Acta Phys. -Chim. Sin. ›› 2007, Vol. 23 ›› Issue (09): 1332-1336.doi: 10.1016/S1872-1508(07)60068-0

• ARTICLE • Previous Articles     Next Articles

Dynamic Simulations of the Hydrogen-bondings on the Proximal Side of the Heme in Terms of ABEEM/MM Method

YANG Zhong-Zhi; CUI Bao-Qiu   

  1. College of Chemistry and Chemical Engineering, Liaoning Normal University, Dalian 116029, Liaoning Province, P. R. China; Department of Chemistry, Jinzhou Teacher College, Jinzhou 121000, Liaoning Province, P. R. China
  • Received:2007-04-24 Revised:2007-05-22 Published:2007-09-06
  • Contact: YANG Zhong-Zhi

Abstract: The structures of spermwhale myoglobin (Mb) and mutants were investigated in terms of the ABEEM/MM method. The molecular dynamic simulations showed that the bifurcated hydrogen-bondings in the proximal side of the heme in Mb were not stable. These simulations indicated that hydrogen-bondings could not determine the overall orientation of imidazole, which could be related to the histidine residue. The amide acids and the bulk of the imidazole can have effects on the flexibility of proximal ligands.

Key words: ABEEM/MMmethod, Dynamic simulation, Heme, Ligated imidazole, Hydrogen-bonding


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