Blodig, W <br/><br/>
Crystal structures of pristine and oxidatively processed lignin peroxidase expressed in Escherichia coli and of the W171F variant that eliminates the redox active tryptophan 171. Implications for the reaction mechanism.  [electronic resource] 

 -  Journal of molecular biology  Jan 2001 
 - 851-61 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>0022-2836 
<br/><br/><label>Standard No.: </label>10.1006/jmbi.2000.4346  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Amino Acid Substitution--genetics<br/>Benzyl Alcohols--metabolism<br/>Catalysis<br/>Crystallography, X-Ray<br/>Escherichia coli--genetics<br/>Heme--chemistry<br/>Hydrogen Bonding<br/>Hydroxylation<br/>Isoenzymes--chemistry<br/>Models, Molecular<br/>Mutation--genetics<br/>Oxidation-Reduction<br/>Peroxidases--chemistry<br/>Phanerochaete--enzymology<br/>Protein Conformation<br/>Recombinant Proteins--chemistry<br/>Tryptophan--genetics