{"id":62,"date":"2020-10-01T22:28:56","date_gmt":"2020-10-02T02:28:56","guid":{"rendered":"https:\/\/sites.bu.edu\/reu-chemistry\/?page_id=62"},"modified":"2022-12-01T09:49:55","modified_gmt":"2022-12-01T14:49:55","slug":"inorganic-bioinorganic","status":"publish","type":"page","link":"https:\/\/sites.bu.edu\/reu-chemistry\/projects\/inorganic-bioinorganic\/","title":{"rendered":""},"content":{"rendered":"<div class=\"bu_collapsible_container \" aria-live=\"polite\" data-customize-animation=\"false\"><h2 class=\"bu_collapsible\" aria-expanded=\"false\"tabindex=\"0\" role=\"button\">Linda Doerrer: Synthesis of Manganese Alkoxide Compounds Relevant to O<sub>2<\/sub> Production in the Water Oxidation Cluster<\/h2><div class=\"bu_collapsible_section\" style=\"display: none;\">\n<ul>\n<li><a href=\"http:\/\/www.bu.edu\/chemistry\/profiles\/linda-helen-doerrer\">Linda Doerrer<\/a><\/li>\n<li style=\"text-align: justify;\">One of the outstanding mysteries in bioinorganic chemistry is the mechanism by which the {Mn<sub>4<\/sub>Ca} water oxidizing complex (WOC) or oxygen evolving complex in photosystem II in plants functions.\u00a0 Photosystem II is part of the photosynthetic process that brings visible light, CO<sub>2<\/sub>, and water together to make carbohydrates and oxygen.\u00a0 It is known that a cluster of four manganese atoms and one calcium atom is critical for this functioning, as well as the participation of a tyrosine residue from the protein environment.\u00a0 The Doerrer Group is synthesizing first-row transition metal complexes with alkoxide anions, and they are interested in extending this chemistry to manganese to mimic WOC.\u00a0 The REU Student will learn how to synthesize transition-metal complexes in the absence of H<sub>2<\/sub>O and O<sub>2<\/sub> and characterize them.\u00a0 Characterization techniques include NMR, UV-Vis, and IR spectroscopy, as well as solid state magnetism and single crystal X-ray diffraction.\u00a0 Successful efforts in the first stages of the project could lead to more advanced work in the project such as reactivity studies.<\/li>\n<li style=\"text-align: center; list-style-type:none;\">\n<p>&nbsp;<\/p>\n<p><a href=\"\/reu-chemistry\/files\/2020\/10\/doerrer-research.png\"><img style=\"width:60%; height: auto;\" src=\"\/reu-chemistry\/files\/2020\/10\/doerrer-research.png\" \/><\/a><\/li>\n<\/ul>\n<p><\/div>\n<\/div>\n<br \/>\n<div class=\"bu_collapsible_container \" aria-live=\"polite\" data-customize-animation=\"false\"><h2 class=\"bu_collapsible\" aria-expanded=\"false\"tabindex=\"0\" role=\"button\">Sean Elliott: Redox enzymology: from enzymatic biosensors to CO<sub>2<\/sub> reduction<\/h2><div class=\"bu_collapsible_section\" style=\"display: none;\"><\/p>\n<ul>\n<li><a href=\"http:\/\/www.bu.edu\/chemistry\/profiles\/sean-j-elliott\">Sean Elliott<\/a><\/li>\n<li style=\"text-align: justify;\">The research of the Elliott Group focuses on the electron transfer reactions found in nature that are mediated by proteins and enzymes. Such proteins include cytochromes <em>c, <\/em>a class of metalloprotein that contains heme iron, and iron-sulfur cluster proteins, where iron and sulfide are assembled into redox-active units. In either type of protein, these inorganic parts serve as molecular &#8220;wiring&#8221; for how a cell moves electronic equivalents, and they serve as enzymatic active sites. . Such enzymes are capable of\u00a0multi-electron transfer reactions, and these types of chemistry incredibly important to the energy sciences. Further, our group specializes in the use of electrochemistry as a tool for assessing how these proteins and enzymes work. \u00a0Projects in our group focus on the structure-function relationship of biological electron transfer in model systems, encompassing many areas of biological chemistry. One example involves the study of ferredoxins, small redox-carriers that are essential for shuttling electrons across key steps of microbial CO<sub>2<\/sub> reduction. An REU student may design mutations of such a ferredoxin, to test how changes in the environment around the ferredoxin iron-sulfur cluster results in changes in redox chemistry. In other areas, our group develops strategies for deposition of enzymes at electrode surfaces, a potentially exploitable technology for biosensor development. In this area, an REU student will develop co-immobilization of multiple enzymes to develop a multi-enzyme cascade that allows for sensing analytes through direct and mediated voltammetry.<\/li>\n<li style=\"text-align: center; list-style-type:none;\">\n<p>&nbsp;<\/p>\n<p><a href=\"\/reu-chemistry\/files\/2020\/10\/elliott-fig.jpg\"><img style=\"width:80%; height: auto;\" src=\"\/reu-chemistry\/files\/2020\/10\/elliott-fig.jpg\" \/><\/a><\/li>\n<\/ul>\n<p><\/div>\n<\/div>\n<\/p>\n","protected":false},"excerpt":{"rendered":"","protected":false},"author":10766,"featured_media":0,"parent":47,"menu_order":1,"comment_status":"closed","ping_status":"closed","template":"","meta":[],"_links":{"self":[{"href":"https:\/\/sites.bu.edu\/reu-chemistry\/wp-json\/wp\/v2\/pages\/62"}],"collection":[{"href":"https:\/\/sites.bu.edu\/reu-chemistry\/wp-json\/wp\/v2\/pages"}],"about":[{"href":"https:\/\/sites.bu.edu\/reu-chemistry\/wp-json\/wp\/v2\/types\/page"}],"author":[{"embeddable":true,"href":"https:\/\/sites.bu.edu\/reu-chemistry\/wp-json\/wp\/v2\/users\/10766"}],"replies":[{"embeddable":true,"href":"https:\/\/sites.bu.edu\/reu-chemistry\/wp-json\/wp\/v2\/comments?post=62"}],"version-history":[{"count":50,"href":"https:\/\/sites.bu.edu\/reu-chemistry\/wp-json\/wp\/v2\/pages\/62\/revisions"}],"predecessor-version":[{"id":567,"href":"https:\/\/sites.bu.edu\/reu-chemistry\/wp-json\/wp\/v2\/pages\/62\/revisions\/567"}],"up":[{"embeddable":true,"href":"https:\/\/sites.bu.edu\/reu-chemistry\/wp-json\/wp\/v2\/pages\/47"}],"wp:attachment":[{"href":"https:\/\/sites.bu.edu\/reu-chemistry\/wp-json\/wp\/v2\/media?parent=62"}],"curies":[{"name":"wp","href":"https:\/\/api.w.org\/{rel}","templated":true}]}}