Results 211 to 220 of about 12,726,180 (242)

Isolation, Characterization, and Comparison of a Ubiquitous Pigment-Protein Complex Consisting of a Reaction Center and Light-Harvesting Bacteriochlorophyll Proteins Present in Purple Photosynthetic Bacteria1

The Journal of Biochemistry, 1985
Protein complexes (photochemical reaction complex; PR complex) bound to both light-harvesting bacteriochlorophyll-1 (LH-Bchl-1) and reaction center Bchl (RC-Bchl) were purified from Rhodospirillum rubrum (wild and carotenoid-less), Rhodopseudomonas sphaeroides (wild), and Chromatium vinosum (wild).
Tetsuya UEDA, Yukio MORIMOTO, Mamoru SATO, Tomisaburo KAKUNO, Jinpei YAMASHITA, Takekazu HORIO   +5 more
openaire   +2 more sources

Gene duplication and the evolution of photosynthetic reaction center proteins [PDF]

FEBS Letters, 1996
We investigate the evolutionary relationships between photosynthetic reaction center proteins (D1, D2, L and M) and demonstrate that the pattern of nucleotide substitution in these is more complicated than has been assumed in previous phylogenetic ...
Anthony Larkum, P J Lockhart, A W Larkum   +2 more
exaly   +2 more sources

Isolation and properties of a pigment-protein complex associated with the reaction center of the green photosynthetic sulfur bacterium Prosthecochloris aestuarii

Biochimica et Biophysica Acta (BBA) - Bioenergetics, 1983
Abstract The membrane-bound pigment system of green sulfur bacteria consists of light-harvesting bacteriochlorophyll a -protein and a ‘core complex’ that is associated with the reaction center (Kramer, H.J.M., Kingma, H., Swarthoff, T. and Amesz, J. (1982) Biochim. Biophys. Acta 681, 359–364).
Henk Vasmel, Ton Swarthoff, Herman J.M. Kramer, Jan Amesz   +3 more
openaire   +1 more source

Towards a New Taxonomy of Photosynthetic Bacteria: ADMR‐Monitored Triplet Difference Spectroscopy of Reaction Center Pigment–Protein Complexes

Israel Journal of Chemistry, 1988
AbstractLow‐temperature (1.2 K) triplet‐minus‐singlet absorbance difference spectra of a number of photosynthetic bacteria, including members of almost all genera with the exception of Heliobacteriaceae, have been recorded by absorbance‐detected magnetic resonance (ADMR). The spectra of the purple bacteria fall into two distinct classes.
J. Antonie Dijkman, Hubert J. Den Blanken, Arnold J. Hoff   +2 more
openaire   +1 more source

Enhanced Photocurrent Generation by Photosynthetic Bacterial Reaction Centers through Molecular Relays, Light-Harvesting Complexes, and Direct Protein–Gold Interactions

Langmuir, 2011
The utilization of proteins as nanodevices for solar cells, bioelectronics, and sensors generally necessitates the transfer of electrons to or from a conducting material. Here we report on efforts to maximize photocurrent generation by bacterial photosynthetic reaction center pigment-protein complexes (RCs) interfaced with a metal electrode.
den Hollander, M-J, Magis, J.G, Fuchsenberger, P, Aartsma, T.J, Jones, M.R, Frese, R.N   +5 more
openaire   +4 more sources

High-Potential Iron−Sulfur Protein (HiPIP) Is the Major Electron Donor to the Reaction Center Complex in Photosynthetically Growing Cells of the Purple Bacterium Rubrivivax gelatinosus

Biochemistry, 2002
A gene encoding the high-potential iron-sulfur protein (HiPIP) was cloned from the purple photosynthetic bacterium Rubrivivax gelatinosus. An insertional disruption of this gene by a kanamycin resistance cartridge resulted in a significant decrease in the growth rate under photosynthetic growth conditions. Flash-induced kinetic measurements showed that
Kenji V P, Nagashima, Katsumi, Matsuura, Keizo, Shimada, André, Verméglio   +3 more
openaire   +2 more sources

Solution structure of a biological bimolecular electron transfer complex: characterization of the photosynthetic reaction center-cytochrome c₂ protein complex by small angle neutron scattering

Journal of Applied Crystallography, 2000
The structures of kinetically distinct electron transfer complexes formed between the photosynthetic reaction center from Rhodobacter sphaeroides R-26, and a water-soluble cytochrome c2 were characterized using small angle neutron scattering, SANS.
D. M. Tiede, K. Littrell, P. A. Marone, R. Zhang, P. Thiyagarajan   +4 more
openaire   +1 more source

Cytochromes, Iron-Sulfur, and Copper Proteins Mediating Electron Transfer from the Cyt bc1 Complex to Photosynthetic Reaction Center Complexes

2006
Electron transfer between the photosynthetic reaction center and the cytochrome bc1 complexes is often mediated by a high redox potential soluble cytochrome. In purple non-sulfur bacteria, this electron donor is usually cytochrome c2 (Cyt c2), while cyanobacteria and green algae can use the distantly related cytochrome c6 protein.
T. E. Meyer, Timothy J. Donohue
openaire   +1 more source

Role of the PufX protein in photosynthetic growth of Rhodobacter sphaeroides. 2. PufX is required for efficient ubiquinone/ubiquinol exchange between the reaction center QB site and the cytochrome bc1 complex.

Biochemistry, 1995
The PufX membrane protein is essential for photosynthetic growth of Rhodobacter sphaeroides because it is required for multiple-turnover electron transfer under anaerobic conditions [see accompanying article; Barz, W. P., Francia, F., Venturoli, G., Melandri, B. A., Verméglio, A., & Oesterhelt, D. (1995) Biochemistry 34, 15235-15247].
W P, Barz, A, Verméglio, F, Francia, G, Venturoli, B A, Melandri, D, Oesterhelt   +5 more
openaire   +2 more sources

Chemical nature of protein complex of photoreaction unit including reaction center in chromatophores of photosynthetic bacterium, Rhodospirillum rubrum, as detected by successive dissociation method.

Journal of biochemistry, 1984
Reaction center of chromatophores of Rhodospirillum rubrum consists of three kinds of protein, H-, M-, and L-subunit, and is bound with many other kinds of protein to form a larger protein complex (PRU; photoreaction unit), which contains all the bacteriochlorophyll.
K, Tanaka, T, Kakuno, J, Yamashita, T, Horio   +3 more
openaire   +1 more source