The partial-proton-transfer concept

TTie geometries of the substrate-acid complexes suggest partial-proton-transfer through changes in the C=0 and acidic proton (X—H) bond lengths. The 

It is possible to phrase the partial-proton-transfer concept in the same language of hydrogen bonding that has been employed in the current debate as to whether 

It is unlikely that a given partial-proton-transfer would be overly efficient in aqueous solution. In much the same way as has been argued in the context of the LBHB hypothesis [97], the hydrogen bonding donor/acceptor properties of water and the entropic disorder associated with such a solution are likely to disrupt the hydrogen bond. However, the active sites of many enzymes are sequestered from bulk water, at least to some extent, and may therefore provide 

Although we have only discussed the partial-proton-transfer model for one of the B 12-dependent carbon-skeleton mutases [69], we can expect that there also exists a continuum between no protonation and full protonation of the substrate in the other reactions. Analogously, partial hydride removal from the substrate of glutamate mutase may serve to facilitate this rearrangement. 

Despite the abundance of literature on coenzyme-B 2 and the reactions it catalyzes, the field remains open. We hope that the present article provides useful 

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