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Structural Insight into the Prolyl Hydroxylase PHD2: A Molecular Dynamics and DFT Study (Eur. J. Inorg. Chem. 31/2012)
Author(s) -
Wick Christian R.,
Lanig Harald,
Jäger Christof M.,
Burzlaff Nicolai,
Clark Timothy
Publication year - 2012
Publication title -
european journal of inorganic chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.667
H-Index - 136
eISSN - 1099-0682
pISSN - 1434-1948
DOI - 10.1002/ejic.201290098
Subject(s) - chemistry , molecular dynamics , molecular mechanics , carboxylate , stereochemistry , computational chemistry , crystallography
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.