Widner, Florian J., Lawrence, Andrew D., Deery, Evelyne, Heldt, Dana, Frank, Stefanie, Gruber, Karl, Wurst, Klaus, Warren, Martin J., Kräutler, Bernhard (2016) Total Synthesis, Structure, and Biological Activity of Adenosylrhodibalamin, the Non-Natural Rhodium Homologue of Coenzyme B12. Angewandte Chemie International Edition, 55 (37). pp. 11281-11286. ISSN 1433-7851. (doi:10.1002/anie.201603738) (KAR id:57087)
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Official URL: http://doi.org/10.1002/anie.201603738 |
Abstract
B12 is unique among the vitamins as it is biosynthesized only by certain prokaryotes. The complexity of its synthesis relates to its distinctive cobalt corrin structure, which is essential for B12 biochemistry and renders coenzyme B12 (AdoCbl) so intriguingly suitable for enzymatic radical reactions. However, why is cobalt so fit for its role in B12‐dependent enzymes? To address this question, we considered the substitution of cobalt in AdoCbl with rhodium to generate the rhodium analogue 5′‐deoxy‐5′‐adenosylrhodibalamin (AdoRbl). AdoRbl was prepared by de novo total synthesis involving both biological and chemical steps. AdoRbl was found to be inactive in vivo in microbial bioassays for methionine synthase and acted as an in vitro inhibitor of an AdoCbl‐dependent diol dehydratase. Solution NMR studies of AdoRbl revealed a structure similar to that of AdoCbl. However, the crystal structure of AdoRbl revealed a conspicuously better fit of the corrin ligand for RhIII than for CoIII, challenging the current views concerning the evolution of corrins.
Item Type: | Article |
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DOI/Identification number: | 10.1002/anie.201603738 |
Uncontrolled keywords: | biosynthesis cobalt, total synthesis, transition metal, Vitamin B12 |
Subjects: | Q Science |
Divisions: | Divisions > Division of Natural Sciences > Biosciences |
Depositing User: | Susan Davies |
Date Deposited: | 02 Sep 2016 14:46 UTC |
Last Modified: | 05 Feb 2021 10:04 UTC |
Resource URI: | https://kar.kent.ac.uk/id/eprint/57087 (The current URI for this page, for reference purposes) |
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