Substrate Profiling of the Cobalt Nitrile Hydratase from <i>Rhodococcus rhodochrous</i> ATCC BAA 870

The aromatic substrate profile of the cobalt nitrile hydratase from <i>Rhodococcus rhodochrous</i> ATCC BAA 870 was evaluated against a wide range of nitrile containing compounds (>60). To determine the substrate limits of this enzyme, compounds ranging in size from small (90 Da)...

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Main Authors:	Adelaide R. Mashweu, Varsha P. Chhiba-Govindjee, Moira L. Bode, Dean Brady
Format:	Article
Language:	English
Published:	MDPI AG 2020-01-01
Series:	Molecules
Subjects:	green chemistry nitrile hydratase biocatalysis carboxamide
Online Access:	https://www.mdpi.com/1420-3049/25/1/238

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record_format	Article
spelling	doaj-fa2bf4b19f9b47aaa7f7664bb0a199dd2020-11-25T01:46:21ZengMDPI AGMolecules1420-30492020-01-0125123810.3390/molecules25010238molecules25010238Substrate Profiling of the Cobalt Nitrile Hydratase from <i>Rhodococcus rhodochrous</i> ATCC BAA 870Adelaide R. Mashweu0Varsha P. Chhiba-Govindjee1Moira L. Bode2Dean Brady3Molecular Sciences Institute, School of Chemistry, University of the Witwatersrand, Johannesburg 2050, South AfricaMolecular Sciences Institute, School of Chemistry, University of the Witwatersrand, Johannesburg 2050, South AfricaMolecular Sciences Institute, School of Chemistry, University of the Witwatersrand, Johannesburg 2050, South AfricaMolecular Sciences Institute, School of Chemistry, University of the Witwatersrand, Johannesburg 2050, South AfricaThe aromatic substrate profile of the cobalt nitrile hydratase from <i>Rhodococcus rhodochrous</i> ATCC BAA 870 was evaluated against a wide range of nitrile containing compounds (>60). To determine the substrate limits of this enzyme, compounds ranging in size from small (90 Da) to large (325 Da) were evaluated. Larger compounds included those with a bi-aryl axis, prepared by the Suzuki coupling reaction, Morita−Baylis−Hillman adducts, heteroatom-linked diarylpyridines prepared by Buchwald−Hartwig cross-coupling reactions and imidazo[1,2-<i>a</i>]pyridines prepared by the Groebke−Blackburn−Bienaymé multicomponent reaction. The enzyme active site was moderately accommodating, accepting almost all of the small aromatic nitriles, the diarylpyridines and most of the bi-aryl compounds and Morita−Baylis−Hillman products but not the Groebke−Blackburn−Bienaymé products. Nitrile conversion was influenced by steric hindrance around the cyano group, the presence of electron donating groups (e.g., methoxy) on the aromatic ring, and the overall size of the compound.https://www.mdpi.com/1420-3049/25/1/238green chemistrynitrile hydratasebiocatalysiscarboxamide
collection	DOAJ
language	English
format	Article
sources	DOAJ
author	Adelaide R. Mashweu Varsha P. Chhiba-Govindjee Moira L. Bode Dean Brady
spellingShingle	Adelaide R. Mashweu Varsha P. Chhiba-Govindjee Moira L. Bode Dean Brady Substrate Profiling of the Cobalt Nitrile Hydratase from <i>Rhodococcus rhodochrous</i> ATCC BAA 870 Molecules green chemistry nitrile hydratase biocatalysis carboxamide
author_facet	Adelaide R. Mashweu Varsha P. Chhiba-Govindjee Moira L. Bode Dean Brady
author_sort	Adelaide R. Mashweu
title	Substrate Profiling of the Cobalt Nitrile Hydratase from <i>Rhodococcus rhodochrous</i> ATCC BAA 870
title_short	Substrate Profiling of the Cobalt Nitrile Hydratase from <i>Rhodococcus rhodochrous</i> ATCC BAA 870
title_full	Substrate Profiling of the Cobalt Nitrile Hydratase from <i>Rhodococcus rhodochrous</i> ATCC BAA 870
title_fullStr	Substrate Profiling of the Cobalt Nitrile Hydratase from <i>Rhodococcus rhodochrous</i> ATCC BAA 870
title_full_unstemmed	Substrate Profiling of the Cobalt Nitrile Hydratase from <i>Rhodococcus rhodochrous</i> ATCC BAA 870
title_sort	substrate profiling of the cobalt nitrile hydratase from <i>rhodococcus rhodochrous</i> atcc baa 870
publisher	MDPI AG
series	Molecules
issn	1420-3049
publishDate	2020-01-01
description	The aromatic substrate profile of the cobalt nitrile hydratase from <i>Rhodococcus rhodochrous</i> ATCC BAA 870 was evaluated against a wide range of nitrile containing compounds (>60). To determine the substrate limits of this enzyme, compounds ranging in size from small (90 Da) to large (325 Da) were evaluated. Larger compounds included those with a bi-aryl axis, prepared by the Suzuki coupling reaction, Morita−Baylis−Hillman adducts, heteroatom-linked diarylpyridines prepared by Buchwald−Hartwig cross-coupling reactions and imidazo[1,2-<i>a</i>]pyridines prepared by the Groebke−Blackburn−Bienaymé multicomponent reaction. The enzyme active site was moderately accommodating, accepting almost all of the small aromatic nitriles, the diarylpyridines and most of the bi-aryl compounds and Morita−Baylis−Hillman products but not the Groebke−Blackburn−Bienaymé products. Nitrile conversion was influenced by steric hindrance around the cyano group, the presence of electron donating groups (e.g., methoxy) on the aromatic ring, and the overall size of the compound.
topic	green chemistry nitrile hydratase biocatalysis carboxamide
url	https://www.mdpi.com/1420-3049/25/1/238
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Substrate Profiling of the Cobalt Nitrile Hydratase from <i>Rhodococcus rhodochrous</i> ATCC BAA 870

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