Davydov, Dmitri R <br/><br/>
An electrostatically driven conformational transition is involved in the mechanisms of substrate binding and cooperativity in cytochrome P450eryF.  [electronic resource] 

 -  Biochemistry  Jun 2004 
 - 6475-85 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S. 
<br/><br/><label>ISSN: </label>0006-2960 
<br/><br/><label>Standard No.: </label>10.1021/bi036260l  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Allosteric Site<br/>Amino Acid Substitution<br/>Bacterial Proteins<br/>Binding Sites<br/>Cysteine--chemistry<br/>Cytochrome P-450 Enzyme System--chemistry<br/>Fluorescence Resonance Energy Transfer<br/>Glutamic Acid--chemistry<br/>Heme<br/>Mixed Function Oxygenases--chemistry<br/>Osmolar Concentration<br/>Protein Conformation<br/>Protein Structure, Secondary<br/>Pyrenes--chemistry<br/>Static Electricity