The Fitness of the Environment by Henderson L.J.

By Henderson L.J.

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S. Thayer, in Organometallic Compounds and Living Organisms, Academic Press, Orlando, 1984. 45 M. Peyrone, Ann. Chem. Pharm. 1844, Band LI, 1 ff. 46 B. Rosenberg, L. Vancamp, T. Krigas, Nature 1965, 205, 698–699. 47 B. Rosenberg, L. Vancamp, J. E. Trosko, V. H. Mansour, Nature 1969, 222, 385–386. 48 B. Lippert, in Cisplatin: Chemistry and Biochemistry of a Leading Anticancer Drug, John Wiley and Sons, New York, 1999. 49 B. K. Keppler, in Metal Complexes in Cancer Chemotherapy, VCH, Weinheim, 1993.

This synthetic challenge to activate molecular nitrogen by organometallic means was undertaken among others by the Russian group of Shilov, and also by Chatt and by Schrock [136– 140]. Despite structural determinations to a resolution of 1 Å it is still not completely understood how the hydrogen is reduced by the nitrogenase nor even how it binds initially to the cofactor FeMo, although majority opinion leans towards the belief that the association and the reduction of the nitrogen occur on one of the faces of the Fe4S4 cluster.

This area therefore will not be covered in this book. 15 Coenzyme B12 catalyzes 1–2 rearrangement. g. Schrauzer’s cobaloximes [125], have been developed. g. 16). It is interesting to note that bacteria (mercury lyases) can cleave the mercury carbon bond. This type of cleavage together with the reduction of organometallic compounds by biocatalysts has been reviewed by Ryabov [13]. 16 Biomethylation with methylcobalamin. 1* 19 20 1 A Novel Field of Research: Bioorganometallic Chemistry, Origins, and Founding Principles Although the question of the B12 coenzyme remains of current interest [126– 128], recent research has focused on other cofactors of metal enzymes, certain of which owe their suprising properties to an organometallic reactivity that is not yet understood.

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