organic matter, molybdenum can be bound and retained by compounds made by plants and microbes. Molybdenum has been found to be complexed by molecules like tannic acid in leaf litter samples and to iron oxides deeper in soil (Leimkühler & Iobbi-Nivol, 2015). In this project, we will compare sulfite dehydrogenase and aldehyde oxidoreductase proteins from bacteria extrapolated from southern Utah. Sulfite dehydrogenase and aldehyde oxidoreductase are two enzymes that use molybdenum cofactors to catalyze chemical reactions. Our goal is to clone, express, and purify SOX protein from soil cyanobacteria. We are interested in studying how molybdenum is retained and used by microbial communities in soil.
