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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred

12 Issues per year


IMPACT FACTOR 2017: 3.022

CiteScore 2017: 2.81

SCImago Journal Rank (SJR) 2017: 1.562
Source Normalized Impact per Paper (SNIP) 2017: 0.705

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1437-4315
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Volume 388, Issue 1

Issues

Metal-binding sites at the active site of restriction endonuclease BamHI can conform to a one-ion mechanism

Letif Mones
  • Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, H-1113 Budapest, Hungary
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ István Simon
  • Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, H-1113 Budapest, Hungary
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
/ Monika Fuxreiter
  • Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, H-1113 Budapest, Hungary
  • Other articles by this author:
  • De Gruyter OnlineGoogle Scholar
Published Online: 2007-01-10 | DOI: https://doi.org/10.1515/BC.2007.009

Abstract

The number of metal ions required for phosphoryl transfer in restriction endonucleases is still an unresolved question in molecular biology. The two Ca2+ and Mn2+ ions observed in the pre- and post-reactive complexes of BamHI conform to the classical two-metal ion choreography. We probed the Mg2+ cofactor positions at the active site of BamHI by molecular dynamics simulations with one and two metal ions present and identified several catalytically relevant sites. These can mark the pathway of a single ion during catalysis, suggesting its critical role, while a regulatory function is proposed for a possible second ion.

Keywords: metal ion cofactors; phosphoryl transfer; restriction endonucleases; two-metal ion mechanism

About the article

Corresponding author


Received: June 8, 2006

Accepted: August 30, 2006

Published Online: 2007-01-10

Published in Print: 2007-01-01


Citation Information: Biological Chemistry, Volume 388, Issue 1, Pages 73–78, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2007.009.

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