The enzyme nitrogenase is a biological catalyst that can reduce dinitrogen (N2) to ammonia in the presence of a suite of complex metallocofactors. However, the mechanistic details of the reaction remain scarce. In a new report on Science, Wonchull Kang and a research team in chemistry, molecular biology and biochemistry at the University of California-Irvine, U.S., reported a 1.83-angstrom crystal structure for the nitrogenase molybdenum-iron (MoFe) protein, which they captured under physiological dinitrogen turnover conditions. The results of the study can assess the possible mechanisms of N2 reduction and the role of belt-sulfur sites during the process.
Click here for original story, Structural evidence for a dynamic metallocofactor during dinitrogen reduction by Mo-nitrogenase
Source: Phys.org