title: Dioxygen Binding in the Active Site of Histone Demethylase JMJD2A and the Role of the Protein Environment.
abstract: 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.
authors.affiliation: Chemistry Research Laboratory, University of Oxford, 12 Mansfield Road, Oxford, OX1 3TA (UK) paton.chem.ox.ac.uk.|Physical and Theoretical Chemistry Laboratory, South Parks Road, Oxford OX1 3QZ (UK).
authors.forename: Wilian A
authors.initials: WA
authors.lastname: Cortopassi
authors.affiliation: Chemistry Research Laboratory, University of Oxford, 12 Mansfield Road, Oxford, OX1 3TA (UK) paton.chem.ox.ac.uk.|Physical and Theoretical Chemistry Laboratory, South Parks Road, Oxford OX1 3QZ (UK).
authors.forename: Robert
authors.initials: R
authors.lastname: Simion
authors.affiliation: Chemistry Research Laboratory, University of Oxford, 12 Mansfield Road, Oxford, OX1 3TA (UK) paton.chem.ox.ac.uk.|Physical and Theoretical Chemistry Laboratory, South Parks Road, Oxford OX1 3QZ (UK).
authors.forename: Charles E
authors.initials: CE
authors.lastname: Honsby
authors.affiliation: Department of Chemical Engineering, Military Institute of Engineering, 80 Praça General Tibúrcio, Urca, 22290 270, Rio de Janeiro (Brazil).|Center for Basic and Applied Research, Faculty of Informatics and Management, University of Hradec Kralove, Hradec Kralove (Czech Republic).
authors.forename: Tanos C C
authors.initials: TC
authors.lastname: França
authors.affiliation: Chemistry Research Laboratory, University of Oxford, 12 Mansfield Road, Oxford, OX1 3TA (UK) paton.chem.ox.ac.uk. robert.paton@chem.ox.ac.uk.|Physical and Theoretical Chemistry Laboratory, South Parks Road, Oxford OX1 3QZ (UK). robert.paton@chem.ox.ac.uk.
authors.forename: Robert S
authors.initials: RS
authors.lastname: Paton
mesh_terms: D001665:Binding Sites; D056466:Histone Demethylases / Q000737:chemistry* / Q000378:metabolism; D006657:Histones / Q000737:chemistry* / Q000378:metabolism; D056484:Jumonji Domain-Containing Histone Demethylases / Q000737:chemistry* / Q000378:metabolism; D011485:Protein Binding
chemical_list: D006657:Histones; D056466:Histone Demethylases; D056484:Jumonji Domain-Containing Histone Demethylases; C494424:KDM4A protein, human