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Caption: MIT chemists have determined the structure of the complex that forms when gaseous dinitrogen, or N2, binds to an iron-sulfur cluster, offering clues as to how microbes (in yellow) use nitrogenases to break the nitrogen-nitrogen bond (in pink and green). *Terms of Use: Images for download on the MIT News office website are made available to non-commercial entities, press and the general public under a Creative Commons Attribution Non-Commercial No Derivatives license. You may not alter the images provided, other than to crop them to s...

 E-Mail In a number of biological processes, iron-sulfur clusters play a vital role, where they act as cofactors to enzymes. Research published in Angewandte Chemie now shows that cubic clusters can support unusual bonding states. This study shows that the cluster copes well with a multiple bond between iron and nitrogen--a structural motif that may be involved in biological nitrogen fixation. Clusters made of iron and sulfur atoms are essential cofactors for a number of enzymes, especially in biological processes involving electron transfer. As an example, nitrogen-fixing bacteria use iron...