Shortcut of the photosynthetic electron transfer in a mutant lacking the reaction center‐bound cytochrome subunit by gene disruption in a purple bacterium, <i>Rubrivivax gelatinosus</i>

Nagashima, Kenji V. P.; Shimada, Keizo; Matsuura, Kiyotaka

doi:10.1016/0014-5793(96)00382-1

Cited by 30 publications

(32 citation statements)

References 30 publications

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“…We have previously reported that a R. gelatinosus mutant lacking the cytochrome subunit is able to grow photosynthetically (43). Possibly, the main role of the cytochrome subunit is to reduce the photo-oxidized special pair of bacteriochlorophyll fast enough to avoid the electron backflow ("back reaction") from the ubiquinone to the oxidized special pair.…”

Section: Discussionmentioning

confidence: 99%

A New Cytochrome Subunit Bound to the Photosynthetic Reaction Center in the Purple Bacterium, Rhodovulum sulfidophilum

Masuda

Yoshida

Nagashima

et al. 1999

Journal of Biological Chemistry

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The nucleotide sequence of the puf operon, which contains the genes encoding the B870 light-harvesting protein and the reaction center complex of the purple photosynthetic bacterium, Rhodovulum sulfidophilum, was determined. The operon, which consisted of six genes, pufQ, pufB, pufA, pufL, pufM, and pufC, is a new variety in photosynthetic bacteria in the sense that pufQ and pufC coexist. The amino acid sequence of the cytochrome subunit of the reaction center deduced from the pufC sequence revealed that this cytochrome contains only three possible heme-binding motifs; the heme-1-binding motif of the corresponding tetraheme cytochrome subunits was not present. This is the first exception of the "tetraheme" cytochrome family in purple bacteria and green filamentous bacteria. The pufC sequence also revealed that the sixth axial ligands to heme-1 and heme-2 irons were not present in the cytochrome either. This cytochrome was actually detected in membrane preparation as a 43-kDa protein and shown to associate functionally with the photosynthetic reaction center as the immediate electron donor to the photo-oxidized special pair of bacteriochlorophyll. This new cytochrome should be useful for studies on the role of each heme in the cytochrome subunit of the bacterial reaction center and the evolution of proteins in photosynthetic electron transfer systems.

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Section: Discussionmentioning

confidence: 99%

A New Cytochrome Subunit Bound to the Photosynthetic Reaction Center in the Purple Bacterium, Rhodovulum sulfidophilum

Masuda

Yoshida

Nagashima

et al. 1999

Journal of Biological Chemistry

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“…Rvi. gelatinosus strains were grown in a rotary shaker in the dark at 30°C in PYS medium (43). Microoxic and oxic growth regimes were achieved as described previously (15).…”

Section: Methodsmentioning

confidence: 99%

“…Rvi. gelatinosus was transformed using a method described by Nagashima et al (43). Sequences of primers used in this study are listed in Table S3.…”

Section: Construction Of Mutantsmentioning

confidence: 99%

Three classes of oxygen-dependent cyclase involved in chlorophyll and bacteriochlorophyll biosynthesis

Chen

Canniffe

Hunter

2017

Proc. Natl. Acad. Sci. U.S.A.

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The biosynthesis of (bacterio)chlorophyll pigments is among the most productive biological pathways on Earth. Photosynthesis relies on these modified tetrapyrroles for the capture of solar radiation and its conversion to chemical energy. (Bacterio)chlorophylls have an isocyclic fifth ring, the formation of which has remained enigmatic for more than 60 y. This reaction is catalyzed by two unrelated cyclase enzymes using different chemistries. The majority of anoxygenic phototrophic bacteria use BchE, an O 2 -sensitive [4Fe-4S] cluster protein, whereas plants, cyanobacteria, and some phototrophic bacteria possess an O 2 -dependent enzyme, the major catalytic component of which is a diiron protein, AcsF. Plant and cyanobacterial mutants in ycf54 display impaired function of the O 2 -dependent enzyme, accumulating the reaction substrate. Swapping cyclases between cyanobacteria and purple phototrophic bacteria reveals three classes of the O 2 -dependent enzyme. AcsF from the purple betaproteobacterium Rubrivivax (Rvi.) gelatinosus rescues the loss not only of its cyanobacterial ortholog, cycI, in Synechocystis sp. PCC 6803, but also of ycf54; conversely, coexpression of cyanobacterial cycI and ycf54 is required to complement the loss of acsF in Rvi. gelatinosus. These results indicate that Ycf54 is a cyclase subunit in oxygenic phototrophs, and that different classes of the enzyme exist based on their requirement for an additional subunit. AcsF is the cyclase in Rvi. gelatinosus, whereas alphaproteobacterial cyclases require a newly discovered protein that we term BciE, encoded by a gene conserved in these organisms. These data delineate three classes of O 2 -dependent cyclase in chlorophototrophic organisms from higher plants to bacteria, and their evolution is discussed herein.

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“…palustris strain Rits from our culture collection and Rhodobacter (Rba.) sphaeroides 2.4.1 were grown on agar plate of PYS medium [10], and each single clone was used for this study. These bacteria were cultured anaerobically at 30°C with a usual light intensity of 30 lE m À2 s À1 in the liquid PYS medium.…”

Section: Culturing Of Purple Photosynthetic Bacteriamentioning

confidence: 99%

Structural determination of dihydro‐ and tetrahydrogeranylgeranyl groups at the 17‐propionate of bacteriochlorophylls‐a

2006

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In the final stage of bacteriochlorophyll (BChl) biosynthesis, the presence of BChl-a molecules possessing dihydrogeranylgeranyl and tetrahydrogeranylgeranyl groups at the 17-propionate has been reported. However, the molecular structures of such BChls-a have not yet been determined in terms of the positions of C‚C double bonds in the 17 2 -ester. In this study, we isolated significant amounts of such pure BChls-a from Rhodopseudomonas palustris and determined their structures by both mass spectrometry and 1 H and 13 C NMR spectroscopy. The determined structures enable us to discuss a stepwise reduction from a geranylgeranyl to phytyl substituent.

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Shortcut of the photosynthetic electron transfer in a mutant lacking the reaction center‐bound cytochrome subunit by gene disruption in a purple bacterium, Rubrivivax gelatinosus

Cited by 30 publications

References 30 publications

A New Cytochrome Subunit Bound to the Photosynthetic Reaction Center in the Purple Bacterium, Rhodovulum sulfidophilum

A New Cytochrome Subunit Bound to the Photosynthetic Reaction Center in the Purple Bacterium, Rhodovulum sulfidophilum

Three classes of oxygen-dependent cyclase involved in chlorophyll and bacteriochlorophyll biosynthesis

Structural determination of dihydro‐ and tetrahydrogeranylgeranyl groups at the 17‐propionate of bacteriochlorophylls‐a

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