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Molybdenum and Tungsten Oxidoreductase Models (Eur. J. Inorg. Chem. 8/2011)
Author(s) -
Schulzke Carola
Publication year - 2011
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.201190021
Subject(s) - chemistry , rhodobacter , molybdenum , tungsten , metal , protein data bank (rcsb pdb) , crystallography , stereochemistry , inorganic chemistry , biochemistry , organic chemistry , mutant , gene
The cover picture shows the different aspects that contribute to the optimisation of processes catalysed by molybdenum‐ and tungsten‐dependent oxidoreductases, such as active‐site geometry, proteinic and non‐proteinic ligands, temperature and the metal itself. At the centre, the inorganic site of tungsten‐substituted DMSO reductase from Rhodobacter capsulatus is shown (generated with Jmol; PDB‐ID 1E18). Details are presented in the Microreview by C. Schulzke on p. 1189 ff.