Abstract
Publisher Summary This chapter discusses the methods for isolation and characterization of nitrogenase from Klebsiella pneumoniae. Nitrogenase is composed to two oxygen-sensitive proteins, component I (MoFe protein, dinitrogenase) and component II (Fe protein, dinitrogenase reductase). Electrons are transferred from reduced flavodoxin or ferredoxin to the MgATP complex of component II. Component II, in turn, reduces component I with concomitant hydrolysis of Adenosine-5'-triphosphate (ATP). Dinitrogen (and other alternate substrates, such as acetylene, cyanide, and azide) binding and reduction take place on component I. Nitrogenase components I and II, by themselves, have no known enzymatic activity. A major problem in the purification of nitrogenase components is their extreme sensitivity to oxygen. The chapter describes the methods and equipment that are routinely used for excluding oxygen and obtain nitrogenase components of high specific activities.
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