The active site structure and catalytic mechanism of arsenite oxidase

Abstract Arsenite oxidase is thought to be an ancient enzyme, originating before the divergence of the Archaea and the Bacteria. We have investigated the nature of the molybdenum active site of the arsenite oxidase from the Alphaproteobacterium Rhizobium sp. str. NT-26 using a combination of X-ray a...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Thomas P. Warelow, M. Jake Pushie, Julien J. H. Cotelesage, Joanne M. Santini, Graham N. George
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/55118be17e5a408eac6c4e27b9f5fa69
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:55118be17e5a408eac6c4e27b9f5fa69
record_format	dspace
spelling	oai:doaj.org-article:55118be17e5a408eac6c4e27b9f5fa692021-12-02T12:31:48ZThe active site structure and catalytic mechanism of arsenite oxidase10.1038/s41598-017-01840-y2045-2322https://doaj.org/article/55118be17e5a408eac6c4e27b9f5fa692017-05-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-01840-yhttps://doaj.org/toc/2045-2322Abstract Arsenite oxidase is thought to be an ancient enzyme, originating before the divergence of the Archaea and the Bacteria. We have investigated the nature of the molybdenum active site of the arsenite oxidase from the Alphaproteobacterium Rhizobium sp. str. NT-26 using a combination of X-ray absorption spectroscopy and computational chemistry. Our analysis indicates an oxidized Mo(VI) active site with a structure that is far from equilibrium. We propose that this is an entatic state imposed by the protein on the active site through relative orientation of the two molybdopterin cofactors, in a variant of the Rây-Dutt twist of classical coordination chemistry, which we call the pterin twist hypothesis. We discuss the implications of this hypothesis for other putatively ancient molybdopterin-based enzymes.Thomas P. WarelowM. Jake PushieJulien J. H. CotelesageJoanne M. SantiniGraham N. GeorgeNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-9 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Thomas P. Warelow M. Jake Pushie Julien J. H. Cotelesage Joanne M. Santini Graham N. George The active site structure and catalytic mechanism of arsenite oxidase
description	Abstract Arsenite oxidase is thought to be an ancient enzyme, originating before the divergence of the Archaea and the Bacteria. We have investigated the nature of the molybdenum active site of the arsenite oxidase from the Alphaproteobacterium Rhizobium sp. str. NT-26 using a combination of X-ray absorption spectroscopy and computational chemistry. Our analysis indicates an oxidized Mo(VI) active site with a structure that is far from equilibrium. We propose that this is an entatic state imposed by the protein on the active site through relative orientation of the two molybdopterin cofactors, in a variant of the Rây-Dutt twist of classical coordination chemistry, which we call the pterin twist hypothesis. We discuss the implications of this hypothesis for other putatively ancient molybdopterin-based enzymes.
format	article
author	Thomas P. Warelow M. Jake Pushie Julien J. H. Cotelesage Joanne M. Santini Graham N. George
author_facet	Thomas P. Warelow M. Jake Pushie Julien J. H. Cotelesage Joanne M. Santini Graham N. George
author_sort	Thomas P. Warelow
title	The active site structure and catalytic mechanism of arsenite oxidase
title_short	The active site structure and catalytic mechanism of arsenite oxidase
title_full	The active site structure and catalytic mechanism of arsenite oxidase
title_fullStr	The active site structure and catalytic mechanism of arsenite oxidase
title_full_unstemmed	The active site structure and catalytic mechanism of arsenite oxidase
title_sort	active site structure and catalytic mechanism of arsenite oxidase
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/55118be17e5a408eac6c4e27b9f5fa69
work_keys_str_mv	AT thomaspwarelow theactivesitestructureandcatalyticmechanismofarseniteoxidase AT mjakepushie theactivesitestructureandcatalyticmechanismofarseniteoxidase AT julienjhcotelesage theactivesitestructureandcatalyticmechanismofarseniteoxidase AT joannemsantini theactivesitestructureandcatalyticmechanismofarseniteoxidase AT grahamngeorge theactivesitestructureandcatalyticmechanismofarseniteoxidase AT thomaspwarelow activesitestructureandcatalyticmechanismofarseniteoxidase AT mjakepushie activesitestructureandcatalyticmechanismofarseniteoxidase AT julienjhcotelesage activesitestructureandcatalyticmechanismofarseniteoxidase AT joannemsantini activesitestructureandcatalyticmechanismofarseniteoxidase AT grahamngeorge activesitestructureandcatalyticmechanismofarseniteoxidase
_version_	1718394278859767808

The active site structure and catalytic mechanism of arsenite oxidase

Ejemplares similares