Within the background of biological nitrogen fixation mediated by the enzyme nitrogenase, transition-metal complexes capable of binding and activating dinitrogen towards protonation and reduction have been synthesised. Of particular interest in this research area has been the transition-metal mediated conversion of dinitrogen to ammonia (stoichiometric and catalytic) and the elucidation of the corresponding mechanistic pathways. The present review summarises recent studies in this field. To this end, the available complexes binding N 2 and/or its intermediates on the pathway to ammonia are subdivided into systems containing early transition metals, Mo & W, iron and late transition metals. The implications of the findings obtained on low-molecular weight compounds with respect to the functionalisation of N 2 and the reduction of N 2 to ammonia on the FeMoco of nitrogenase are considered.
Metallomics and metalloproteomics are an emerging scientific area focusing on the molecular mechanisms of metal-dependent life processes and the entirety of metal and metalloid species within a cell or tissue/organ. Metallomics is also a part of functional proteomics, complements metabonomics and structural geonomics of metalloproteins. This review summarizes the recent progress of metallomics with a focus on analytical techniques capable of high-throughput quantification, distribution, speciation, identification and structural characterisation. The applications of these advanced analytical methods in the identification of metallo-/phosphor-/seleno-proteins, probing of structure-function relationships of metalloproteins, and the study of metallodrugs will be selectively outlined.
This chapter reviews the literature reported during 2011 on fullerene chemistry including fullerene production and properties, organic and organometallic chemistry, endohedral derivatives and advanced materials as well as theoretical studies and possible applications of fullerene and its derivatives.