CHARACTERIZATION OF MN-OXIDIZING PROTEINS FROM HYPERTHERMOPHILLIC ARCHAEA

Manganese (Mn) oxides are some of the strongest naturally occurring oxides in nature, playing an important role in geochemical cycling, and living systems. Several theories on the role of Mn in microbial systems exist, but there is not enough supporting evidence to provide a strong argument for these theories. Understanding the role of Mn in microbial systems will allow for further investigations into the evolution of early life, defensive mechanisms, and electron transfer systems in microbes. Preliminary sequence data of biofilms and enrichments of biofilms collected from a Mn-depositing hot spring (102ºC) in Yellowstone National Park (YNP), have yielded findings that a novel hyperthermophilic archaea may be responsible for the accumulation of Mn(III/IV) oxides. There are currently no known hyperthermophilic archaea that is capable of oxidizing Mn(II), an investigation into the properties of the Mn oxidizing properties will have wide impacts in study of early life, bioremediation, and industry. A biochemical analysis of the investigation will involve an examination of the genome and mapping of possible gene sequences responsible for Mn oxidation. These sequences will be isolated and expressed, then synthesized as proteins. As a protein originating from hyperthermophilic archaea, it is hypothesized that it will have retained activity in high temperatures and possibly pH outside of physiological conditions. These hypothesis will be tested by running activity assays, in respect to product/intermediate formations. In addition, denaturation conditions will be tested to examine the durability of the protein structure. Characterization of the novel Mn oxidation components of the thermophilic archaea will be impactful in fields of environmental science, bioinorganic chemistry, and industry.