The light-harvesting complex II (B800-850) of<i>Rhodobacter sulfidophilus</i>: Characterization and formation under different growth conditions

Hagemann, Gesine E.; Gad’on, Nasser; García, Augusto F.; Drews, Gerhart; Tadros, Monier H.

doi:10.1111/j.1574-6968.1995.tb07382.x

Cited by 10 publications

(2 citation statements)

References 9 publications

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“…sulfidophilus exhibits a blue-shift of the long wavelength absorbance maximum from 800-850 to 800-826 rim. This blue-shifted form is fully reversible upon addition of salts [16,17,19]. Currently, there are a number of complexes known to show considerable blue-shift of the absorption maximum as a result of modifications of the pigment binding proteins through site-directed mutagenesis [26,27], detergent treatments [28], or salt treatment [29].…”

Section: Discussionmentioning

confidence: 99%

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Isolation and complete amino acid sequence of the β‐ and α‐polypeptides from the peripheral light‐harvesting pigment‐protein complex II of Rhodobacter sulfidophilus

et al. 1995

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The peripheral light-harvesting bacteriochlorophyilcarotenoid-protein complex B800-850 (LHII) has been isolated from membranes of semi-aerobic dark-grown cells of Rhodobacter sulfidophilus strain W4. A reversed-phase HPLC system resolved one j3-and one a-polypeptide in the ratio 1 : 1. The material obtained was of high purity and suitable for direct microsequence analysis. The primary structures of the/3-and apolypeptides have been determined. The/]-polypeptide consists of 51 amino acid residues, yielding a molecular mass of 5512 Da and having 64.7% hydrophobicity. The a-polypeptide consists of 52 amino acid residues, with a calculated molecular mass of 5661 Da and 75% hydrophobicity. The significance of uncommon structure motives with respect to the unusual spectroscopic characteristics of this light-harvesting complex is discussed.

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Section: Discussionmentioning

confidence: 99%

“…sulfidophilus strain W4 as described by Hagemann et al [19]. The LHII complex was isolated and purified as described by Doi et al [16] with small modifications as described by Hagemann et al [19] …”

Section: Growth Of Bacteria Membrane Isolation and Purification Of Tmentioning

confidence: 99%

Isolation and complete amino acid sequence of the β‐ and α‐polypeptides from the peripheral light‐harvesting pigment‐protein complex II of Rhodobacter sulfidophilus

et al. 1995

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Oxygen intervention in the regulation of gene expression: the photosynthetic bacterial paradigm

Zeilstra-Ryalls

Kaplan²

2004

Cellular and Molecular Life Sciences (CMLS)

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The means by which oxygen intervenes in gene expression has been examined in considerable detail in the metabolically versatile bacterium Rhodobacter sphaeroides. Three regulatory systems are now known in this organism, which are used singly and in combination to modulate genes in response to changing oxygen availability. The outcome of these regulatory events is that the molecular machinery is present for the cell to obtain energy by means that are best suited to prevailing conditions, while at the same time maintaining cellular redox balance. Here, we explore the dangers associated with molecular oxygen relative to the various metabolisms used by R. sphaeroides, and then present the most recent findings regarding the features and operation of each of the three regulatory systems which collectively mediate oxygen control in this organism.

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Characterization of a mutant strain of Rhodovulum sulfidophilum lacking the pufA and pufB genes encoding the polypeptides for the light-harvesting complex 1 (B 870)

et al. 2006

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Contradictory results on the effectiveness of energy transfer from the light harvesting complex 2 (LH2) directly to the reaction center (RC) in mutant strains lacking the core light-harvesting complex 1 (LH1) have been obtained with cells of Rhodobacter capsulatus and Rhodobacter sphaeroides. A LH1(-) mutant of Rhodovulum sulfidophilum, named rsLRI, was constructed by deletion of the pufBA genes, resulting in a kanamycin resistant photosynthetically positive clone. To restore the wild type phenotype, a complemented strain C2 was constructed by inserting in trans a DNA segment containing the pufBA genes. Light-induced FTIR difference spectra indicate that the RC in the rsLRI mutant and in the C2 complemented strains are functionally and structurally identical with those in the wild type strain, demonstrating that the assembly and the function of the RC is not impaired by the LH1 deletion. The photosynthetic growth rate of the rsLRI strain increased with decreasing light intensity. At 50 W m(-2 )no photosynthetic growth was observed. These results indicate that the light energy harvested by the LH2 complex was not or inefficiently transferred to the RC; thus most of the energy necessary for photosynthetic growth is in the LH1(-) strain directly absorbed by the RC. It is supposed that in the mutant strain, RC and LH2 cannot interact in an efficient way.

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The light-harvesting complex II (B800-850) ofRhodobacter sulfidophilus: Characterization and formation under different growth conditions

Cited by 10 publications

References 9 publications

Isolation and complete amino acid sequence of the β‐ and α‐polypeptides from the peripheral light‐harvesting pigment‐protein complex II of Rhodobacter sulfidophilus

Isolation and complete amino acid sequence of the β‐ and α‐polypeptides from the peripheral light‐harvesting pigment‐protein complex II of Rhodobacter sulfidophilus

Oxygen intervention in the regulation of gene expression: the photosynthetic bacterial paradigm

Characterization of a mutant strain of Rhodovulum sulfidophilum lacking the pufA and pufB genes encoding the polypeptides for the light-harvesting complex 1 (B 870)

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