Bioinorganic Active Sites that Drive Challenging Chemical Conversions

Metalloproteins are remarkable in their ability to use metal active sites in order to effect challenging conversions under ambient conditions. These include the conversion of dinitrogen to ammonia by the Fe/Mo/V-containing cofactors of the nitrogenase family of enzymes, the splitting of water by the Mn/Ca-containing oxygen evolving complex of photosystem II, H2 production by hydrogenases, and the reversible conversion between CO2 and CO by Mo/Fe and Ni/Fe-containing carbon monoxide dehydrogenases – to highlight only a few examples. In addition to the earth abundant transition metals, in more recent years it has also been found that rare earth elements are involved in biological processes, enabling for example methanol oxidation using lanthanide based active sites. Current research in understanding how these inorganic cofactors enable these challenging transformations is enormous and continues to drive efforts in synthetic biology, protein engineering, computational chemistry, and synthetic catalyst design.

The 2022 Gordon Research Conference will highlight recent progress in understanding the fundamental chemistry and underlying mechanism of these remarkable cofactors. The conference will bring together a diverse group of scientists - spanning molecular biology, biochemistry, synthetic inorganic chemistry, spectroscopy, and theoretical chemistry – in order to catalyze cross-disciplinary interactions to push the forefront of metallocofactor research.