By Butler P.A., Krautler B.
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Extra resources for Biological Organometallic Chemistry of B 12
Tetanomorphum and Cl. cochlearium consist of a pair of B12 -binding subunits (σ ) and a larger substrate binding unit (ε). Two molecules of adenosyl-cobamide are bound in the heterotetramers (ε2 τ2 ). The cofactors from the two Clostridia were identiﬁed as pseudocoenzyme B12 (37) [151, 201] and adenosyl-factor A (38) , but coenzyme B12 (2) also functions as a cofactor [175, 200]. Binding of the substrate triggers homolysis of the Co – C bond of the adenosyl cofactor and in a similar situation to MMCM, homolysis and H-atom abstraction of the bound substrate are kinetically coupled.
To complete the catalytic cycle, the B12 -binding doare separated by ≈ 50 ˚ main thus must shuttle back and forth between these distant active sites . In the active site of the homocysteine binding domain the substrate forms a metal-ligand cluster with approximately tetrahedral geometry. This result agrees with the measurements showing four sulfur ligands to zinc in homocysteine complexes of E. coli MetH  (as mentioned earlier in the section). The crystallographic results on the structure of MetH and the ﬁnding of the base-off/His-on binding of the cofactor in a B12 -dependent methyl transferase were consistent with earlier ESR spectroscopic evidence for histidine binding to the cobalt center of p-cresolyl-cobamide (52) in the acetogen Sporomusa ovata [145, 169].
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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