electron transfer pathway
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2022 ◽  
Author(s):  
Olga Mazuryk ◽  
Ewelina Janczy-Cempa ◽  
Justyna Lagosz ◽  
Dorota Rutkowska-Zbik ◽  
Agata Machnicka ◽  
...  

The purpose of this study was to investigate a correlation between the spectroscopic and photophysical properties of Ru(II) polypyridyl complexes and their photodynamic activity in vitro. A series of Ru(II)...


2021 ◽  
Author(s):  
James Birrell ◽  
Chris Furlan ◽  
Nipa Chongdar ◽  
Pooja Gupta ◽  
Wolfgang Lubitz ◽  
...  

Abstract Electron-bifurcation is a fundamental energy conservation mechanism in nature. The electron-bifurcating [FeFe] hydrogenase from Thermotoga maritima (HydABC) requires both NADH and ferredoxin to reduce protons generating hydrogen. The mechanism of electron-bifurcation in HydABC remains enigmatic primarily due to the lack of structural information. Here, we present a 2.3 Å electron cryo-microscopy structure of HydABC. The structure is a heterododecamer composed of two independent ‘halves’ each made of two strongly interacting HydABC heterotrimers electrically connected via a [4Fe-4S] cluster. A central electron transfer pathway connects the active sites for NADH oxidation and proton reduction. Symmetry expansion identified two conformations of a flexible iron-sulfur cluster domain: a “closed bridge” and an “open bridge” conformation, where a Zn2+ site may act as a “hinge” allowing domain movement. Based on these structural revelations, we propose two new mechanisms of electron-bifurcation in HydABC.


PLoS ONE ◽  
2021 ◽  
Vol 16 (11) ◽  
pp. e0258380
Author(s):  
Moshe Baruch ◽  
Sara Tejedor-Sanz ◽  
Lin Su ◽  
Caroline M. Ajo-Franklin

Microorganisms regulate the redox state of different biomolecules to precisely control biological processes. These processes can be modulated by electrochemically coupling intracellular biomolecules to an external electrode, but current approaches afford only limited control and specificity. Here we describe specific electrochemical control of the reduction of intracellular biomolecules in Escherichia coli through introduction of a heterologous electron transfer pathway. E. coli expressing cymAmtrCAB from Shewanella oneidensis MR-1 consumed electrons directly from a cathode when fumarate or nitrate, both intracellular electron acceptors, were present. The fumarate-triggered current consumption occurred only when fumarate reductase was present, indicating all the electrons passed through this enzyme. Moreover, CymAMtrCAB-expressing E. coli used current to stoichiometrically reduce nitrate. Thus, our work introduces a modular genetic tool to reduce a specific intracellular redox molecule with an electrode, opening the possibility of electronically controlling biological processes such as biosynthesis and growth in any microorganism.


2021 ◽  
Vol 8 (1) ◽  
Author(s):  
Zhan Song ◽  
Cancan Wei ◽  
Chao Li ◽  
Xin Gao ◽  
Shuhong Mao ◽  
...  

AbstractFerredoxin (Fdx) is regarded as the main electron carrier in biological electron transfer and acts as an electron donor in metabolic pathways of many organisms. Here, we screened a self-sufficient P450-derived reductase PRF with promising production yield of 9OHAD (9α-hydroxy4-androstene-3,17-dione) from AD, and further proved the importance of [2Fe–2S] clusters of ferredoxin-oxidoreductase in transferring electrons in steroidal conversion. The results of truncated Fdx domain in all oxidoreductases and mutagenesis data elucidated the indispensable role of [2Fe–2S] clusters in the electron transfer process. By adding the independent plant-type Fdx to the reaction system, the AD (4-androstene-3,17-dione) conversion rate have been significantly improved. A novel efficient electron transfer pathway of PRF + Fdx + KshA (KshA, Rieske-type oxygenase of 3-ketosteroid-9-hydroxylase) in the reaction system rather than KshAB complex system was proposed based on analysis of protein–protein interactions and redox potential measurement. Adding free Fdx created a new conduit for electrons to travel from reductase to oxygenase. This electron transfer pathway provides new insight for the development of efficient exogenous Fdx as an electron carrier. Graphical Abstract


2021 ◽  
Author(s):  
Lei Luo ◽  
Lei Fu ◽  
Huifen Liu ◽  
Youxun Xu ◽  
Jialiang Xing ◽  
...  

Abstract Methane (CH4) oxidation to high value chemicals under mild conditions through photocatalysis is a sustainable and appealing pathway, nevertheless confronting the critical issues on both conversion and selectivity. Herein, under visible irradiation (420 nm), the synergy of palladium (Pd) atom cocatalyst and oxygen vacancies (OVs) on In2O3 nanorods enabled superior photocatalytic CH4 activation by O2. The optimised catalyst reached ca. 100 µmol·h− 1 of C1 oxygenates, with a selectivity of primary products (CH3OH and CH3OOH) up to 82.5 %. Mechanism investigation elucidated that such superior photocatalysis was induced by the dedicated function of Pd single atoms and oxygen vacancies on boosting hole and electron transfer pathway, respectively. O2 was proven to be the only oxygen source for CH3OH production, while H2O acted as the promoter for efficient CH4 activation through ·OH production and facilitated product desorption as indicated by DFT modelling. This work thus provides new understandings on simultaneous regulation of activity and selectivity by the significant synergy of single atom cocatalysts and oxygen vacancies.


Author(s):  
Zhan Song ◽  
Cancan Wei ◽  
Chao Li ◽  
Xin Gao ◽  
Shuhong Mao ◽  
...  

Ferredoxin (Fdx) is regarded as the main electron carrier in biological electron transfer and acts as an electron donor in metabolic pathways of many organisms. Here, we screened a self-sufficient P450-derived reductase PRF with promising NADPH reduction activity and 9OHAD production yield and proved the importance of [2Fe-2S] clusters of Fdx-containing oxidoreductase in transferring electrons in steroidal conversion. The truncated Fdx domain in all oxidoreductases, together with mutagenesis data, further elucidated the indispensable role of [2Fe-2S] clusters in the electron transfer process. By adding the independent plant-type Fdx to the reaction system, the AD conversion rate have been significantly improved. A novel efficient electron transfer pathway of PRF+Fdx+KshA in the reaction system rather than KshAB complex system was proposed based on analysis of protein-protein interactions and redox potential measurement. Adding free Fdx created a new conduit for electrons to travel from reductase to oxygenase. This electron transfer pathway provides new insight for the development of efficient exogenous Fdx as an electron carrier.


2021 ◽  
Vol 12 ◽  
Author(s):  
Samuel E. H. Piper ◽  
Marcus J. Edwards ◽  
Jessica H. van Wonderen ◽  
Carla Casadevall ◽  
Anne Martel ◽  
...  

Shewanella oneidensis exchanges electrons between cellular metabolism and external redox partners in a process that attracts much attention for production of green electricity (microbial fuel cells) and chemicals (microbial electrosynthesis). A critical component of this pathway is the outer membrane spanning MTR complex, a biomolecular wire formed of the MtrA, MtrB, and MtrC proteins. MtrA and MtrC are decaheme cytochromes that form a chain of close-packed hemes to define an electron transfer pathway of 185 Å. MtrA is wrapped inside MtrB for solubility across the outer membrane lipid bilayer; MtrC sits outside the cell for electron exchange with external redox partners. Here, we demonstrate tight and spontaneous in vitro association of MtrAB with separately purified MtrC. The resulting complex is comparable with the MTR complex naturally assembled by Shewanella in terms of both its structure and rates of electron transfer across a lipid bilayer. Our findings reveal the potential for building bespoke electron conduits where MtrAB combines with chemically modified MtrC, in this case, labeled with a Ru-dye that enables light-triggered electron injection into the MtrC heme chain.


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