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Photosynthetic complexes and light-dependant electron transport chain in the aerobic anoxygenic phototroph Roseicyclus mahoneyensis and its spontaneous mutants.
Hughes, Elizabeth; Alric, Jean; Yurkov, Vladimir.
Afiliação
  • Hughes E; Department of Microbiology, University of Manitoba, Winnipeg, Canada.
  • Alric J; Photosynthesis and Environment, Aix Marseille Univ, CEA Cadarache, CNRS UMR7265, BIAM, 13108, Saint Paul-Lez-Durance, France.
  • Yurkov V; Department of Microbiology, University of Manitoba, Winnipeg, Canada. vyurkov@umanitoba.ca.
Photosynth Res ; 144(3): 341-347, 2020 Jun.
Article em En | MEDLINE | ID: mdl-32248389
ABSTRACT
Spontaneous photosynthetic mutants of the aerobic anoxygenic phototrophic bacterium Roseicyclus mahoneyensis, strain ML6 have been identified based on phenotypic differences and spectrophotometric analysis. ML6 contains a reaction centre (RC) with absorption peaks at 755, 800, and 870 nm, light harvesting (LH) complex 1 at 870 nm, and monomodal LH2 at 805 nm; the mutant ML6(B) has only the LH2; ML6(DB) has also lost the LH1; in ML6(BN9O), the LH2 is absent and concentrations of LH1 and RC are much lower than in the wild type. RCs were isolated and purified from ML6 and ML6(BN9O); LH1-RC from ML6; and LH2 from ML6, ML6(B), and ML6(DB). All protein subunits composing the complexes were found to be of typical size. Flash-induced difference spectra revealed ML6 has a fully functional photosynthetic apparatus under aerobic and microaerophilic conditions, and as is typical for AAP, there is no photosynthetic activity anaerobically. ML6(BN9O), while also functional photosynthetically aerobically, showed lower rates due to the lack of LH2 and decreased concentrations of LH1 and RC. ML6(B) and ML6(DB) showed no photoinduced electron transport. Action spectra of light-mediated reactions were also performed on ML6 and ML6(BN9O) to reveal that the majority of carotenoids are not involved in light harvesting. Finally, redox titrations were carried out on membranes of ML6 and ML6(BN9O) to confirm that midpoint redox potentials of the QA, RC-bound cytochrome, and P+ were similar in both strains. QA midpoint potential is + 65 mV, cytochrome is + 245 mV, and P+ is + 430 mV.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Fotossíntese / Rhodobacteraceae / Complexo de Proteínas do Centro de Reação Fotossintética / Transporte de Elétrons Idioma: En Ano de publicação: 2020 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Fotossíntese / Rhodobacteraceae / Complexo de Proteínas do Centro de Reação Fotossintética / Transporte de Elétrons Idioma: En Ano de publicação: 2020 Tipo de documento: Article