Base de dados : MEDLINE
Pesquisa : B03.440.475.100.655 [Categoria DeCS]
Referências encontradas : 3 [refinar]
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[PMID]:24508456
[Au] Autor:Araki M; Akimoto S; Mimuro M; Tsuchiya T
[Ad] Endereço:Graduate School of Human and Environmental Studies, Kyoto University, Kyoto 606-8501, Japan.
[Ti] Título:Artificially acquired chlorophyll b is highly acceptable to the thylakoid-lacking cyanobacterium, Gloeobacter violaceus PCC 7421.
[So] Source:Plant Physiol Biochem;81:155-62, 2014 Aug.
[Is] ISSN:1873-2690
[Cp] País de publicação:France
[La] Idioma:eng
[Ab] Resumo:Unicellular cyanobacterium Gloeobacter violaceus is an only known oxygenic photosynthetic organism that lacks thylakoid membrane. Molecular phylogenetic analyses indicate that G. violaceus is an early-branching cyanobacterium within cyanobacterial clade. Therefore, the photosynthetic system of G. violaceus is considered to be partly similar to that of the ancestral cyanobacteria that would lack thylakoid membrane. G. violaceus possesses chlorophyll (Chl) a as the only chlorophyll species like most cyanobacteria. It was proposed that the ancestral oxygenic photosynthetic organism had not only Chl a and phycobilins but also Chl b. However, no organism which contains both Chl a and Chl b and lacks thylakoid membrane has been found in nature. Therefore, we introduced the chlorophyllide a oxygenase gene responsible for Chl b biosynthesis into G. violaceus. In the resultant transformant, Chl b accumulated at approximately 11% of total Chl independent of growth phase. Photosystem I complexes isolated from the transformant contained Chl b at 9.9% of total Chl. The presence of Chl b in the photosystem I complexes did not inhibit trimer formation. Furthermore, time-resolved fluorescence spectrum demonstrated that Chl b transferred energy to Chl a in the photosystem I complexes and did not disturb the energy transfer among the Chl a molecules. These results show that G. violaceus is tolerant to artificially produced Chl b and suggest the flexibility of photosystem for Chl composition in the ancestral oxygenic photosynthetic organism.
[Mh] Termos MeSH primário: Clorofila/genética
Cianobactérias/genética
Oxigenases/genética
[Mh] Termos MeSH secundário: Proteínas de Bactérias/genética
Cianobactérias/metabolismo
Complexo de Proteína do Fotossistema I/metabolismo
Proclorófitas/genética
Proclorófitas/metabolismo
Fatores de Tempo
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Photosystem I Protein Complex); 1406-65-1 (Chlorophyll); 5712ZB110R (chlorophyll b); EC 1.13.- (Oxygenases); EC 1.13.12.- (chlorophyll a oxygenase); YF5Q9EJC8Y (chlorophyll a)
[Em] Mês de entrada:1503
[Cu] Atualização por classe:161020
[Lr] Data última revisão:
161020
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:140211
[St] Status:MEDLINE


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[PMID]:19761753
[Au] Autor:Herbstová M; Litvín R; Gardian Z; Komenda J; Vácha F
[Ad] Endereço:Institute of Plant Molecular Biology, Biology Centre, Academy of Sciences of the Czech Republic, Branisovská 31, 37005 Ceské Budejovice, Czech Republic.
[Ti] Título:Localization of Pcb antenna complexes in the photosynthetic prokaryote Prochlorothrix hollandica.
[So] Source:Biochim Biophys Acta;1797(1):89-97, 2010 Jan.
[Is] ISSN:0006-3002
[Cp] País de publicação:Netherlands
[La] Idioma:eng
[Ab] Resumo:The freshwater filamentous green oxyphotobacterium Prochlorothrix hollandica is an unusual oxygenic photoautotrophic cyanobacterium differing from most of the others by the presence of light-harvesting Pcb antenna binding both chlorophylls a and b and by the absence of phycobilins. The pigment-protein complexes of P. hollandica SAG 10.89 (CCAP 1490/1) were isolated from dodecylmaltoside solubilized thylakoid membranes on sucrose density gradient and characterized by biochemical, spectroscopic and immunoblotting methods. The Pcb antennae production is suppressed by high light conditions (>200 mumol photons m(-2) s(-1)) in P. hollandica. PcbC protein was found either in higher oligomeric states or coupled to PS I (forming antenna rings around PS I). PcbA and PcbB are most probably only very loosely bound to photosystems; we assume that these pigment-protein complexes function as low light-induced mobile antennae. Further, we have detected alpha-carotene in substantial quantities in P. hollandica thylakoid membranes, indicating the presence of chloroplast-like carotenoid synthetic pathway which is not present in common cyanobacteria.
[Mh] Termos MeSH primário: Fotossíntese/fisiologia
Prochlorothrix/metabolismo
[Mh] Termos MeSH secundário: Cromatografia em Gel
Cromatografia Líquida de Alta Pressão
Eletroforese em Gel de Poliacrilamida
Immunoblotting
Luz
Complexo de Proteína do Fotossistema I/isolamento & purificação
Complexo de Proteína do Fotossistema I/metabolismo
Complexo de Proteína do Fotossistema II/isolamento & purificação
Complexo de Proteína do Fotossistema II/metabolismo
Proclorófitas/metabolismo
Tilacoides/metabolismo
Tilacoides/ultraestrutura
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Photosystem I Protein Complex); 0 (Photosystem II Protein Complex)
[Em] Mês de entrada:1004
[Cu] Atualização por classe:161126
[Lr] Data última revisão:
161126
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:090919
[St] Status:MEDLINE
[do] DOI:10.1016/j.bbabio.2009.09.002


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[PMID]:11943141
[Au] Autor:Chen M; Quinnell RG; Larkum AW
[Ad] Endereço:School of Biological Sciences, The University of Sydney, Sydney, NSW 2006, Australia.
[Ti] Título:The major light-harvesting pigment protein of Acaryochloris marina.
[So] Source:FEBS Lett;514(2-3):149-52, 2002 Mar 13.
[Is] ISSN:0014-5793
[Cp] País de publicação:England
[La] Idioma:eng
[Ab] Resumo:The major light-harvesting protein complex containing chlorophyll (Chl) d was isolated from Acaryochloris marina thylakoid membranes. Isolation was achieved by detergent solubilisation followed by separation on 6-40% sucrose gradients using ultracentrifugation. The best Chl d yield (70%) used 0.3% dodecyl maltoside, 0.15% octyl glucoside, 0.05% zwittergent 3-14 with the detergent:total Chl d ratio around 10:1 (w/w). Characterisation of the light-harvesting pigment protein complex (lhc) involved non-denaturing electrophoresis, SDS-PAGE, absorbance and fluorescence spectroscopy. The main polypeptide in the lhc was shown to be ca. 34 kDa and to contain Chl d and Chl a, indicating that the Acaryochloris lhc is similar to that of prochlorophytes. The Chl a level varied with the culture conditions, which is consistent with previous findings.
[Mh] Termos MeSH primário: Complexo de Proteínas do Centro de Reação Fotossintética/química
[Mh] Termos MeSH secundário: Proteínas de Bactérias/química
Proteínas de Bactérias/isolamento & purificação
Centrifugação com Gradiente de Concentração
Cianobactérias
Detergentes/química
Eletroforese em Gel de Poliacrilamida
Complexo de Proteínas do Centro de Reação Fotossintética/isolamento & purificação
Proclorófitas
Espectrometria de Fluorescência
Espectrofotometria
Tilacoides/química
[Pt] Tipo de publicação:JOURNAL ARTICLE; RESEARCH SUPPORT, NON-U.S. GOV'T
[Nm] Nome de substância:
0 (Bacterial Proteins); 0 (Detergents); 0 (Photosynthetic Reaction Center Complex Proteins)
[Em] Mês de entrada:0205
[Cu] Atualização por classe:061115
[Lr] Data última revisão:
061115
[Sb] Subgrupo de revista:IM
[Da] Data de entrada para processamento:020412
[St] Status:MEDLINE



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