Results 221 to 230 of about 26,899 (249)
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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 +5 more
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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 +5 more
openaire +4 more sources
Biochimica Et Biophysica Acta - Bioenergetics, 2020 Precise folding of photosynthetic proteins and organization of multicomponent assemblies to form functional entities are fundamental to efficient photosynthetic electron transfer. The bacteriochlorophyll b-producing purple bacterium Blastochloris viridis
Daniel P Canniffe, , Lu-Ning Liu
exaly +2 more sources
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 +3 more
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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 +3 more
openaire +2 more sources
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 +4 more
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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 +4 more
openaire +1 more source
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
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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
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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 +5 more
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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 +5 more
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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 +3 more
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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 +3 more
openaire +1 more source
Journal of molecular biology, 1984
X-ray analysis of three-dimensional crystals of the photosynthetic reaction center from the purple bacterium Rhodopseudomonas viridis led to an electron density distribution at 3 A resolution calculated with phases from multiple isomorphous replacement. The protein subunits of the complex were identified. An atomic model of the prosthetic groups of the
Deisenhofer, J. +4 more
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X-ray analysis of three-dimensional crystals of the photosynthetic reaction center from the purple bacterium Rhodopseudomonas viridis led to an electron density distribution at 3 A resolution calculated with phases from multiple isomorphous replacement. The protein subunits of the complex were identified. An atomic model of the prosthetic groups of the
Deisenhofer, J. +4 more
openaire +2 more sources