scholarly journals Use of Purple Non-Sulfur Photosynthetic Bacteria (Rhodobacter sphaeroides) in Promoting Ciliated Protozoa Growth

2020 ◽  
Vol 25 (2) ◽  
pp. 81-89
Author(s):  
ISLAM TEIBA ◽  
SUGURU OKUNISHI ◽  
TAKESHI YOSHIKAWA ◽  
MAKOTO IKENAGA ◽  
MOHAMMED FOUAD EL BASUINI ◽  
...  
Keyword(s):  
Rhodobacter Sphaeroides ◽  
Photosynthetic Bacteria ◽  
Ciliated Protozoa

scholarly journals Biosynthesis of pinene in purple non-sulfur photosynthetic bacteria

2021 ◽  
Vol 20 (1) ◽  
Author(s):  
Xiaomin Wu ◽  
Guang Ma ◽  
Chuanyang Liu ◽  
Xin-yuan Qiu ◽  
Lu Min ◽  
...  
Keyword(s):  
Fusion Protein ◽  
Heterologous Expression ◽  
Rhodobacter Sphaeroides ◽  
Photosynthetic Bacteria ◽  
Fine Chemicals ◽  
Isopentenyl Diphosphate ◽  
Isopentenyl Diphosphate Isomerase ◽  
Geranyl Diphosphate ◽  
Ribosome Binding ◽  
Geranyl Diphosphate Synthase

Abstract Background Pinene is a monoterpene, that is used in the manufacture of fragrances, insecticide, fine chemicals, and renewable fuels. Production of pinene by metabolic-engineered microorganisms is a sustainable method. Purple non-sulfur photosynthetic bacteria belong to photosynthetic chassis that are widely used to synthesize natural chemicals. To date, researches on the synthesis of pinene by purple non-sulfur photosynthetic bacteria has not been reported, leaving the potential of purple non-sulfur photosynthetic bacteria synthesizing pinene unexplored. Results Rhodobacter sphaeroides strain was applied as a model and engineered to express the fusion protein of heterologous geranyl diphosphate synthase (GPPS) and pinene synthase (PS), hence achieving pinene production. The reaction condition of pinene production was optimized and 97.51 μg/L of pinene was yielded. Then, genes of 1-deoxy-d-xylulose 5-phosphate synthase, 1-deoxy-d-xylulose 5-phosphate reductoisomerase and isopentenyl diphosphate isomerase were overexpressed, and the ribosome binding site of GPPS-PS mRNA was optimized, improving pinene titer to 539.84 μg/L. Conclusions In this paper, through heterologous expression of GPPS-PS, pinene was successfully produced in R. sphaeroides, and pinene production was greatly improved by optimizing the expression of key enzymes. This is the first report on pinene produce by purple non-sulfur photosynthetic bacteria, which expands the availability of photosynthetic chassis for pinene production.

Rhodobacter sphaeroides has a family II pyrophosphatase: comparison with other species of photosynthetic bacteria

2003 ◽  
Vol 179 (5) ◽  
pp. 368-376 ◽  
Author(s):  
Heliodoro Celis ◽  
Bernardo Franco ◽  
Silvia Escobedo ◽  
Irma Romero
Keyword(s):  
Rhodobacter Sphaeroides ◽  
Photosynthetic Bacteria

Hypersensitivity of Rhodobacter sphaeroides ribosomes to protein synthesis inhibitors: structural and functional implications

1994 ◽  
Vol 40 (9) ◽  
pp. 699-704 ◽  
Author(s):  
E. Sánchez ◽  
J. Teixidó ◽  
R. Guerrero ◽  
R. Amils
Keyword(s):  
Escherichia Coli ◽  
Protein Synthesis ◽  
Rhodobacter Sphaeroides ◽  
Photosynthetic Bacteria ◽  
Protein Synthesis Inhibitors ◽  
Chemical Structures ◽  
Elongation Cycle ◽  
Functional Differences ◽  
Functional Implications ◽  
Ribosomal Function

The elongation cycle of protein synthesis systems of purple nonsulfur photosynthetic bacteria Rhodobacter sphaeroides, grown both phototrophically and chemotrophically, was studied using 33 inhibitors with different chemical structures and functional and domain specificities. No functional differences between phototrophic and chemotrophic ribosomal systems were detected. Rhodobacter sphaeroides ribosomes exhibited strong hypersensitivity to nine functional inhibitors when compared with Escherichia coli ribosomes. Most of the R. sphaeroides ribosomal hypersensitivities corresponded to peptidyltransferase inhibitors, implying that this important functional neighborhood must be somehow different in the two organisms.Key words: protein synthesis inhibitors, ribosomal function, peptidyltransferase, photosynthetic bacteria.

Nondestructive Structural Analysis of Photosynthetic Pigments in Living Rhodobacter Sphaeroides Mutants by Near-Infrared Fourier Transform Raman Spectroscopy

1992 ◽  
Vol 46 (3) ◽  
pp. 518-523 ◽  
Author(s):  
K. Okada ◽  
E. Nishizawa ◽  
Y. Fujimoto ◽  
Y. Koyama ◽  
S. Muraishi ◽  
...  
Keyword(s):  
Fourier Transform ◽  
Rhodobacter Sphaeroides ◽  
Photosynthetic Pigments ◽  
Photosynthetic Bacteria ◽  
Near Infrared ◽  
Living Cells ◽  
Electronic Transitions ◽  
Fourier Transform Raman Spectroscopy ◽  
Fourier Transform Raman

The 1064-nm excited Fourier transform Raman spectra have been measured for two kinds of whole living cells of photosynthetic bacteria, Rhodobacter sphaeroides G1C and R26 mutants, to investigate in situ structures of photosynthetic pigments, bacteriochlorophyll- a (BChl- a) and neurosporene (the only carotenoid included in the G1C mutant). The 1064-nm excited spectra consist of contributions from both neurosporene and BChl- a in the light harvesting (LH) complexes (G1C) or from BChl- a alone in the LH complexes (R26). The pattern of the 1064-nm excited spectrum of BChl- a in the LH complexes, whose Raman bands are pre-resonance enhanced via its Qy band, is dramatically different from that of its 355-nm excited spectrum, whose Raman bands are resonance enhanced via the B bands; for example, a band at 1606 cm−1 due to a Ca=Cm stretching mode of BChl- a, which is the most intense in the 355-nm excited spectrum, is barely observed in the 1064-nm excited spectrum. The frequency of the above band indicates that BChl- a in the LH complexes is five-coordinate. Bands due to C=O stretching modes of the 9-keto and 2-acetyl groups of BChl- a appear clearly near 1665 and 1640 cm−1, respectively, in the 1064-nm excited spectra. The frequencies of these C=O stretching bands suggest that most of the 9-keto and 2-acetyl groups of BChl- a in the complexes are involved in intermolecular interaction with the proteins. Bands assignable to Ca=N and Ca=Cb stretching modes, which are, in general, very weak in the 355-nm excited spectra, appear strongly in the 1064-nm excited spectra, implying that their bond lengths are changed sizably in the electronic transitions corresponding to the Qy bands.

scholarly journals CHARACTERIZATION OF DIMETHYLSULFOXIDE REDUCTASE, A NOVEL MOLYBDO-ENZYME FROM PHOTOSYNTHETIC BACTERIA, Rhodobacter sphaeroides f.s. denitrificans

1991 ◽  
Vol 7 (Supple) ◽  
pp. 821-824
Author(s):  
SUNAO YAMAZAKI ◽  
NAOYUKI KOBAYASHI ◽  
AKIRA OKUBO ◽  
TOSHIO SATO ◽  
YUZURU TOZAWA ◽  
...  
Keyword(s):  
Rhodobacter Sphaeroides ◽  
Photosynthetic Bacteria ◽  
Dimethylsulfoxide Reductase

scholarly journals Biosynthesis of Pinene in Purple Non-Sulfur Photosynthetic Bacteria

2021 ◽  
Author(s):  
Xiaomin Wu ◽  
Guang Ma ◽  
Chuanyang Liu ◽  
Xin-yuan Qiu ◽  
Lu Min ◽  
...  
Keyword(s):  
Fusion Protein ◽  
Heterologous Expression ◽  
Rhodobacter Sphaeroides ◽  
Photosynthetic Bacteria ◽  
Fine Chemicals ◽  
Isopentenyl Diphosphate ◽  
Isopentenyl Diphosphate Isomerase ◽  
Geranyl Diphosphate ◽  
Ribosome Binding ◽  
Geranyl Diphosphate Synthase

Abstract Background: Pinene is a monoterpene, that is used in the manufacture of fragrances, insecticide, fine chemicals, and renewable fuels. Production of pinene by metabolic-engineered microorganisms is a sustainable method. Purple non-sulfur photosynthetic bacteria belong to photosynthetic chassis that are widely used to synthesize natural chemicals. To date, researches on the synthesis of pinene by purple non-sulfur photosynthetic bacteria has not been reported, leaving the potential of purple non-sulfur photosynthetic bacteria synthesizing pinene unexplored. Results: Rhodobacter sphaeroides strain was applied as a model and engineered to express the fusion protein of heterologous geranyl diphosphate synthase (GPPS) and pinene synthase (PS), hence achieving pinene production. The reaction condition of pinene production was optimized and 97.51 μg/L of pinene was yielded. Then, genes of 1-deoxy-D-xylulose 5-phosphate synthase, 1-deoxy-D-xylulose 5-phosphate reductoisomerase and isopentenyl diphosphate isomerase were overexpressed, and the ribosome binding site of GPPS-PS mRNA was optimized, improving pinene titer to 539.84 μg/L. Conclusions: In this paper, through heterologous expression of GPPS-PS, pinene was successfully produced in R. sphaeroides, and pinene production was greatly improved by optimizing the expression of key enzymes. This is the first report on pinene produce by purple non-sulfur photosynthetic bacteria, which expands the availability of photosynthetic chassis for pinene production.

The petite purple photosynthetic powerpack

2009 ◽  
Vol 37 (2) ◽  
pp. 400-407 ◽  
Author(s):  
Michael R. Jones
Keyword(s):  
Biological Activity ◽  
Rhodobacter Sphaeroides ◽  
Molecular Basis ◽  
Photosynthetic Bacteria ◽  
Genetic Manipulation ◽  
Proton Translocation ◽  
Structural Studies ◽  
Light Harvesting Complexes ◽  
Purple Photosynthetic Bacteria ◽  
Solar Batteries

Photoreaction centres are Nature's solar batteries. These nanometre-scale power producers are responsible for transducing the energy of sunlight into a form that can be used by biological systems, thereby powering most of the biological activity on the planet. Although to the layman the word ‘photosynthesis’ is usually associated with green plants, much of our understanding of the molecular basis of biological transduction of light energy has come from studies of purple photosynthetic bacteria. Their RCs (reaction centres) and attendant light-harvesting complexes have been subjected to an intensive spectroscopic scrutiny, coupled with genetic manipulation and structural studies, that has revealed many of the molecular and mechanistic details of biological energy transfer, electron transfer and coupled proton translocation. This review provides a short overview of the structure and mechanism of the purple bacterial RC, focusing in the main on the most heavily studied complex from Rhodobacter sphaeroides.

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