Exemplar Abstract for Rhodopseudomonas palustris (Molisch 1907) van Niel 1944 (Approved Lists 1980) emend. Venkata Ramana et al. 2012.

2003 ◽  
Author(s):  
Charles Thomas Parker ◽  
Dorothea Taylor ◽  
George M Garrity
Keyword(s):  
Rhodopseudomonas Palustris

Enhancing the power generation of Rhodopseudomonas palustris-based MFC

2020 ◽  
Vol 64 (1-4) ◽  
pp. 1261-1268
Author(s):  
Shu Otani ◽  
Dang-Trang Nguyen ◽  
Kozo Taguchi
Keyword(s):  
Activated Carbon ◽  
Rhodopseudomonas Palustris ◽  
Ozone Treatment ◽  
Maximum Power Density ◽  
On Demand ◽  
Long Time ◽  
Dry Conditions ◽  
Carbon Sheet ◽  
Uv Ozone

In this study, a portable and disposable paper-based microbial fuel cell (MFC) was fabricated. The MFC was powered by Rhodopseudomonas palustris bacteria (R. palustris). An activated carbon sheet-based anode pre-loaded organic matter (starch) and R. palustris was used. By using starch in the anode, R. palustris-loaded on the anode could be preserved for a long time in dry conditions. The MFC could generate electricity on-demand activated by adding water to the anode. The activated carbon sheet anode was treated by UV-ozone treatment to remove impurities and to improve its hydrophilicity before being loaded with R. palustris. The developed MFC could generate the maximum power density of 0.9 μW/cm2 and could be preserved for long-term usage with little performance degradation (10% after four weeks).

scholarly journals Structures of Rhodopseudomonas palustris RC-LH1 complexes with open or closed quinone channels

2021 ◽  
Vol 7 (3) ◽  
pp. eabe2631
Author(s):  
David J. K. Swainsbury ◽  
Pu Qian ◽  
Philip J. Jackson ◽  
Kaitlyn M. Faries ◽  
Dariusz M. Niedzwiedzki ◽  
...  
Keyword(s):  
Binding Sites ◽  
Rhodopseudomonas Palustris ◽  
Ring Closure ◽  
Light Harvesting Complex ◽  
The Core ◽  
Quinone Binding ◽  
Cryo Electron Microscopy ◽  
Unique Protein ◽  
Center Light ◽  
Resolution Structure

The reaction-center light-harvesting complex 1 (RC-LH1) is the core photosynthetic component in purple phototrophic bacteria. We present two cryo–electron microscopy structures of RC-LH1 complexes from Rhodopseudomonas palustris. A 2.65-Å resolution structure of the RC-LH114-W complex consists of an open 14-subunit LH1 ring surrounding the RC interrupted by protein-W, whereas the complex without protein-W at 2.80-Å resolution comprises an RC completely encircled by a closed, 16-subunit LH1 ring. Comparison of these structures provides insights into quinone dynamics within RC-LH1 complexes, including a previously unidentified conformational change upon quinone binding at the RC QB site, and the locations of accessory quinone binding sites that aid their delivery to the RC. The structurally unique protein-W prevents LH1 ring closure, creating a channel for accelerated quinone/quinol exchange.

The degradation mechanisms of Rhodopseudomonas palustris toward hexabromocyclododecane by time-course transcriptome analysis

2021 ◽  
pp. 130489
Author(s):  
Yi-Jie Li ◽  
Reuben Wang ◽  
Chung-Yen Lin ◽  
Shu-Hwa Chen ◽  
Chia-Hsien Chuang ◽  
...  
Keyword(s):  
Transcriptome Analysis ◽  
Time Course ◽  
Rhodopseudomonas Palustris ◽  
Degradation Mechanisms

scholarly journals Spectroscopic evidence for direct flavin-flavin contact in a bifurcating electron transfer flavoprotein

2020 ◽  
Vol 295 (36) ◽  
pp. 12618-12634
Author(s):  
H. Diessel Duan ◽  
Nishya Mohamed-Raseek ◽  
Anne-Frances Miller
Keyword(s):  
Electron Transfer ◽  
Density Functional ◽  
Protein Denaturation ◽  
Rhodopseudomonas Palustris ◽  
Density Functional Theory Calculations ◽  
Site Directed Mutagenesis ◽  
Functional Theory ◽  
Electron Transfer Flavoprotein ◽  
Midpoint Potential ◽  
Ct Complex

A remarkable charge transfer (CT) band is described in the bifurcating electron transfer flavoprotein (Bf-ETF) from Rhodopseudomonas palustris (RpaETF). RpaETF contains two FADs that play contrasting roles in electron bifurcation. The Bf-FAD accepts electrons pairwise from NADH, directs one to a lower-reduction midpoint potential (E°) carrier, and the other to the higher-E° electron transfer FAD (ET-FAD). Previous work noted that a CT band at 726 nm formed when ET-FAD was reduced and Bf-FAD was oxidized, suggesting that both flavins participate. However, existing crystal structures place them too far apart to interact directly. We present biochemical experiments addressing this conundrum and elucidating the nature of this CT species. We observed that RpaETF missing either FAD lacked the 726 nm band. Site-directed mutagenesis near either FAD produced altered yields of the CT species, supporting involvement of both flavins. The residue substitutions did not alter the absorption maximum of the signal, ruling out contributions from residue orbitals. Instead, we propose that the residue identities modulate the population of a protein conformation that brings the ET-flavin and Bf-flavin into direct contact, explaining the 726 nm band based on a CT complex of reduced ET-FAD and oxidized Bf-FAD. This is corroborated by persistence of the 726 nm species during gentle protein denaturation and simple density functional theory calculations of flavin dimers. Although such a CT complex has been demonstrated for free flavins, this is the first observation of such, to our knowledge, in an enzyme. Thus, Bf-ETFs may optimize electron transfer efficiency by enabling direct flavin-flavin contact.

scholarly journals 1H, 13C and 15N assignment of the paramagnetic high potential iron–sulfur protein (HiPIP) PioC from Rhodopseudomonas palustris TIE-1

2020 ◽  
Vol 14 (2) ◽  
pp. 211-215 ◽  
Author(s):  
Inês B. Trindade ◽  
Michele Invernici ◽  
Francesca Cantini ◽  
Ricardo O. Louro ◽  
Mario Piccioli
Keyword(s):  
Rhodopseudomonas Palustris ◽  
High Potential ◽  
Iron Sulfur ◽  
Sulfur Protein ◽  
Iron Sulfur Protein
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