Chemolithautotrophs are lifeforms that catabolize inorganic compounds. Among them, nitrifying bacteria and archaea oxidize ammonia in order to generate reducing equivalents. The biochemical pathways and the enzymatic machinery underlying nitrification remain largely uncharacterized, and some enzymes driving key steps remain to be identified. Discovering the enzymes pertinent to these pathways represents not only an investigation into a fundamental mode of energy transduction utilized by life but also an investigation into the chemistry that affords these enzymes the control over challenging reactions. Two metalloproteins have been investigated as candidates in both bacterial and archaeal nitrification pathways: a nonheme diiron protein—a homolog of a previously characterized pathogenic agent in Chlamydia—and a copper protein with a unique coordination sphere—nitrosocyanin. Both candidates were expressed and purified from E. coli. UV-vis, electron paramagnetic resonance, and Mössbauer spectroscopic data are presented as characterization of both candidates. Furthermore, reactivity assays pertinent to nitrification were performed and are also presented.

Identifying missing links in the biogeochemical nitrogen cycle

Macromolecular Chemistry: The Second Century

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ACS Spring 2020 National Meeting & Expo

The official archive and repository for all ACS Meetings & Expositions abstracts and select posters or presentations.