Insights into Hydrocarbon Formation by Nitrogenase Cofactor Homologs

ABSTRACT The L-cluster is an all-iron homolog of nitrogenase cofactors. Driven by europium(II) diethylenetriaminepentaacetate [Eu(II)-DTPA], the isolated L-cluster is capable of ATP-independent reduction of CO and CN− to C1 to C4 and C1 to C6 hydrocarbons, respectively. Compared to its cofactor homo...

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Autores principales:	Chi Chung Lee, Yilin Hu, Markus W. Ribbe
Formato:	article
Lenguaje:	EN
Publicado:	American Society for Microbiology 2015
Materias:	Microbiology QR1-502
Acceso en línea:	https://doaj.org/article/bbe783271b1c4c8895a29b02f4dd5e7d
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spelling	oai:doaj.org-article:bbe783271b1c4c8895a29b02f4dd5e7d2021-11-15T15:41:32ZInsights into Hydrocarbon Formation by Nitrogenase Cofactor Homologs10.1128/mBio.00307-152150-7511https://doaj.org/article/bbe783271b1c4c8895a29b02f4dd5e7d2015-05-01T00:00:00Zhttps://journals.asm.org/doi/10.1128/mBio.00307-15https://doaj.org/toc/2150-7511ABSTRACT The L-cluster is an all-iron homolog of nitrogenase cofactors. Driven by europium(II) diethylenetriaminepentaacetate [Eu(II)-DTPA], the isolated L-cluster is capable of ATP-independent reduction of CO and CN− to C1 to C4 and C1 to C6 hydrocarbons, respectively. Compared to its cofactor homologs, the L-cluster generates considerably more CH4 from the reduction of CO and CN−, which could be explained by the presence of a “free” Fe atom that is “unmasked” by homocitrate as an additional site for methanation. Moreover, the elevated CH4 formation is accompanied by a decrease in the amount of longer hydrocarbons and/or the lengths of the hydrocarbon products, illustrating a competition between CH4 formation/release and C−C coupling/chain extension. These observations suggest the possibility of designing simpler synthetic clusters for hydrocarbon formation while establishing the L-cluster as a platform for mechanistic investigations of CO and CN− reduction without complications originating from the heterometal and homocitrate components. IMPORTANCE Nitrogenase is a metalloenzyme that is highly complex in structure and uniquely versatile in function. It catalyzes two reactions that parallel two important industrial processes: the reduction of nitrogen to ammonia, which parallels the Haber-Bosch process in ammonia production, and the reduction of carbon monoxide to hydrocarbons, which parallels the Fischer-Tropsch process in fuel production. Thus, the significance of nitrogenase can be appreciated from the perspective of the useful products it generates: (i) ammonia, the “fixed” nitrogen that is essential for the existence of the entire human population; and (ii) hydrocarbons, the “recycled” carbon fuel that could be used to directly address the worldwide energy shortage. This article provides initial insights into the catalytic characteristics of various nitrogenase cofactors in hydrocarbon formation. The reported assay system provides a useful tool for mechanistic investigations of this reaction while suggesting the possibility of designing bioinspired catalysts based on nitrogenase cofactors.Chi Chung LeeYilin HuMarkus W. RibbeAmerican Society for MicrobiologyarticleMicrobiologyQR1-502ENmBio, Vol 6, Iss 2 (2015)
institution	DOAJ
collection	DOAJ
language	EN
topic	Microbiology QR1-502
spellingShingle	Microbiology QR1-502 Chi Chung Lee Yilin Hu Markus W. Ribbe Insights into Hydrocarbon Formation by Nitrogenase Cofactor Homologs
description	ABSTRACT The L-cluster is an all-iron homolog of nitrogenase cofactors. Driven by europium(II) diethylenetriaminepentaacetate [Eu(II)-DTPA], the isolated L-cluster is capable of ATP-independent reduction of CO and CN− to C1 to C4 and C1 to C6 hydrocarbons, respectively. Compared to its cofactor homologs, the L-cluster generates considerably more CH4 from the reduction of CO and CN−, which could be explained by the presence of a “free” Fe atom that is “unmasked” by homocitrate as an additional site for methanation. Moreover, the elevated CH4 formation is accompanied by a decrease in the amount of longer hydrocarbons and/or the lengths of the hydrocarbon products, illustrating a competition between CH4 formation/release and C−C coupling/chain extension. These observations suggest the possibility of designing simpler synthetic clusters for hydrocarbon formation while establishing the L-cluster as a platform for mechanistic investigations of CO and CN− reduction without complications originating from the heterometal and homocitrate components. IMPORTANCE Nitrogenase is a metalloenzyme that is highly complex in structure and uniquely versatile in function. It catalyzes two reactions that parallel two important industrial processes: the reduction of nitrogen to ammonia, which parallels the Haber-Bosch process in ammonia production, and the reduction of carbon monoxide to hydrocarbons, which parallels the Fischer-Tropsch process in fuel production. Thus, the significance of nitrogenase can be appreciated from the perspective of the useful products it generates: (i) ammonia, the “fixed” nitrogen that is essential for the existence of the entire human population; and (ii) hydrocarbons, the “recycled” carbon fuel that could be used to directly address the worldwide energy shortage. This article provides initial insights into the catalytic characteristics of various nitrogenase cofactors in hydrocarbon formation. The reported assay system provides a useful tool for mechanistic investigations of this reaction while suggesting the possibility of designing bioinspired catalysts based on nitrogenase cofactors.
format	article
author	Chi Chung Lee Yilin Hu Markus W. Ribbe
author_facet	Chi Chung Lee Yilin Hu Markus W. Ribbe
author_sort	Chi Chung Lee
title	Insights into Hydrocarbon Formation by Nitrogenase Cofactor Homologs
title_short	Insights into Hydrocarbon Formation by Nitrogenase Cofactor Homologs
title_full	Insights into Hydrocarbon Formation by Nitrogenase Cofactor Homologs
title_fullStr	Insights into Hydrocarbon Formation by Nitrogenase Cofactor Homologs
title_full_unstemmed	Insights into Hydrocarbon Formation by Nitrogenase Cofactor Homologs
title_sort	insights into hydrocarbon formation by nitrogenase cofactor homologs
publisher	American Society for Microbiology
publishDate	2015
url	https://doaj.org/article/bbe783271b1c4c8895a29b02f4dd5e7d
work_keys_str_mv	AT chichunglee insightsintohydrocarbonformationbynitrogenasecofactorhomologs AT yilinhu insightsintohydrocarbonformationbynitrogenasecofactorhomologs AT markuswribbe insightsintohydrocarbonformationbynitrogenasecofactorhomologs
_version_	1718427665966301184

Insights into Hydrocarbon Formation by Nitrogenase Cofactor Homologs

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