Perspectives in biological nitrogen fixation research

Nitrogen fixation, along with photosynthesis is the basis of all life on earth. Current understanding suggests that no plant fixes its own nitrogen. Some plants (mainly legumes) fix nitrogen via symbiotic anaerobic microorganisms (mainly rhizobia). The nature of biological nitrogen fixation is that the dinitrogenase catalyzes the reaction-splitting triple-bond inert atmospheric nitrogen (N(2)) into organic ammonia molecule (NH(3)). All known nitrogenases are found to be prokaryotic, multi-complex and normally oxygen liable. Not surprisingly, the engineering of autonomous nitrogen-fixing plants would be a long-term effort because it requires the assembly of a complex enzyme and provision of anaerobic conditions. However, in the light of evolving protein catalysts, the anaerobic enzyme has almost certainly been replaced in many reactions by the more efficient and irreversible aerobic version that uses O(2). On the other hand, nature has shown numerous examples of evolutionary convergence where an enzyme catalyzing a highly specific, O(2)-requiring reaction has an oxygen-independent counterpart, able to carry out the same reaction under anoxic conditions. In this review, I attempt to take the reader on a simplified journey from conventional nitrogenase complex to a possible simplified version of a yet to be discovered light-utilizing nitrogenase.