{"487661":{"#nid":"487661","#data":{"type":"news","title":"Keeping Tabs on Electron Flow","body":[{"value":"\u003Cp class=\u0022p1\u0022\u003EOne of the most basic processes in nature is the transfer of electrons from one molecule to another. For example, this flow of electrons is essential in the critical biological processes of photosynthesis, respiration, and DNA synthesis. \u0026nbsp;\u003C\/p\u003E\u003Cp class=\u0022p1\u0022\u003EElectron transfer involves the generation of highly reactive intermediates, called radicals.\u0026nbsp; A fundamental question in biological chemistry is how the movement of electrons is controlled and radical-induced damage is prevented.\u003C\/p\u003E\u003Cp class=\u0022p1\u0022\u003EThe lab of Bridgette Barry at the Petit Institute for Bioengineering and Bioscience is helping to provide an answer with their research paper, \u201cA tyrosine-tryptophan dyad and radical-based charge transfer in a ribonucleotide reductase-inspired maquette,\u201d published last month in the journal \u003Cem\u003ENature Communications\u003C\/em\u003E.\u003C\/p\u003E\u003Cp class=\u0022p1\u0022\u003EA large number of different proteins \u2013 especially metalloproteins like ribonucleotide reductase (RNR) \u2013 can mediate a high-energy flow of electrons.\u0026nbsp; Often, the movement of electrons involves hopping between aromatic groups, such as tyrosine and tryptophan.\u0026nbsp; In RNR and other proteins, these aromatic amino acids have complex interactions with each other and with other components of the protein. \u0026nbsp; Often, tyrosine and tryptophan are found in close proximity.\u0026nbsp; Because proteins like RNR are complex, it is difficult to determine the functional role of these tyrosine-tryptophan pairs or \u201cdyads.\u201d\u003C\/p\u003E\u003Cp class=\u0022p1\u0022\u003ETo better understand their role, Barry, a professor in the School of Chemistry and Biochemistry, and her collaborators designed and characterized a peptide model of RNR.\u0026nbsp; This model or maquette contains a tyrosine-tryptophan pair, but has a much simpler structure than RNR.\u0026nbsp; The results showed that an unpaired electron is shared between a tyrosine-based radical and the nearby tryptophan.\u0026nbsp; This transfer of charge between the tyrosine and tryptophan may be critical in directing a flow of electrons and in protecting the protein from damage.\u003C\/p\u003E\u003Cp class=\u0022p1\u0022\u003EUltimately, the lab\u2019s findings could have implications for cancer biology.\u0026nbsp; A hallmark of cancer is rapid cell proliferation. RNR is an iron-dependent enzyme that is essential for DNA synthesis. If you can inhibit the rapid synthesis of DNA, you can prevent cancer cells from proliferation. So, Barry and her team are learning more about RNR and its electron transfer pathway.\u003C\/p\u003E\u003Cp class=\u0022p1\u0022\u003E\u201cWhen we understand the mechanism of a protein, we are better at designing inhibitors and useful drugs,\u201d says Barry, whose co-authors for the \u003Cem\u003ENature Communications\u003C\/em\u003E paper are Cynthia Pagba, Tyler McCaslin, Gianluigi Veglia, Fernando Porcelli, Jiby Yohannan, Zhanjun Guo, and Miranda McDaniel.\u003C\/p\u003E\u003Cp class=\u0022p1\u0022\u003EVeglia is a faculty member at the University of Minnesota, and Porcelli is a faculty member of the University of Tuscia in Italy. The other coauthors are or were students in the School of Chemistry and Biochemistry and two of them \u2013 McDaniel and Yohannan \u2013 contributed to the research as undergraduates.\u003C\/p\u003E\u003Cp class=\u0022p1\u0022\u003E\u003Ca href=\u0022http:\/\/www.nature.com\/ncomms\/2015\/151202\/ncomms10010\/full\/ncomms10010.html\u0022\u003E\u003Cem\u003EBarry Lab Research Paper\u003C\/em\u003E\u003C\/a\u003E\u003C\/p\u003E\u003Cp class=\u0022p1\u0022\u003E\u0026nbsp;\u003C\/p\u003E\u003Cp class=\u0022p1\u0022\u003E\u0026nbsp;\u003C\/p\u003E\u003Cp class=\u0022p1\u0022\u003E\u003Cstrong\u003ECONTACT:\u003C\/strong\u003E\u003C\/p\u003E\u003Cp class=\u0022p1\u0022\u003E\u003Ca href=\u0022http:\/\/hg.gatech.edu\/node\/jerry.grillo@ibb.gatech.edu\u0022\u003EJerry Grillo\u003C\/a\u003E\u003Cbr \/\u003ECommunications Officer II\u003Cbr \/\u003EParker H. Petit Institute for\u003Cbr \/\u003EBioengineering and Bioscience\u003C\/p\u003E","summary":null,"format":"limited_html"}],"field_subtitle":[{"value":"Barry lab publishes latest research in Nature Communications"}],"field_summary":[{"value":"\u003Cp class=\u0022p1\u0022\u003EBarry lab publishes latest research in Nature Communications\u003C\/p\u003E","format":"limited_html"}],"field_summary_sentence":[{"value":"Barry lab publishes latest research in Nature Communications"}],"uid":"28153","created_gmt":"2016-01-19 12:00:23","changed_gmt":"2016-10-08 03:20:27","author":"Jerry Grillo","boilerplate_text":"","field_publication":"","field_article_url":"","dateline":{"date":"2016-01-19T00:00:00-05:00","iso_date":"2016-01-19T00:00:00-05:00","tz":"America\/New_York"},"extras":[],"hg_media":{"487631":{"id":"487631","type":"image","title":"DNA Barry story","body":null,"created":"1453233601","gmt_created":"2016-01-19 20:00:01","changed":"1475895242","gmt_changed":"2016-10-08 02:54:02","alt":"DNA Barry story","file":{"fid":"204356","name":"dna_barry_story.jpg","image_path":"\/sites\/default\/files\/images\/dna_barry_story_0.jpg","image_full_path":"http:\/\/www.tlwarc.hg.gatech.edu\/\/sites\/default\/files\/images\/dna_barry_story_0.jpg","mime":"image\/jpeg","size":1009544,"path_740":"http:\/\/www.tlwarc.hg.gatech.edu\/sites\/default\/files\/styles\/740xx_scale\/public\/images\/dna_barry_story_0.jpg?itok=bBr344NO"}}},"media_ids":["487631"],"groups":[{"id":"1292","name":"Parker H. Petit Institute for Bioengineering and Bioscience (IBB)"}],"categories":[],"keywords":[],"core_research_areas":[{"id":"39441","name":"Bioengineering and Bioscience"}],"news_room_topics":[],"event_categories":[],"invited_audience":[],"affiliations":[],"classification":[],"areas_of_expertise":[],"news_and_recent_appearances":[],"phone":[],"contact":[{"value":"\u003Cp\u003E\u003Ca href=\u0022http:\/\/hg.gatech.edu\/node\/jerry.grillo@ibb.gatech.edu\u0022\u003EJerry Grillo\u003C\/a\u003E\u003Cbr \/\u003ECommunications Officer II\u003Cbr \/\u003EParker H. Petit Institute for\u003Cbr \/\u003EBioengineering and Bioscience\u003C\/p\u003E","format":"limited_html"}],"email":["jerry.grillo@ibb.gatech.edu"],"slides":[],"orientation":[],"userdata":""}}}