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Solvent water interactions within the active site of the membrane type I matrix metalloproteinase.

Decaneto, Elena, Vasilevskaya, Tatiana, Kutin, Yuri, Ogata, Hideaki, Grossman, Moran, Sagi, Irit, Havenith, Martina, Lubitz, Wolfgang, Thiel, Walter, Cox, Nicholas·2017·Physical Chemistry Chemical Physics
DOI 10.1039/c7cp05572b
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Abstract

EPR, MCD, crystallographic and QM/MM investigation reveals the role of the 1st solvation shell waters in the catalytic mechanism of MT1-MMP.

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Metadata

Authors
Decaneto, E., Vasilevskaya, T., Kutin, Y., Ogata, H., Grossman, M., Sagi, I., Havenith, M., Lubitz, W., Thiel, W., & Cox, N.
Affiliations
  • Max Planck Institute for Chemical Energy Conversion
  • Max-Planck-Institut für Kohlenforschung
  • Department of Physical Chemistry II
  • Department of Biological Regulation
ORCID
Venue
Physical Chemistry Chemical Physics
Publisher
Royal Society of Chemistry (RSC)
Published
2017
Volume
19
Issue
45
Pages
30316-30331
ISSN
  • 1463-9076
  • 1463-9084
DOI
10.1039/c7cp05572b
Cited by
23
References
0
Language
en
Licence
creativecommons.org/licenses/by/3.0/ (vor, 262 d)
Funders
  • Israel Science Foundation
  • United States-Israel Binational Science Foundation
  • Weizmann Institute of Science (National Postdoctoral Award Program for Advancing)
  • Max-Planck-Gesellschaft
  • H2020 European Research Council (Advanced Grant 695437 THz-Calorimetry)
  • Alexander von Humboldt-Stiftung
  • Australian Research Council (FT140100834)
  • Deutsche Forschungsgemeinschaft (Cluster of Excellence RESOLV (EXC 1069))

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