Fluorescence Blinking of the RC–LH1 Complex from Rhodopseudomonas palustris

ChemPhysChem ◽  
2010 ◽  
Vol 12 (3) ◽  
pp. 711-716 ◽  
Author(s):  
Sarah Unterkofler ◽  
Tobias Pflock ◽  
June Southall ◽  
Richard J. Cogdell ◽  
Jürgen Köhler
Keyword(s):  
Rhodopseudomonas Palustris ◽  
Fluorescence Blinking

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.

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.

Sign in / Sign up

Export Citation Format

Share Document