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

By Butler P.A., Krautler B.

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Tollinger M, Konrat R, Kräutler B (1999) Helv Chim Acta 82:1596 83. Kontaxis G, Riether D, Hannak RB, Tollinger M, Kräutler B (1999) Helv Chim Acta 82:848 84. Kräutler B, Caderas C (1984) Helv Chim Acta 67:1891 85. Randaccio L, Furlan M, Geremia S, Slouf M (1998) Inorg Chem 37:5390 86. Kräutler B (1987) Helv Chim Acta 70:1268 87. Kräutler B (1999) In: Banerjee R (ed) Chemistry and Biochemistry of B12 . Wiley, New York, p 315 88. Ragsdale SW (1991) Crit Rev Biochem Mol Biol 26:261 89. Steiger B, Ruhe A, Walder L (1990) Anal Chem 62:759 90.

241. 242. 243. 244. 245. 246. 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.

1 Carbon Skeleton Mutases In the four known carbon skeleton rearrangement reactions, catalyzed by coenzyme B12 -dependent mutases, two vicinal groups (a hydrogen atom and an organic substituent) exchange their positions in a (pseudo)intramolecular fashion [173]. The B12 -cofactor is bound base-off/His-on at an interface between two modules, the B12 -binding and substrate activating domains (or subunits) as proven by the analysis of the crystal structures of methylmalonyl-CoA mutase (MMCM) [18] and glutamate mutase (GM) [19].

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