Dioxygen Binding in the Active Site of Histone Demethylase JMJD2A and the Role of the Protein Environment

Wilian A Cortopassi; Robert Simion; Charles E Honsby; Tanos C C França; Robert S Paton

doi:10.1002/chem.201504536

Dioxygen Binding in the Active Site of Histone Demethylase JMJD2A and the Role of the Protein Environment

Chemistry. 2015 Dec 21;21(52):18869. doi: 10.1002/chem.201504536. Epub 2015 Dec 10.

Authors

Wilian A Cortopassi^{1

2}, Robert Simion^{1

2}, Charles E Honsby^{1

2}, Tanos C C França^{3

4}, Robert S Paton^{5

6}

Affiliations

¹ Chemistry Research Laboratory, University of Oxford, 12 Mansfield Road, Oxford, OX1 3TA (UK) paton.chem.ox.ac.uk.
² Physical and Theoretical Chemistry Laboratory, South Parks Road, Oxford OX1 3QZ (UK).
³ Department of Chemical Engineering, Military Institute of Engineering, 80 Praça General Tibúrcio, Urca, 22290 270, Rio de Janeiro (Brazil).
⁴ Center for Basic and Applied Research, Faculty of Informatics and Management, University of Hradec Kralove, Hradec Kralove (Czech Republic).
⁵ Chemistry Research Laboratory, University of Oxford, 12 Mansfield Road, Oxford, OX1 3TA (UK) paton.chem.ox.ac.uk. [email protected].
⁶ Physical and Theoretical Chemistry Laboratory, South Parks Road, Oxford OX1 3QZ (UK). [email protected].

PMID: 26663343
DOI: 10.1002/chem.201504536

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.

MeSH terms

Binding Sites
Histone Demethylases / chemistry*
Histone Demethylases / metabolism
Histones / chemistry*
Histones / metabolism
Jumonji Domain-Containing Histone Demethylases / chemistry*
Jumonji Domain-Containing Histone Demethylases / metabolism
Protein Binding

Substances

Histones
Histone Demethylases
Jumonji Domain-Containing Histone Demethylases
KDM4A protein, human