Crystal structure of a photosynthetic LH1-RC in complex with its electron donor HiPIP

The high potential iron-sulfur (HiPIP) proteins are direct electron donors to the light-harvesting-reaction center complexes (LH1-RC) in photosynthetic β- and γ-Proteobacteria. Here, the authors present the 2.9 Å crystal structure of the HiPIP-bound LH1-RC complex from the thermophilic purple sulfur...

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Autores principales:	Tomoaki Kawakami, Long-Jiang Yu, Tai Liang, Koudai Okazaki, Michael T. Madigan, Yukihiro Kimura, Zheng-Yu Wang-Otomo
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/92c1475d6a364e6e9efc7f1b8a0fe6f4
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spelling	oai:doaj.org-article:92c1475d6a364e6e9efc7f1b8a0fe6f42021-12-02T14:21:27ZCrystal structure of a photosynthetic LH1-RC in complex with its electron donor HiPIP10.1038/s41467-021-21397-92041-1723https://doaj.org/article/92c1475d6a364e6e9efc7f1b8a0fe6f42021-02-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-21397-9https://doaj.org/toc/2041-1723The high potential iron-sulfur (HiPIP) proteins are direct electron donors to the light-harvesting-reaction center complexes (LH1-RC) in photosynthetic β- and γ-Proteobacteria. Here, the authors present the 2.9 Å crystal structure of the HiPIP-bound LH1-RC complex from the thermophilic purple sulfur bacterium Thermochromatium tepidum and discuss mechanistic implications for the electron transfer pathway.Tomoaki KawakamiLong-Jiang YuTai LiangKoudai OkazakiMichael T. MadiganYukihiro KimuraZheng-Yu Wang-OtomoNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-8 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Tomoaki Kawakami Long-Jiang Yu Tai Liang Koudai Okazaki Michael T. Madigan Yukihiro Kimura Zheng-Yu Wang-Otomo Crystal structure of a photosynthetic LH1-RC in complex with its electron donor HiPIP
description	The high potential iron-sulfur (HiPIP) proteins are direct electron donors to the light-harvesting-reaction center complexes (LH1-RC) in photosynthetic β- and γ-Proteobacteria. Here, the authors present the 2.9 Å crystal structure of the HiPIP-bound LH1-RC complex from the thermophilic purple sulfur bacterium Thermochromatium tepidum and discuss mechanistic implications for the electron transfer pathway.
format	article
author	Tomoaki Kawakami Long-Jiang Yu Tai Liang Koudai Okazaki Michael T. Madigan Yukihiro Kimura Zheng-Yu Wang-Otomo
author_facet	Tomoaki Kawakami Long-Jiang Yu Tai Liang Koudai Okazaki Michael T. Madigan Yukihiro Kimura Zheng-Yu Wang-Otomo
author_sort	Tomoaki Kawakami
title	Crystal structure of a photosynthetic LH1-RC in complex with its electron donor HiPIP
title_short	Crystal structure of a photosynthetic LH1-RC in complex with its electron donor HiPIP
title_full	Crystal structure of a photosynthetic LH1-RC in complex with its electron donor HiPIP
title_fullStr	Crystal structure of a photosynthetic LH1-RC in complex with its electron donor HiPIP
title_full_unstemmed	Crystal structure of a photosynthetic LH1-RC in complex with its electron donor HiPIP
title_sort	crystal structure of a photosynthetic lh1-rc in complex with its electron donor hipip
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/92c1475d6a364e6e9efc7f1b8a0fe6f4
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_version_	1718391561245425664

Crystal structure of a photosynthetic LH1-RC in complex with its electron donor HiPIP

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