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Dioxygen Binding in the Active Site of Histone Demethylase JMJD2A and the Role of the Protein Environment
Author(s) -
Cortopassi Wilian A.,
Simion Robert,
Honsby Charles E.,
França Tanos C. C.,
Paton Robert S.
Publication year - 2015
Publication title -
chemistry – a european journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.687
H-Index - 242
eISSN - 1521-3765
pISSN - 0947-6539
DOI - 10.1002/chem.201504536
Subject(s) - demethylase , histone , active site , czech , chemistry , enzyme , action (physics) , binding site , cover (algebra) , biochemistry , stereochemistry , physics , engineering , philosophy , dna , linguistics , mechanical engineering , quantum mechanics
Invited for the cover of this issue is the group of Robert S. Paton at the University of Oxford and his collaborators from Brazil and the Czech Republic. The image depicts histone–enzyme complexation and the chemical interactions inside the active site that define the mode of action. Read the full text of the article at 10.1002/chem.201502983 .