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Photosynthetic Growth and Energy Conversion in an Engineered Phototroph Containing Thermochromatium tepidum Light-Harvesting Complex 1 and the Rhodobacter sphaeroides Reaction Center Complex.
Nagashima, Kenji V P; Nagashima, Sakiko; Kitashima, Masaharu; Inoue, Kazuhito; Madigan, Michael T; Kimura, Yukihiro; Wang-Otomo, Zheng-Yu.
Afiliación
  • Nagashima KVP; Research Institute for Integrated Science, Kanagawa University, 2946 Tsuchiya, Hiratsuka, Kanagawa 259-1293, Japan.
  • Nagashima S; Research Institute for Integrated Science, Kanagawa University, 2946 Tsuchiya, Hiratsuka, Kanagawa 259-1293, Japan.
  • Kitashima M; Department of Biological Sciences, Faculty of Science, Kanagawa University, 2946 Tsuchiya, Hiratsuka, Kanagawa 259-1293, Japan.
  • Inoue K; Research Institute for Integrated Science, Kanagawa University, 2946 Tsuchiya, Hiratsuka, Kanagawa 259-1293, Japan.
  • Madigan MT; Department of Biological Sciences, Faculty of Science, Kanagawa University, 2946 Tsuchiya, Hiratsuka, Kanagawa 259-1293, Japan.
  • Kimura Y; Department of Microbiology, Southern Illinois University, Carbondale, Illinois 62901, United States.
  • Wang-Otomo ZY; Department of Agrobioscience, Graduate School of Agriculture, Kobe University, Nada, Kobe 657-8501, Japan.
Biochemistry ; 60(36): 2685-2690, 2021 09 14.
Article en En | MEDLINE | ID: mdl-34448581
ABSTRACT
Light-harvesting complex 1 (LH1) of the thermophilic purple sulfur bacterium Thermochromatium tepidum can be expressed in the purple non-sulfur bacterium Rhodobacter sphaeroides and forms a functional RC-LH1 complex with the native Rba. sphaeroides reaction center (Nagashima, K. V. P., et al. Proc. Natl. Acad. Sci. U. S. A. 2017, 114, 10906-10911). Although there is a large uphill energy gap between Tch. tepidum LH1 and the Rba. sphaeroides RC in this chimeric complex, it has been shown that light energy can be transferred, consistent with that seen in the native Rba. sphaeroides RC-LH1 complex. In this study, the contribution of this chimeric complex to growth and photosynthetic energy conversion in the hybrid organism was quantified. The mutant synthesizing this chimeric complex was grown phototrophically under 940 nm light-emitting diode (LED) light preferentially absorbed by Tch. tepidum LH1 and showed faster growth at low intensities of this wavelength than both a mutant strain of Rba. sphaeroides lacking LH2 and a mutant lacking all light-harvesting complexes. When grown with 850 nm LED light, the strain containing the native Rba. sphaeroides LH1-RC grew faster than the chimeric strain. Electron transfer from the RC to the membrane-integrated cytochrome bc1 complex was also estimated by flash-induced absorption changes in heme b. The rate of ubiquinone transport through the LH1 ring structure in the chimeric strain was virtually the same as that in native Rba. sphaeroides. We conclude that Tch. tepidum LH1 can perform the physiological functions of native LH1 in Rba. sphaeroides.
Asunto(s)

Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Proteínas Bacterianas / Rhodobacter sphaeroides / Chromatiaceae / Proteínas del Complejo del Centro de Reacción Fotosintética / Complejos de Proteína Captadores de Luz Idioma: En Año: 2021 Tipo del documento: Article

Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Proteínas Bacterianas / Rhodobacter sphaeroides / Chromatiaceae / Proteínas del Complejo del Centro de Reacción Fotosintética / Complejos de Proteína Captadores de Luz Idioma: En Año: 2021 Tipo del documento: Article