The fixation of molecular oxygen into organic compounds is one of the key steps in the biodegradative side of the carbon and oxygen cycle in nature in that it initiates the aerobic degradation of many compounds. This process recycles carbon and is mediated by microbial enzymes called oxygenases. Many aromatic hydrocarbons / such as benzene and naphthalene / are priority pollutants in the environment and their remediation is mediated by such microbial enzymes. In addition, these enzymes have turned out to be very useful in producing high value compounds that are of potential value in the pharmaceutical and chemical industry. Such chemicals are extremely difficult to make chemically. This because the enzyme, unlike cruder chemical reactions, can accurately add chemical groups, in the case of di-oxygenases hydroxyl groups, to produce chiral molecules / that is either one of a pair of compounds that are mirror images on each other but are not identical. The current understanding is that microbial dioxygenases / that incorporate two oxygen atoms into aromatic compounds / employ an electron transfer process from cellular cofactors through a complex of proteins. Recent work here has indicated that we have discovered a very novel and potentially more efficient electron transfer system in soil bacteria called rhodococci. We intend to study the mechanism involved in this process in detail. Exploitation of this oxygenase system in these bacteria has significant implications for the efficient production of new chiral compounds.