Journal
NATURE CHEMICAL BIOLOGY
Volume 14, Issue 1, Pages 8-+Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/NCHEMBIO.2512
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Funding
- Superfund Research Program under the National Institute of Environmental Health Sciences [R01ES024294]
- Strategic Environmental Research and Development Program (SERDP) [ER-2312]
- Natural Science and Engineering Research Council of Canada (NSERC) Industrial Biocatalysis Network
- China-UT One-Hundred Scholars Program by the China Scholarship Council
- University of Tennessee
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Cobamides such as vitamin B-12 are structurally conserved, cobalt-containing tetrapyrrole biomolecules that have essential biochemical functions in all domains of life. In organohalide respiration, a vital biological process for the global cycling of natural and anthropogenic organohalogens, cobamides are the requisite prosthetic groups for carbon-halogen bond-cleaving reductive dehalogenases. This study reports the biosynthesis of a new cobamide with unsubstituted purine as the lower base and assigns unsubstituted purine a biological function by demonstrating that Co alpha-purinyl-cobamide (purinyl-Cba) is the native prosthetic group in catalytically active tetrachloroethene reductive dehalogenases of Desulfitobacterium hafniense. Cobamides featuring different lower bases are not functionally equivalent, and purinyl-Cba elicits different physiological responses in corrinoid-auxotrophic, organohalide-respiring bacteria. Given that cobamide-dependent enzymes catalyze key steps in essential metabolic pathways, the discovery of a novel cobamide structure and the realization that lower bases can effectively modulate enzyme activities generate opportunities to manipulate functionalities of microbiomes.
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