TY - CHAP
T1 - Deciphering structural fingerprints for metalloproteins with quantum chemical calculations
AU - Ling, Yan
AU - Zhang, Yong
PY - 2010
Y1 - 2010
N2 - 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.
AB - 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.
KW - Hydrogen bonding
KW - Mössbauer
KW - Oxymyoglobin
KW - Quantum chemical calculations
UR - http://www.scopus.com/inward/record.url?scp=77955757352&partnerID=8YFLogxK
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U2 - 10.1016/S1574-1400(10)06005-6
DO - 10.1016/S1574-1400(10)06005-6
M3 - Chapter
AN - SCOPUS:77955757352
T3 - Annual Reports in Computational Chemistry
SP - 64
EP - 77
BT - Annual Reports in Computational Chemistry
ER -