Intrinsic dinitrogen activation at bare metal atoms.
There is ongoing interest in metal complexes which bind dinitrogen and facilitate either its reduction or oxidation under mild conditions. In nature, the enzyme nitrogenase catalyzes this process, and dinitrogen fixation occurs under mild and ambient conditions at a metal-sulfur cluster in the center of the MoFe protein, but the mechanism of this process remains largely unknown. In the last few years, new important discoveries have been made in this field. In this review are discussed recent findings on the interaction of N(2) with metal atoms and metal-atom dimers from all groups of the periodic table as provided by gas-phase as well as matrix-isolation experiments. Intrinsic dinitrogen activation at such bare metal atoms is then related to corresponding processes at complexes, clusters, and surfaces.
Himmel
Hans-Jörg
HJ
Anorganisch-Chemisches Institut, Ruprecht-Karls-Universität Heidelberg, Im Neuenheimer Feld 270, 69120 Heidelberg, Germany. hans-jorg.himmel@aci.uni-heidelberg.de
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Markus
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