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Wiley, New York, p 201 134. Kräutler B (1988) In: Glockling F (ed) The Biological Alkylation of Heavy Elements. Royal Society of Chemistry, London, p 168 135. Pailes WH, Hogenkamp HPC (1968) Biochem 7:4160 136. Milton P, Brown TL (1977) J Am Chem Soc 99:1390 137. Hogenkamp HPC, Bratt GT, Sun S (1985) Biochem 24:6428 138. Drennan CL, Matthews RG, Ludwig ML (1994) Curr Opin Struct Biol 4:919 139. Kräutler B (1995) In: Maskill H (ed) Organic Reactivity: Physical and Biological Aspects. Royal Society of Chemistry, London, p 209 140.

Uniquely in RNR-Ll, with relation to other B12 -dependent enzymes, a protein-centered thiyl-radical is generated (at cysteine-408) from the homolysis of the Co – C bond of the bound coenzyme, and this induces the radical reaction that formally leads to the reductive substitution by hydrogen of the 2 -hydroxyl group of the ribonucleotide. Homolytic cleavage of the Co – C bond is known to be accelerated by about 1011 -fold in RNR [237]. The crystal structures of both dGTP-free AdoCbl-dependent RNR-Ll in the apoform, and complexed with Coβ -adeninylpentyl-cobalamin (53), have been solved [236].

247. 248. 249. 250. 251. 252. 253. 254. 255. 256. 257. 258. 259. A. Butler · B. Kräutler Wetmore SD, Smith DM, Bennett JT, Radom L (2002) J Am Chem Soc 124:14054 Semialjac M, Schwarz H (2003) J Org Chem 68:6967 Semialjac M, Schwarz H (2004) Chem Eur J 10:2781 Tang K-H, Harms A, Frey PA (2002) Biochem 41:8767 Tang K-H, Casarez AD, Wu W, Frey PA (2003) Arch Biochem Biophys 418:49 Chang CH, Frey PA (2000) J Biol Chem 275:106 Berkovitch F, Behshad E, Tang K-H, Enns EA, Frey PA, Drennan CL (2004) Proc Nat Acad Sci USA 101:15870 Blakley RL (1982) In: Dolphin D (ed) B12 , vol II.

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Biological Organometallic Chemistry of B 12 by Butler P.A., Krautler B.

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