Cleaving the N,N triple bond: The transformation of dinitrogen to ammonia by nitrogenases

Abstract

Biological nitrogen fixation is a natural process that converts atmospheric nitrogen (N2) to bioavailable ammonia (NH3). This reaction not only plays a key role in supplying bio-accessible nitrogen to all life forms on Earth, but also embodies the powerful chemistry of cleaving the inert N,N triple bond under ambient conditions. The group of enzymes that carry out this reaction are called nitrogenases and typically consist of two redox active protein components, each containing metal cluster(s) that are crucial for catalysis. In the past decade, a number of crystal structures, including several at high resolutions, have been solved. However, the catalytic mechanism of nitrogenase, namely, how the N,N triple bond is cleaved by this enzyme under ambient conditions, has remained elusive. Nevertheless, recent biochemical and spectroscopic studies have led to a better understanding of the potential intermediates of N2 reduction by the molybdenum (Mo)-nitrogenase. In addition, it has been demonstrated that carbon monoxide (CO), which was thought to be an inhibitor of N2 reduction, could also be reduced by the vanadium (V)-nitrogenase to small alkanes and alkenes. This chapter will begin with an introduction to biological nitrogen fixation and Mo-nitrogenase, continue with a discussion of the catalytic mechanism of N2 reduction by Mo-nitrogenase, and conclude with a survey of the current knowledge of N2- and CO-reduction by V-nitrogenase and how V-nitrogenase compares to its Mo-counterpart in these catalytic activities.