Electron transfer dynamics and enhanced H2 production activity of hydrangea-like BiOBr/Bi2S3-based photocatalysts with Cu-complex as a redox mediator

2021 ◽  
pp. 151870
Author(s):  
Chi-Jung Chang ◽  
Chieh-Lin Huang ◽  
Yuan-Hsiang Yu ◽  
Ming-Chun Teng ◽  
Chao-Lung Chiang ◽  
...  
2014 ◽  
Vol 4 (10) ◽  
pp. 1301925 ◽  
Author(s):  
Jun Zhang ◽  
Lifang Qi ◽  
Jingrun Ran ◽  
Jiaguo Yu ◽  
Shi Zhang Qiao

Author(s):  
Osamu Tomita ◽  
Hiroki Naito ◽  
Akinobu Nakada ◽  
Masanobu Higashi ◽  
Ryu Abe

Because the majority of Z-scheme water splitting systems employ a shuttle redox mediator that allows electron transfer between two photocatalyst materials, the development of an effective redox mediator is crucial...


2021 ◽  
Author(s):  
Weerapong Bootluck ◽  
Thawat Chittrakarn ◽  
Kuaanan Techato ◽  
Panitan Jutaporn ◽  
Watsa Khongnakorn

2021 ◽  
Author(s):  
Jae Kyu Lim ◽  
Ji-In Yang ◽  
Yun Jae Kim ◽  
Yeong-Jun Park ◽  
Yong Hwan Kim

Abstract Ferredoxin-dependent metabolic engineering of electron transfer circuits has been developed to enhance redox efficiency in the field of synthetic biology, e.g., for hydrogen production and for reduction of flavoproteins or NAD(P)+. Here, we present the bioconversion of carbon monoxide (CO) gas to formate via a synthetic CO:formate oxidoreductase (CFOR), designed as an enzyme complex for direct electron transfer between noninteracting CO dehydrogenase and formate dehydrogenase using an electron-transferring Fe-S fusion protein. The CFOR-introduced Thermococcus onnurineus mutant strains showed CO-dependent formate production in vivo and in vitro. The formate production rate from purified CFOR complex and specific formate productivity from the bioreactor were 348 ± 34 μmol/mg/min and 90.2 ± 20.4 mmol/g-cells/h, respectively. The CO-dependent CO2 reduction/formate production activity of synthetic CFOR was confirmed, indicating that direct electron transfer between two unrelated dehydrogenases was feasible via mediation of the FeS-FeS fusion protein.


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