Evidence for interstitial carbon in nitrogenase FeMo cofactor
18.11.2011
Spatzal T, Aksoyoglu M, Zhang L, Andrade SL, Schleicher E, Weber S, Rees DC, Einsle O
Science 2011;334(6058):940.
The enzyme nitrogenase catalyzes the biological fixation of atmospheric dinitrogen into bioavailable ammonium, a necessary prerequisite for organismic growth. Nitrogenase is a complex, two-component metalloenzyme that harbors the largest biological metal cluster known to date, the FeMo-cofactor. After discovering the presence of an interstitial light atom in the FeMo-cofactor a decade ago, the identity of this atom has now been revealed by a combination of atomic-resolution X-ray diffraction analysis and electron resonance spectroscopy. FeMo cofactor contains a central carbon atom, making it a unique metalloorganic compound. The identification of this atom represents a crucial step towards understanding the biosynthesis and functionality of the FeMo cofactor and is expected to pave the way for developing a mechanistic model for the enzyme that can be used to optimize catalysis in industrial nitrogen fixation for the production of plant fertilizers.
