Cofactor Binding Dynamics Influence the Catalytic Activity and Selectivity of an Artificial Metalloenzyme
We present an artificial metalloenzyme based on the transcriptional regulator LmrR that exhibits dynamics involving the positioning of its abiological metal cofactor. The position of the cofactor, in turn, was found to be related to the preferred catalytic reactivity, which is either the enantiosele...
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Published in | ACS catalysis Vol. 10; no. 20; pp. 11783 - 11790 |
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Main Authors | , , , , , , , |
Format | Journal Article |
Language | English |
Published |
American Chemical Society
16.10.2020
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Online Access | Get full text |
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Summary: | We
present an artificial metalloenzyme based on the transcriptional
regulator LmrR that exhibits dynamics involving the positioning of
its abiological metal cofactor. The position of the cofactor, in turn,
was found to be related to the preferred catalytic reactivity, which
is either the enantioselective Friedel–Crafts alkylation of
indoles with β-substituted enones or the tandem Friedel–Crafts
alkylation/enantioselective protonation of indoles with α-substituted
enones. The artificial metalloenzyme could be specialized for one
of these catalytic reactions introducing a single mutation in the
protein. The relation between cofactor dynamics and activity and selectivity
in catalysis has not been described for natural enzymes and, to date,
appears to be particular for artificial metalloenzymes. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 2155-5435 2155-5435 |
DOI: | 10.1021/acscatal.0c01619 |