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- W2052097800 abstract "Enzyme-bound methyl-B12 transfers its methyl group to homocysteine during methionine synthesis. However, treatment of several types of organocobalt B12 models with arene- and alkanethiolates under ambient conditions leads only to thiolate ligation. The structure of [AsPh4][EtSCo(DH)2CH3] (DH = monoanion of dimethylglyoxime), the first characterization by X-ray crystallography of an organocobalt complex containing a unidentate coordinated thiolate, demonstrates unambiguously the S-ligation of ethanethiolate to Co, trans to the CH3 ligand. This compound contains a very long Co−S bond (2.342(2) A). However, the length of the Co−C bond (2.005(7) A) is typical; this result strongly supports reported FT-Raman spectroscopic data indicating that the thiolate-type ligand does not have a strong trans influence and does not significantly weaken the Co−C bond in the ground state. Since a strong trans influence alkyl ligand weakens the trans Co−C bond, we examined the effect of EtS- on Co((DO)(DOH)pn)(CH3)2 [(DO)(DOH)..." @default.
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- W2052097800 title "The First X-ray Structural Evidence Demonstrating Thiolate Coordination in an Organocobalt B<sub>12</sub> Model Complex: Implications for Methionine Synthase" @default.
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