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|Title:||Tuning Heme Functionality: The Cases of Cytochrome c Oxidase and Myoglobin Oxidation||Authors:||Daskalakis, Evangelos
Farantos, Stavros C.
Cytochrome c oxidase
|Issue Date:||2012||Publisher:||Springer, Berlin, Heidelberg||Source:||Computational Science and Its Applications – ICCSA 2012, 12th International Conference, Salvador de Bahia, Brazil, June 18-21, 2012, Proceedings, Part I, Pages 304-315||Abstract:||The (Fe-O) moiety of Cytochrome c oxidase ferryl intermediate of the dioxygen activation reaction and the oxy-myoglobin (Mb-O2) structure have been probed by QM/MM (hybrid quantum mechanical/ molecular mechanical) calculations using Density Functional Theory (DFT)/MM to elucidate the effect of the heme propionates and the protein matrix on the chemistry of heme Fe-O moieties. On this line, we have probed the role of His97 in various protonation states of the heme propionate-6 in Mb and compared the results to that of the Cytochrome c oxidase chemistry.||URI:||http://ktisis.cut.ac.cy/handle/10488/10008||ISBN:||Print 978-3-642-31124-6
|Rights:||© 2017 Springer International Publishing AG|
|Appears in Collections:||Κεφάλαια βιβλίων/Book chapters|
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