TY - JOUR
T1 - Quantum Refinement Does Not Support Dinuclear Copper Sites in Crystal Structures of Particulate Methane Monooxygenase
AU - Cao, Lili
AU - Caldararu, Octav
AU - Rosenzweig, Amy C.
AU - Ryde, Ulf
N1 - Funding Information:
This investigation has been supported by grants from the Swedish research council project 2014-5540 (U.R.), from
Funding Information:
This investigation has been supported by grants from the Swedish research council project 2014-5540 (U.R.), from COST through Action CM1305 (U.R.), by NIH grant GM118035 (A.C.R.), and by a scholarship to L.C. from the China Scholarship Council. The computations were performed on computer resources provided by the Swedish National Infrastructure for Computing (SNIC) at Lunarc at Lund University and HPC2N at Umeå University.
Funding Information:
COST through Action CM1305 (U.R.), by NIH grant GM118035 (A.C.R.), and by a scholarship to L.C. from the China Scholarship Council. The computations were performed on computer resources provided by the Swedish National Infrastructure for Computing (SNIC) at Lunarc at Lund University and HPC2N at Umeå University.
PY - 2018/1/2
Y1 - 2018/1/2
N2 - Particulate methane monooxygenase (pMMO) is one of the few enzymes that can activate methane. The metal content of this enzyme has been highly controversial, with suggestions of a dinuclear Fe site or mono-, di-, or trinuclear Cu sites. Crystal structures have shown a mono- or dinuclear Cu site, but the resolution was low and the geometry of the dinuclear site unusual. We have employed quantum refinement (crystallographic refinement enhanced with quantum-mechanical calculations) to improve the structure of the active site. We compared a number of different mono- and dinuclear geometries, in some cases enhanced with more protein ligands or one or two water molecules, to determine which structure fits two sets of crystallographic raw data best. In all cases, the best results were obtained with mononuclear Cu sites, occasionally with an extra water molecule. Thus, we conclude that there is no crystallographic support for a dinuclear Cu site in pMMO.
AB - Particulate methane monooxygenase (pMMO) is one of the few enzymes that can activate methane. The metal content of this enzyme has been highly controversial, with suggestions of a dinuclear Fe site or mono-, di-, or trinuclear Cu sites. Crystal structures have shown a mono- or dinuclear Cu site, but the resolution was low and the geometry of the dinuclear site unusual. We have employed quantum refinement (crystallographic refinement enhanced with quantum-mechanical calculations) to improve the structure of the active site. We compared a number of different mono- and dinuclear geometries, in some cases enhanced with more protein ligands or one or two water molecules, to determine which structure fits two sets of crystallographic raw data best. In all cases, the best results were obtained with mononuclear Cu sites, occasionally with an extra water molecule. Thus, we conclude that there is no crystallographic support for a dinuclear Cu site in pMMO.
KW - copper
KW - density functional theory
KW - particulate methane monooxygenase
KW - quantum refinement
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U2 - 10.1002/anie.201708977
DO - 10.1002/anie.201708977
M3 - Article
C2 - 29164769
AN - SCOPUS:85039050887
VL - 57
SP - 162
EP - 166
JO - Angewandte Chemie - International Edition
JF - Angewandte Chemie - International Edition
SN - 1433-7851
IS - 1
ER -