The effects of removal of manganese ions on the structure of the enzyme chloroperoxidase

سال انتشار: 1395
نوع سند: مقاله کنفرانسی
زبان: انگلیسی
مشاهده: 444

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تاریخ نمایه سازی: 7 اسفند 1396

چکیده مقاله:

Chloroperoxidase (CPO) is the most versatile of the knownheme enzymes [1]. This enzyme has amanganese ions in its structure [2]. We have carried out molecular dynamics (MD) simulation studies onthe removal of manganese(Mn2+) and studied its effect on the CPO. In this study protein secondarystructure, root-mean-square deviation of atomic positions(RMSD), root mean square fluctuation (RMSF)and contact map were studied before and after the removal of manganese and corresponding graphs weredrawn. The study of secondary structure of protein showed that with manganese removal, three of aminoacids were rearranged in 3.1 Helix, and the percent of alpha helix, extended and isolated bridge in theprotein secondary structure are decreased, while the percent of coil and turn are increased. The results ofthe RMSD diagram showed that the presence of manganese does not have a large impact on the on thestability of the tertiary structure of the CPO. The results of the RMSF diagram showed that the removalof manganese very effective on amino acid binding site and C-terminal.


Maryam Ghorbani

Department of Chemistry, Ferdowsi University of Mashhad, International Campus, Mashhad, Iran

Mohammad Reza Housaindokht

Department of Chemistry, Faculty of Sciences, Ferdowsi University of Mashhad, Mashhad, Iran

Mohammad Reza Bozorgmehr

Department of Chemistry, Faculty of Sciences, Mashhad Branch, Islamic Azad University, Mashhad, Iran