Computational methods are powerful approaches for investigating transition metals in proteins. Herein we present an application of density functional theory to Mn-containing bacterial enzymes. Interaction of ionizing radiation with bacteria induces the production of reactive oxygen species (ROS) including superoxide radicals. Superoxide is well known as a regulator of cell decay and cell death. <i>In vivo</i>, this radical species is dismutated into stable compounds by means of proteins which carry out its dismutation to either molecular oxygen or hydrogen peroxide. In particular, enzymes known as manganese superoxide dismutases (Mn-SODs) are responsible for redox reactions which produce dioxygen and/or hydrogen peroxide. Spin density functional theory (SDFT) allows accurate calculation of structural and spectroscopic properties of metal-containing protein active sites. We have performed structural-functional-energetic SDFT-based characterization of the Mn-containing active sites of Mn-SODs of bacterial species, including their reaction intermediate states, to further elucidate their catalytic mechanisms. In particular, the geometric and electronic structures of reaction intermediates have been investigated which provide insight about the superoxide-neutralizing capabilities of Mn-SODs.<br/>

Structure-function relationships of Mn-containing super oxide dismutases (SOD) studied via quantum mechanical computational methods

253rd National Meeting (2017)

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