Scientists of the Max Planck Institute for Chemical Energy Conversion recently published a paper on the Spectroscopy of Nitrogenases in the journal Chemical Reviews. The cover accompanying the paper, was selected as front cover for the journal.
Nitrogenase (N2ase) enzymes catalyze the reduction of atmospheric N2 to NH3, an essential process for life on earth and a critical step in the biogeochemical cycle. These enzymes perform this impressive 6e-, 6H+ process not only at ambient temperatures and pressures, but also using protons and biological electron donors rather than H2. This has made N2ases a holy-grail for understanding efficient, green N2 reduction, which is key for the future of fertilizer production and energy storage. While it’s been nearly 60 years since the first of these enzymes was isolated, unraveling the catalytic mechanism of N2ases still remains a subject of intense study.
„Much of what we know regarding their structure and mechanism has come from the use of a wide range of spectroscopic methods. In this review, we ´dig up` the past 50 years of N2ase research to highlight the critical roles different spectroscopic approaches have played in shaping our current understanding of these enzymes and biological N2 fixation“, says author Casey van Stappen, Postdoc in the Department of Inorganic Spectroscopy (S. DeBeer).
Original Publication: van Stappen, C., Decamps, L., Cutsail III, G.E., Björnsson, R., Henthorn, J.T., Birrell, J.A., DeBeer, S., The Spectroscopy of Nitrogenases, Chemical Reviews. https://doi.org/10.1021/acs.chemrev.9b00650