Real-time observation of tetrapyrrole binding to an engineered bacterial phytochrome

Near-infrared fluorescent proteins engineered from bacterial phytochromes are important for deep-tissue imaging in vivo, but the mechanism through which they bind to chromophores is not fully understood. Here the authors structurally analyze biliverdin binding to miRFP proteins using time-resolved s...

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Autores principales:	Yusaku Hontani, Mikhail Baloban, Francisco Velazquez Escobar, Swetta A. Jansen, Daria M. Shcherbakova, Jörn Weißenborn, Miroslav Kloz, Maria Andrea Mroginski, Vladislav V. Verkhusha, John T. M. Kennis
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Chemistry QD1-999
Acceso en línea:	https://doaj.org/article/27b7026a2cc7487aa17fc5c6ab44f7c5
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spelling	oai:doaj.org-article:27b7026a2cc7487aa17fc5c6ab44f7c52021-12-02T12:00:27ZReal-time observation of tetrapyrrole binding to an engineered bacterial phytochrome10.1038/s42004-020-00437-32399-3669https://doaj.org/article/27b7026a2cc7487aa17fc5c6ab44f7c52021-01-01T00:00:00Zhttps://doi.org/10.1038/s42004-020-00437-3https://doaj.org/toc/2399-3669Near-infrared fluorescent proteins engineered from bacterial phytochromes are important for deep-tissue imaging in vivo, but the mechanism through which they bind to chromophores is not fully understood. Here the authors structurally analyze biliverdin binding to miRFP proteins using time-resolved stimulated Raman spectroscopy and quantum mechanical/molecular mechanics calculations.Yusaku HontaniMikhail BalobanFrancisco Velazquez EscobarSwetta A. JansenDaria M. ShcherbakovaJörn WeißenbornMiroslav KlozMaria Andrea MroginskiVladislav V. VerkhushaJohn T. M. KennisNature PortfolioarticleChemistryQD1-999ENCommunications Chemistry, Vol 4, Iss 1, Pp 1-11 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Chemistry QD1-999
spellingShingle	Chemistry QD1-999 Yusaku Hontani Mikhail Baloban Francisco Velazquez Escobar Swetta A. Jansen Daria M. Shcherbakova Jörn Weißenborn Miroslav Kloz Maria Andrea Mroginski Vladislav V. Verkhusha John T. M. Kennis Real-time observation of tetrapyrrole binding to an engineered bacterial phytochrome
description	Near-infrared fluorescent proteins engineered from bacterial phytochromes are important for deep-tissue imaging in vivo, but the mechanism through which they bind to chromophores is not fully understood. Here the authors structurally analyze biliverdin binding to miRFP proteins using time-resolved stimulated Raman spectroscopy and quantum mechanical/molecular mechanics calculations.
format	article
author	Yusaku Hontani Mikhail Baloban Francisco Velazquez Escobar Swetta A. Jansen Daria M. Shcherbakova Jörn Weißenborn Miroslav Kloz Maria Andrea Mroginski Vladislav V. Verkhusha John T. M. Kennis
author_facet	Yusaku Hontani Mikhail Baloban Francisco Velazquez Escobar Swetta A. Jansen Daria M. Shcherbakova Jörn Weißenborn Miroslav Kloz Maria Andrea Mroginski Vladislav V. Verkhusha John T. M. Kennis
author_sort	Yusaku Hontani
title	Real-time observation of tetrapyrrole binding to an engineered bacterial phytochrome
title_short	Real-time observation of tetrapyrrole binding to an engineered bacterial phytochrome
title_full	Real-time observation of tetrapyrrole binding to an engineered bacterial phytochrome
title_fullStr	Real-time observation of tetrapyrrole binding to an engineered bacterial phytochrome
title_full_unstemmed	Real-time observation of tetrapyrrole binding to an engineered bacterial phytochrome
title_sort	real-time observation of tetrapyrrole binding to an engineered bacterial phytochrome
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/27b7026a2cc7487aa17fc5c6ab44f7c5
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Real-time observation of tetrapyrrole binding to an engineered bacterial phytochrome

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