Miller, R W <br/><br/>
Transition state complexes of the Klebsiella pneumoniae nitrogenase proteins. Spectroscopic properties of aluminium fluoride-stabilized and beryllium fluoride-stabilized MgADP complexes reveal conformational differences of the Fe protein.  [electronic resource] 

 -  European journal of biochemistry  Feb 2001 
 - 809-18 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>0014-2956 
<br/><br/><label>Standard No.: </label>10.1046/j.1432-1327.2001.01941.x  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Adenosine Diphosphate--metabolism<br/>Adenosine Triphosphate--metabolism<br/>Aluminum Compounds--pharmacology<br/>Beryllium--chemistry<br/>Binding Sites<br/>Catalysis<br/>Electron Transport<br/>Fluorides--chemistry<br/>Iron--chemistry<br/>Klebsiella pneumoniae--enzymology<br/>Magnetic Resonance Spectroscopy<br/>Models, Chemical<br/>Nitrogenase--chemistry<br/>Protein Binding<br/>Protein Conformation<br/>Spectrophotometry<br/>Time Factors<br/>Ultraviolet Rays