Substrate binding to a nitrite reductase induces a spin transition

The multiheme enzyme nitrite reductase catalyzes a 6-electron reduction of nitrite to ammonia. The reaction is initiated by substrate binding to the free axial position of the high spin penta-coordinated heme active site. The spin configuration of the resulting complex is crucial for discrimination...

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Detalles Bibliográficos
Autor principal:	Murgida, Daniel Horacio
Publicado:	2010
Materias:	Coordination reactions Enzymes Hemoglobin Porphyrins Raman spectroscopy Spin dynamics Active site Axial positions Catalytic cycles Electron reduction Experimental evidence High spins Nitrite reductase Resonance Raman spectroscopy Spin configurations Spin transition Substrate binding Vulgaris Electron spin resonance spectroscopy
Acceso en línea:	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_15206106_v114_n16_p5563_Martins http://hdl.handle.net/20.500.12110/paper_15206106_v114_n16_p5563_Martins
Aporte de:	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

id	paper:paper_15206106_v114_n16_p5563_Martins
record_format	dspace
spelling	paper:paper_15206106_v114_n16_p5563_Martins2023-06-08T16:19:03Z Substrate binding to a nitrite reductase induces a spin transition Murgida, Daniel Horacio Coordination reactions Enzymes Hemoglobin Porphyrins Raman spectroscopy Spin dynamics Active site Axial positions Catalytic cycles Electron reduction Experimental evidence High spins Nitrite reductase Resonance Raman spectroscopy Spin configurations Spin transition Substrate binding Vulgaris Electron spin resonance spectroscopy The multiheme enzyme nitrite reductase catalyzes a 6-electron reduction of nitrite to ammonia. The reaction is initiated by substrate binding to the free axial position of the high spin penta-coordinated heme active site. The spin configuration of the resulting complex is crucial for discrimination between the heterolytic vs homolytic character of the cleavage of the N-O bond and, therefore, subsequent steps of the catalytic cycle. Here, we report the first experimental evidence, based on resonance Raman spectroscopy, that nitrite binding to the enzyme from D. vulgaris induces a transition from the high spin to the low spin configuration in the catalytic heme, thereby favoring the heterolytic route. © 2010 American Chemical Society. Fil:Murgida, D.H. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. 2010 https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_15206106_v114_n16_p5563_Martins http://hdl.handle.net/20.500.12110/paper_15206106_v114_n16_p5563_Martins
institution	Universidad de Buenos Aires
institution_str	I-28
repository_str	R-134
collection	Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic	Coordination reactions Enzymes Hemoglobin Porphyrins Raman spectroscopy Spin dynamics Active site Axial positions Catalytic cycles Electron reduction Experimental evidence High spins Nitrite reductase Resonance Raman spectroscopy Spin configurations Spin transition Substrate binding Vulgaris Electron spin resonance spectroscopy
spellingShingle	Coordination reactions Enzymes Hemoglobin Porphyrins Raman spectroscopy Spin dynamics Active site Axial positions Catalytic cycles Electron reduction Experimental evidence High spins Nitrite reductase Resonance Raman spectroscopy Spin configurations Spin transition Substrate binding Vulgaris Electron spin resonance spectroscopy Murgida, Daniel Horacio Substrate binding to a nitrite reductase induces a spin transition
topic_facet	Coordination reactions Enzymes Hemoglobin Porphyrins Raman spectroscopy Spin dynamics Active site Axial positions Catalytic cycles Electron reduction Experimental evidence High spins Nitrite reductase Resonance Raman spectroscopy Spin configurations Spin transition Substrate binding Vulgaris Electron spin resonance spectroscopy
description	The multiheme enzyme nitrite reductase catalyzes a 6-electron reduction of nitrite to ammonia. The reaction is initiated by substrate binding to the free axial position of the high spin penta-coordinated heme active site. The spin configuration of the resulting complex is crucial for discrimination between the heterolytic vs homolytic character of the cleavage of the N-O bond and, therefore, subsequent steps of the catalytic cycle. Here, we report the first experimental evidence, based on resonance Raman spectroscopy, that nitrite binding to the enzyme from D. vulgaris induces a transition from the high spin to the low spin configuration in the catalytic heme, thereby favoring the heterolytic route. © 2010 American Chemical Society.
author	Murgida, Daniel Horacio
author_facet	Murgida, Daniel Horacio
author_sort	Murgida, Daniel Horacio
title	Substrate binding to a nitrite reductase induces a spin transition
title_short	Substrate binding to a nitrite reductase induces a spin transition
title_full	Substrate binding to a nitrite reductase induces a spin transition
title_fullStr	Substrate binding to a nitrite reductase induces a spin transition
title_full_unstemmed	Substrate binding to a nitrite reductase induces a spin transition
title_sort	substrate binding to a nitrite reductase induces a spin transition
publishDate	2010
url	https://bibliotecadigital.exactas.uba.ar/collection/paper/document/paper_15206106_v114_n16_p5563_Martins http://hdl.handle.net/20.500.12110/paper_15206106_v114_n16_p5563_Martins
work_keys_str_mv	AT murgidadanielhoracio substratebindingtoanitritereductaseinducesaspintransition
_version_	1768544565477769216

Substrate binding to a nitrite reductase induces a spin transition

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