Photooxidase Activity of Heated Chromatophores of Rhodospirillum rubrum

Lindstrom, E. S.

doi:10.1104/pp.37.2.127

Cited by 8 publications

(3 citation statements)

References 12 publications

(12 reference statements)

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“…[ 47,67,68 ] Thus, one can speculate that the latter supports a light‐driven iron redox chemistry in R. rubrum “magneticum” , providing Fe 2+ /Fe 3+ species required for the formation of magnetite. In this respect, light‐induced reactions between BChl and cytochromes (in particular their oxidation [ 69,70 ] ) might be of particular importance. The transferred genes mamP/E/T/X from M. gryphiswaldense encode a series of predicted redox proteins that exhibit c ‐type cytochrome motifs (so‐called magnetochrome (MCR) domains), and a participation of these MCR domains in an electron transfer chain has been suggested.…”

Section: Discussionmentioning

confidence: 99%

High‐Yield Production, Characterization, and Functionalization of Recombinant Magnetosomes in the Synthetic Bacterium Rhodospirillum rubrum “magneticum”

et al. 2021

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Recently, the photosynthetic Rhodospirillum rubrum has been endowed with the ability of magnetosome biosynthesis by transfer and expression of biosynthetic gene clusters from the magnetotactic bacterium Magnetospirillum gryphiswaldense. However, the growth conditions for efficient magnetite biomineralization in the synthetic R. rubrum “magneticum”, as well as the particles themselves (i.e., structure and composition), have so far not been fully characterized. In this study, different cultivation strategies, particularly the influence of temperature and light intensity, are systematically investigated to achieve optimal magnetosome biosynthesis. Reduced temperatures ≤16 °C and gradual increase in light intensities favor magnetite biomineralization at high rates, suggesting that magnetosome formation might utilize cellular processes, cofactors, and/or pathways that are linked to photosynthetic growth. Magnetosome yields of up to 13.6 mg magnetite per liter cell culture are obtained upon photoheterotrophic large‐scale cultivation. Furthermore, it is shown that even more complex, i.e., oligomeric, catalytically active functional moieties like enzyme proteins can be efficiently expressed on the magnetosome surface, thereby enabling the in vivo functionalization by genetic engineering. In summary, it is demonstrated that the synthetic R. rubrum “magneticum” is a suitable host for high‐yield magnetosome biosynthesis and the sustainable production of genetically engineered, bioconjugated magnetosomes.

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Section: Discussionmentioning

confidence: 99%

High‐Yield Production, Characterization, and Functionalization of Recombinant Magnetosomes in the Synthetic Bacterium Rhodospirillum rubrum “magneticum”

et al. 2021

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“…Their low potential makes this hypothesis attractive, since in the reduced form they could transfer electrons to either ferredoxin or ubiquinone, but to date there has been no definitive evidence for such a role. Isolated bacterial chromatophores do react with a number of artificial electron acceptors, however, including oxygen (75,114), quinones (133,134), methyl viologen (coupled to a disulfide as the final acceptor) (82), and methyl red (3). Cytochrome c as Donor for Reaction Center Bchl…”

Section: Ferredoxin Tron Camementioning

confidence: 99%

Photochemical and electron transport reactions of bacterial photosynthesis.

Vernon¹

1968

Bacteriological Reviews

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“…In the dark, the sulfate could first be activated to PAPS and then reduced via reduced pyridine nucleotides. In the light, the sulfate could be activated to adenosine 5'-phosphosulfate and reduced by the cytochrome c found in the chromatophore (Lindstrom, 1962). Once sulfate is reduced, it is extensively metabolized by apparently nonchromatophoral reactions.…”

Section: Data Inmentioning

confidence: 99%

METABOLISM OF SULFATE BY THE CHROMATOPHORE OF RHODOSPIRILLUM

Ibanez

Lindstrom

1962

J Bacteriol

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The chromatophore of Rhodospirillum rubrum was shown to possess enzymes for the activation and reduction of inorganic sulfate. The chromatophore was able to synthesize 3'-phosphoadenosine 5'-phosphosulfate (PAPS), using either exogenous adenosine triphosphate (ATP) or ATP synthesized via photophosphorylation. Light was required for the reduction of sulfate to a volatile form, presumably sulfite. Light enhanced the incorporation of sulfate-sulfur into cystine, cysteine, and cysteic acid of the chromatophore. This incorporation was probably the result of exchange reactions of reduced sulfur, not the result of net synthesis. The 100:1 ratio of the activation to reduction of sulfate and the inhibition of the reduction by exogenous ATP suggested that PAPS might not be the substrate for chromatophoral sulfate reduction. The bacterial chromatophore has been shown to mediate not only a number of photochemical reactions but also several dark reactions (Frenkel, 1959b). Two of the more physiologically significant photochemical reactions are the lightinduced esterification of phosphate (Frenkel, 1956) and the light-induced reduction of pyridine nucleotide (Frenkel, 1959a). Rhodospirillum rubrum is able to satisfy its sulfur requirement by assimilating inorganic sulfate either in the light or dark. As R. rubrum has been shown to reduce sulfate photochemically (Ibanez and Lindstrom, 1959), we wished to determine the relationship between the chromatophoral photometabolism

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Photooxidase Activity of Heated Chromatophores of Rhodospirillum rubrum

Cited by 8 publications

References 12 publications

High‐Yield Production, Characterization, and Functionalization of Recombinant Magnetosomes in the Synthetic Bacterium Rhodospirillum rubrum “magneticum”

High‐Yield Production, Characterization, and Functionalization of Recombinant Magnetosomes in the Synthetic Bacterium Rhodospirillum rubrum “magneticum”

Photochemical and electron transport reactions of bacterial photosynthesis.

METABOLISM OF SULFATE BY THE CHROMATOPHORE OF RHODOSPIRILLUM

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