Structural Analysis of a Nitrogenase Iron Protein from <named-content content-type="genus-species">Methanosarcina acetivorans</named-content>: Implications for CO2 Capture by a Surface-Exposed [Fe4S4] Cluster

ABSTRACT Nitrogenase iron (Fe) proteins reduce CO2 to CO and/or hydrocarbons under ambient conditions. Here, we report a 2.4-Å crystal structure of the Fe protein from Methanosarcina acetivorans (MaNifH), which is generated in the presence of a reductant, dithionite, and an alternative CO2 source, b...

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Autores principales:	Lee A. Rettberg, Wonchull Kang, Martin T. Stiebritz, Caleb J. Hiller, Chi Chung Lee, Jasper Liedtke, Markus W. Ribbe, Yilin Hu
Formato:	article
Lenguaje:	EN
Publicado:	American Society for Microbiology 2019
Materias:	CO2 capture FeS cluster iron protein methanogen nitrogenase Microbiology QR1-502
Acceso en línea:	https://doaj.org/article/b8db188bd46a4cd2bf01b2ab9361b821
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spelling	oai:doaj.org-article:b8db188bd46a4cd2bf01b2ab9361b8212021-11-15T16:22:10ZStructural Analysis of a Nitrogenase Iron Protein from <named-content content-type="genus-species">Methanosarcina acetivorans</named-content>: Implications for CO<sub>2</sub> Capture by a Surface-Exposed [Fe<sub>4</sub>S<sub>4</sub>] Cluster10.1128/mBio.01497-192150-7511https://doaj.org/article/b8db188bd46a4cd2bf01b2ab9361b8212019-08-01T00:00:00Zhttps://journals.asm.org/doi/10.1128/mBio.01497-19https://doaj.org/toc/2150-7511ABSTRACT Nitrogenase iron (Fe) proteins reduce CO2 to CO and/or hydrocarbons under ambient conditions. Here, we report a 2.4-Å crystal structure of the Fe protein from Methanosarcina acetivorans (MaNifH), which is generated in the presence of a reductant, dithionite, and an alternative CO2 source, bicarbonate. Structural analysis of this methanogen Fe protein species suggests that CO2 is possibly captured in an unactivated, linear conformation near the [Fe4S4] cluster of MaNifH by a conserved arginine (Arg) pair in a concerted and, possibly, asymmetric manner. Density functional theory calculations and mutational analyses provide further support for the capture of CO2 on MaNifH while suggesting a possible role of Arg in the initial coordination of CO2 via hydrogen bonding and electrostatic interactions. These results provide a useful framework for further mechanistic investigations of CO2 activation by a surface-exposed [Fe4S4] cluster, which may facilitate future development of FeS catalysts for ambient conversion of CO2 into valuable chemical commodities. IMPORTANCE This work reports the crystal structure of a previously uncharacterized Fe protein from a methanogenic organism, which provides important insights into the structural properties of the less-characterized, yet highly interesting archaeal nitrogenase enzymes. Moreover, the structure-derived implications for CO2 capture by a surface-exposed [Fe4S4] cluster point to the possibility of developing novel strategies for CO2 sequestration while providing the initial insights into the unique mechanism of FeS-based CO2 activation.Lee A. RettbergWonchull KangMartin T. StiebritzCaleb J. HillerChi Chung LeeJasper LiedtkeMarkus W. RibbeYilin HuAmerican Society for MicrobiologyarticleCO2 captureFeS clusteriron proteinmethanogennitrogenaseMicrobiologyQR1-502ENmBio, Vol 10, Iss 4 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	CO2 capture FeS cluster iron protein methanogen nitrogenase Microbiology QR1-502
spellingShingle	CO2 capture FeS cluster iron protein methanogen nitrogenase Microbiology QR1-502 Lee A. Rettberg Wonchull Kang Martin T. Stiebritz Caleb J. Hiller Chi Chung Lee Jasper Liedtke Markus W. Ribbe Yilin Hu Structural Analysis of a Nitrogenase Iron Protein from <named-content content-type="genus-species">Methanosarcina acetivorans</named-content>: Implications for CO<sub>2</sub> Capture by a Surface-Exposed [Fe<sub>4</sub>S<sub>4</sub>] Cluster
description	ABSTRACT Nitrogenase iron (Fe) proteins reduce CO2 to CO and/or hydrocarbons under ambient conditions. Here, we report a 2.4-Å crystal structure of the Fe protein from Methanosarcina acetivorans (MaNifH), which is generated in the presence of a reductant, dithionite, and an alternative CO2 source, bicarbonate. Structural analysis of this methanogen Fe protein species suggests that CO2 is possibly captured in an unactivated, linear conformation near the [Fe4S4] cluster of MaNifH by a conserved arginine (Arg) pair in a concerted and, possibly, asymmetric manner. Density functional theory calculations and mutational analyses provide further support for the capture of CO2 on MaNifH while suggesting a possible role of Arg in the initial coordination of CO2 via hydrogen bonding and electrostatic interactions. These results provide a useful framework for further mechanistic investigations of CO2 activation by a surface-exposed [Fe4S4] cluster, which may facilitate future development of FeS catalysts for ambient conversion of CO2 into valuable chemical commodities. IMPORTANCE This work reports the crystal structure of a previously uncharacterized Fe protein from a methanogenic organism, which provides important insights into the structural properties of the less-characterized, yet highly interesting archaeal nitrogenase enzymes. Moreover, the structure-derived implications for CO2 capture by a surface-exposed [Fe4S4] cluster point to the possibility of developing novel strategies for CO2 sequestration while providing the initial insights into the unique mechanism of FeS-based CO2 activation.
format	article
author	Lee A. Rettberg Wonchull Kang Martin T. Stiebritz Caleb J. Hiller Chi Chung Lee Jasper Liedtke Markus W. Ribbe Yilin Hu
author_facet	Lee A. Rettberg Wonchull Kang Martin T. Stiebritz Caleb J. Hiller Chi Chung Lee Jasper Liedtke Markus W. Ribbe Yilin Hu
author_sort	Lee A. Rettberg
title	Structural Analysis of a Nitrogenase Iron Protein from <named-content content-type="genus-species">Methanosarcina acetivorans</named-content>: Implications for CO<sub>2</sub> Capture by a Surface-Exposed [Fe<sub>4</sub>S<sub>4</sub>] Cluster
title_short	Structural Analysis of a Nitrogenase Iron Protein from <named-content content-type="genus-species">Methanosarcina acetivorans</named-content>: Implications for CO<sub>2</sub> Capture by a Surface-Exposed [Fe<sub>4</sub>S<sub>4</sub>] Cluster
title_full	Structural Analysis of a Nitrogenase Iron Protein from <named-content content-type="genus-species">Methanosarcina acetivorans</named-content>: Implications for CO<sub>2</sub> Capture by a Surface-Exposed [Fe<sub>4</sub>S<sub>4</sub>] Cluster
title_fullStr	Structural Analysis of a Nitrogenase Iron Protein from <named-content content-type="genus-species">Methanosarcina acetivorans</named-content>: Implications for CO<sub>2</sub> Capture by a Surface-Exposed [Fe<sub>4</sub>S<sub>4</sub>] Cluster
title_full_unstemmed	Structural Analysis of a Nitrogenase Iron Protein from <named-content content-type="genus-species">Methanosarcina acetivorans</named-content>: Implications for CO<sub>2</sub> Capture by a Surface-Exposed [Fe<sub>4</sub>S<sub>4</sub>] Cluster
title_sort	structural analysis of a nitrogenase iron protein from <named-content content-type="genus-species">methanosarcina acetivorans</named-content>: implications for co<sub>2</sub> capture by a surface-exposed [fe<sub>4</sub>s<sub>4</sub>] cluster
publisher	American Society for Microbiology
publishDate	2019
url	https://doaj.org/article/b8db188bd46a4cd2bf01b2ab9361b821
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Structural Analysis of a Nitrogenase Iron Protein from <named-content content-type="genus-species">Methanosarcina acetivorans</named-content>: Implications for CO<sub>2</sub> Capture by a Surface-Exposed [Fe<sub>4</sub>S<sub>4</sub>] Cluster

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