Work

Structural Insight into the Prolyl Hydroxylase PHD2: A Molecular Dynamics and DFT Study (Eur. J. Inorg. Chem. 31/2012)

Year: 2012

Type: article

Abstract: The cover picture shows the active site of the iron(II)- and 2-oxoglutarate-dependent dioxygenase prolyl hydroxylase domain containing protein (PHD2). The central iron(II) atom is complexed to the 2-His-1-carboxylate facial triad of PHD2 and 2-oxoglutarate. A combination of molecular dynamics simulations, DFT and quantum mechanics/molecular mechanics geometry optimisations reveals the importance of the protein environment in stabilising this complex and the influence of the ligands on the overall conformational behaviour of the protein. Details are discussed in the article by N. Burzlaff, T. Clark et al. on p. 4973 ff.

Source: European Journal of Inorganic Chemistry

DOI: 10.1002/ejic.201290098

Authors: Christian R. Wick, Harald Lanig, Christof M. Jäger, Nicolai Burzlaff, Timothy Clark

Institutions: Friedrich-Alexander-Universität Erlangen-Nürnberg, University of Portsmouth

Language: English

Topic: Metal-Catalyzed Oxygenation Mechanisms

Subfield: Inorganic Chemistry

Field: Chemistry

Domain: Physical Sciences

Open Access status: bronze

OpenAlex ID: W2027914279

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