Deciphering structural fingerprints for metalloproteins with quantum chemical calculations

Yan Ling, Yong Zhang

Research output: Chapter in Book/Report/Conference proceedingChapterpeer-review

4 Scopus citations

Abstract

Computational investigations of spectroscopic observables can help many experimental studies and provide an important venue for the structural investigations of proteins. Here we report the first detailed quantum chemical investigation of the hydrogen-bonding effect on Mössbauer spectroscopic properties of metalloproteins, using various active site models of oxymyoglobin. The hydrogen bond between O2 and the distal His residue was found to strengthen the binding of oxygen, highlighting the role of protein environment on its biological function. The hydrogen bonding also entails more FeIII- O2-character. These structural effects result in clear differences in the predicted Mössbauer properties, with those of the lowest energy, hydrogen-bonded, Weiss-type, open-shell singlet state, in best agreement with the experiment. These results suggest that the use of quantum chemical calculations of Mössbauer properties can help identify and assess the effect of hydrogen bonding in the protein active site.

Original languageEnglish
Title of host publicationAnnual Reports in Computational Chemistry
Pages64-77
Number of pages14
EditionC
DOIs
StatePublished - 2010

Publication series

NameAnnual Reports in Computational Chemistry
NumberC
Volume6
ISSN (Print)1574-1400

Keywords

  • Hydrogen bonding
  • Mössbauer
  • Oxymyoglobin
  • Quantum chemical calculations

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