Research
·
2021
·
IF 0
Yuqing Cheng,Jiafu Shi,Yizhou Wu,Xueying Wang,Yiying Sun,Ziyi Cai,Yu Chen,Zhongyi Jiang
Solar-driven photocatalytic regeneration of cofactors, including reduced nicotinamide adenine dinucleotide (NADH), reduced nicotinamide adenine dinucleotide phosphate (NADPH), and reduced flavin adenine dinucleotide (FADH2), could ensure the sustainable energy supply of enzymatic reactions catalyzed by oxidoreductases for the efficient synthesis of chemicals. However, the elevation of cofactor regeneration efficiency is severely hindered by the inefficient utilization of electrons transferred on the surface of photocatalysts. Inspired by the phenomenon of ferredoxin-NADP+ reductase (FNR) anchoring on thylakoid membrane, herein, a homogeneous catalyst of rhodium (Rh) complex, [Cp∗Rh(bpy)H2O]2+, was anchored on polymeric carbon nitride (PCN) mediated by a tannic acid/polyethyleneimine (TA/PEI) adhesive layer, acquiring PCN@TA/PEI-Rh core@shell photocatalyst. Illuminated by visible light, electrons were excited from the PCN core, then transferred through the TA/PEI shell, and finally captured by the surface-anchored Rh for instant utilization during the regeneration of NADH. The TA/PEI-Rh shell could facilitate the electron transfer from the PCN core and, more importantly, achieved ~1.3-fold elevation of electron utilization efficiency compared with PCN. Accordingly, the PCN@TA/PEI-Rh afforded the NADH regeneration efficiency of 37.8% after 20 min reaction under LED light (405 nm) illumination, over 1.5 times higher than PCN with free Rh. Coupling of the NADH regeneration system with formate dehydrogenase achieved continuous production of formate from carbon dioxide (CO2). Our study may provide a generic and effective strategy to elevate the catalytic efficiency of a photocatalyst through intensifying the electron utilization.
研究领域:
生物化学
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光催化材料科学
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DOI
BIOSCIENCE REPORTS
·
2016
·Vol. 36
·期 6
·
IF 2.446
Yan Mingguang,Yin Weibing,Fang Xiao,Guo Jianjun,Shi Hong
NADH oxidases (NOXs) catalysing the oxidation of NADH to yield NAD+ and H2O, H2O2, or both play an important role in protecting organisms from oxidative stress and maintaining the balance of NAD+/NADH. A gene encoding NOX was identified from Methanobrevibacter smithii (NOX-ms), the predominant archaeon in the human gut ecosystem. Subsequent analyses showed that it is an FAD-containing protein with a subunit molecular mass of 48 kDa. NOX-ms was purified to homogeneity after expression in Escherichia coli. NOX-ms catalysed the oxidization of NADH and converted O2 to H2O with an optimal pH of 7.5 and a temperature optimum of approximately 37°C. The Vmax and Km values were 42.6–44.1 unit/mg and 47.8–54.6 μM for NADH. The apparent Vmax and Km for oxygen were 189.5–196.1 unit/mg and 14.6–16.8 μM. The mutation analysis suggests that Cys42 in NOX-ms plays a key role in the four-electron reduction of O2 to H2O. Quantitative reverse transcription-PCR (RT-qPCR) revealed that transcription of NOX-ms was also up-regulated after exposing the cells to oxidative stress and glucose. Finally, the potential of NOX-ms as a target to control colonization of M. smithii and its possible applications are discussed.
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ANALYTICAL AND BIOANALYTICAL CHEMISTRY
·
2026
·
IF 4.1
Gao Yuexing,Lang Yunhe,Shi Lei,Bai Ruiyang,Xu Yiping,Xie Yanmei,Huang Saiyan,Zhang Xiufeng
Reduced nicotinamide adenine dinucleotide (NADH) as a biomarker plays a crucial role in studying cell redox homeostasis. Simultaneously, the abnormal behavior of viscosity in cells is often accompanied by changes in the level of related active substances. Thus, real-time monitoring of in situ changes in NADH and viscosity is of great importance. Based on the specific recognition of NADH by the quinoline group, we developed a dual-responsive probe molecule (I-EQ), which is sensitive to both NADH and viscosity. The probe exhibits high sensitivity toward NADH, with a detection limit of 0.027 µM, and also shows excellent response to viscosity. Additionally, its application in monitoring NADH and viscosity in living cells was successfully demonstrated. Given these characteristics, I-EQ is expected to serve as a valuable dual-channel response tool for NADH and viscosity, with promising application in biomedicine and early diagnosis of diseases. Graphical
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Green Energy & Environment
·
2026
·
IF 16.7
Guohua Li,Xiaodi L,Wei Zhang,Di Cai,Hui Cao,Zehan Yao,Tõnu Pullerits,Kaibo Zheng,Tianwei Tan
Photochemical regeneration of NADH is essential for bioinspired redox catalysis but remains limited by inefficient electron-proton coordination. We report a donor-acceptor conjugated polymer system with rhodium centers, where electron-donating substituents (-OH, -OMe, -Me) can modulate both photo-induced charge behavior and surface reaction properties. The optimal -OH subsitutents can, on one hand, enhances dielectric screening and planarity of the polymers to, reduce the exciton binding energy and facilitate charge injection to the rhodium active centers. On the other hand, its hydrophilicity further promotes proton migration, enabling synchronized and co-localized two-electron/one-proton donation to NAD + at the rhodium centers. Therefore, the optimized -OH-containing polymer achieved selective photoreduction of NAD + to 1,4-NADH at a rate of 12.81 mmol g -1 h -1 , which is one of the highest levels reported to date to our knowledge. Integrated into a photo-electro-enzyme cascade, the system synergistically couples NADH regeneration with enzymatic catalysis to achieve the first conversion of CO 2 -derived aldehydes into glycerol, highlighting its potential for sustainable carbon valorization. This work establishes a facile strategy to regulate both electron and proton donation in organic photocatalysts and expands their application in solar-driven biotransformations.
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高影响因子
APPLIED CATALYSIS B-ENVIRONMENTAL
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2022
·
IF 24.319
Jiali Liu,Xiaomin Ren,Chunzhi Li,Maodi Wang,He Li,Qihua Yang
Photocatalytic regeneration of the high-cost co-factor NADH is a promising method to couple photo-enzyme catalysis, however, the usage of homogeneous electron mediator ([Cp*Rh(bpy)H 2 O] 2+ ) which deactivates enzymes deteriorates the whole process efficiency. Herein, we report the immobilization of electron mediator ([Cp*Rh(bpy)H 2 O] 2+ ) on covalent organic frameworks (COFs) by the sequential assembly method. The resultant bi-functional photocatalyst with controlled cascade electron transfer afforded NADH production rate of 9.8 mmol·g COF −1 ·h −1 , much higher than previously reported ones with integrated electron mediator. The photo-enzyme coupling system with the photocatalyst and alcohol dehydrogenase could continuously produce butanol for at least 180 min under visible light irradiation, implying the potential application of bi-functional photocatalyst in artificial photosynthesis.
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BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
·
2024
·
IF 2.5
Xuanming Chang,Xiaoqian Chen,Xiuze Zhang,Nian Chen,Weitao Tang,Zhuo Zhang,Sulin Zheng,Jiong Huang,Yihan Ji,Yuzheng Zhao,Yi Yang,Xie Li
Lactate plays a crucial role in energy metabolism and greatly impacts protein activities, exerting diverse physiological and pathological effects. Therefore, convenient lactate assays for tracking spatiotemporal dynamics in living cells are desirable. In this paper, we engineered and optimized a red fluorescent protein sensor for l -lactate named FiLa-Red. This indicator exhibited a maximal fluorescence change of 730 % and an apparent dissociation constant ( K d ) of approximately 460 μM. By utilizing FiLa-Red and other sensors, we monitored energy metabolism in a multiplex manner by simultaneously tracking lactate and NAD + /NADH abundance in the cytoplasm, nucleus, and mitochondria. The FiLa-Red sensor is expected to be a useful tool for performing metabolic analysis in vitro , in living cells and in vivo .
研究领域:
细胞生物学
·
分子生物学
·
生物技术
·
代谢
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PubMed
高影响因子
CHEMOSPHERE
·
2022
·
IF 8.943
Jinghao Wang,Huimin Liu,Song Song,Yuancai Chen,Yongyou Hu
Microbial electron output capacity is critical for organic contaminants biodegradation. Herein, original C. freundii JH could oxidate formate in anaerobic respiration, but lack the ability to degrade sulfamethoxazole (SMX). While the incorporation of Pd(0) could effectively improve the electron output via improving the combination between flavins and c-type cytochromes (c-Cyts), increasing the activities of key enzymes (formate dehydrogenase , hydrogenase, F 0 F 1 -ATPases), etc. More importantly, the presence of Pd(0) caused the NADH dehydrogenase (complex I) nearly in idle, and triggered the decrease of NADH/NAD + ratio and increase of H + -efflux transmembrane gradient, eventually resulting in the electrons diverting from CoQ-involved long respiratory chain (decreasing from 91.67% to 36.25%) to FDH/Hases-based hydrogen-producing short chain (increasing from 22.44% to 84.88%), which further intensified the electron output. Above changes effectively launched and guaranteed the high-level SMX degradation by palladized C. freundii JH, alleviating the ecotoxicity of SMX in aquatic and terrestrial environments. These conclusions provided the new view to regulate the microbial electron output behaviors.
研究领域:
环境微生物学
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生物修复
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电子传递
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环境毒理学
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PubMed
高影响因子
IEEE JOURNAL OF SELECTED TOPICS IN QUANTUM ELECTRONICS
·
2019
·Vol. 25
·期 1
·1-6
·
IF 4.681
Xinyi Wang,Yonghui Xie,Maojia Huang,Longfang Yao,Yulan Wang,Yiyan Fei,Jiong Ma,Lan Mi
Fluorescence lifetime measurements are often performed on live as well as fixed cells and tissues. Fixation and mounting processes are routinely used in cellular research or clinical diagnosis. In this paper, the effects of fixation and mounting on the fluorescence lifetime of cellular autofluorescence were studied by fluorescence lifetime imaging microscopy over time. Two endogenous fluorescent fluorophores, reduced nicotinamide adenine dinucleotide (NADH) and flavin adenine dinucleotide (FAD), showed different results between live cells and fixed cells. The average lifetime of NADH in live HeLa cells was about 1.02 ns, while maintained about 1.57 ns during the fixation periods of 14 days. The average lifetimes of FAD in live and fixed HeLa cells within 11 days were similar around 1.75 ns but increased to 2.10 ns after 12 days. The free and bound states of the two kinds of fluorophores were further analyzed. It was found that the bound-FAD had two different groups, which was related to the cell division cycle. The effect of mounting medium on fluorescence lifetimes was also studied, indicating glycerol has a negative impact on the fluorescence lifetime compared with neutral balsam.
研究领域:
生物医学工程
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细胞生物学
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DOI
高影响因子
JOURNAL OF PHOTOCHEMISTRY AND PHOTOBIOLOGY A-CHEMISTRY
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2022
·
IF 5.141
Shengnan Fan,Xiaoqing Li,Fanghui Ma,Minghui Yang,Juan Su,Xiang Chen
Lactate dehydrogenase (LDH) plays an important role in the process of glycolysis as well as gluconeogenesis, and is related to many diseases, so it is of great significance to accurately detect LDH activity in serum. The fluorescence of sulfur quantum dots (SQDs) synthesized by the microwave method can be specifically enhanced by nicotinamide adenine dinucleotide (NAD + ). Based on this characteristic, we reported a sensitive fluorescence assay for LDH detection. In the presence of reductive coenzyme I (NADH), LDH catalyzes the reduction of pyruvate to lactic acid, and transforms NADH to NAD + , which specifically enhances the fluorescence intensity of SQDs. Based on the fluorescence intensity increase, the assay achieved detection of LDH in the range from 500 to 40,000 U L −1 , with limit of detection of 262 U L −1 . The assay was successfully applied for the detection of LDH activity in serum, indicating potential clinical applications.
研究领域:
生物化学
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分析化学
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生物医学工程
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高影响因子
CURRENT ISSUES IN MOLECULAR BIOLOGY
·
2026
·Vol. 48
·期 5
·472
·
IF 4.1
Lina Wang,Lian Wu,Kexin Zhang,Rui Ma,Shurong Chen,Tong Ji,Min Zhou,Jiayi Xie,Lingli Zheng,Qingshan Bill Fu
Brucellosis, acting as a typical chronic zoonotic disease, is caused by the invasion ofBrucellainto the human body. Outer membrane protein 25 (Omp25), specifically localized on theBrucellamembrane, is the main virulence factor ofBrucellaand participates in multiple links of the damage process. Omp25c, a porin protein ofBrucella, is a paralog of Omp25 with high sequence identity. NADH dehydrogenase [ubiquinone] complex I assembly factor 2 (Ndufaf2) has a key function in cell energy metabolism, particularly in the formation and activity of the mitochondrial respiratory chain. Loss of Ndufaf2 results in oxidative stress and mitochondrial DNA (mtDNA) deletion. However, the functional relationship between Omp25c and Ndufaf2, the underlying mechanism of the proteins, remains unclear. In this work, we purified the Omp25c and Ndufaf2proteins. Our data revealed that Omp25c directly interacts with Ndufaf2, as determined using Biacore analysis. In addition, assays revealed that Ompa2c reshapes the host cell’s redox environment by decreasing the oxidized nicotinamide adenine dinucleotide/reduced nicotinamide adenine dinucleotide (NAD+/NADH) ratioand adenosine triphosphate (ATP) production, whereas Ndufaf2 exerts an opposing regulatory effect; Co-expression results further revealed an antagonistic relationship between the two during metabolic processes. These findings provide a new perspective for elucidating the mechanisms of mitochondrial functional regulation inBrucella–host interactions and lay the theoretical and experimental foundation for drug development targeting metabolic interventions to eliminate intracellular pathogens.
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PubMed
高影响因子
Materials Chemistry Frontiers
·
2022
·Vol. 6
·期 22
·3391-3401
·
IF 8.683
Shuli Liu,Xiaoling Wu,Jun Xiong,Xin Yuan,Min-Hua Zong,Wen-Yong Lou
Enzymatic cofactor regeneration is of significant importance and highly desired for tremendous biocatalytic processes, which is hindered by fragility intrinsic to natural enzymes. Herein, we report a copper aspartic acid (CuAsp) metal–organic framework (MOF) with a fiber structure exhibiting both NADH peroxidase- and glycerol dehydrogenase (GlyDH)-mimicking activities. The growth mechanism of CuAsp was investigated by changing the functional groups of ligands, which demonstrated that the amino group and two carboxylate groups in aspartic acid were all involved in the formation of MOFs. The CuAsp MOF displayed high NADH peroxidase mimicking activity within a wide range of pH and temperature. A cofactor total turnover number (TTN) of up to 17 500 was obtained in a typical model reaction of glucose dehydrogenase-catalyzed oxidation of glucose. More interestingly, CuAsp exhibited glycerol dehydrogenase (GlyDH)-mimicking activity and showed higher catalytic efficiency (with kcat/Km of 14.42 mL g−1 min−1) than its native counterpart (with kcat/Km of 2.40 mL g−1 min−1). As a proof of concept, CuAsp with the dual function of NADH peroxidase and GlyDH-mimicking activities was used to catalyze the transformation of glycerol to 1,3-dihydroxyacetone (DHA). Besides, free GlyDH was encapsulated into CuAsp via a facile self-assembly process, which enabled the synergistic biosynthesis of DHA. This study may provide new insights into amino acid-based MOFs and suggest the potential of multifunctional nanozymes in the application of biocatalysis and biosensing.
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高影响因子
CHINESE JOURNAL OF CATALYSIS
·
2023
·
IF 16.5
Pengye Zhang,Wenjin Dong,Yuanyuan Zhang,Li-Nan Zhao,Hualei Yuan,Chuanjun Wang,Wenshuo Wang,Hanxiao Wang,Hongyu Zhang,Jian Liu
Photoenzyme-coupled catalysis, featuring the integration of photocatalysis with enzymes, is very promising for next-generation green biomanufacturing. The presence of an Rh complex is a prerequisite for the efficient photocatalytic regeneration of the reduced form of nicotinamide adenine dinucleotide (NADH), which poses the issue of immobilizing homogeneous complexes. In this study, a novel immobilization method based on the thermal polymerization of 2,2 ‘ -bipyridine-5,5 ‘ -diamine (DABP) onto a polymeric carbon nitride (PCN) framework is proposed. PCNbpy 4 is metalated by immobilizing Rh on the terminal bipyridine structure. Notably, partial DABP has the ability to undergo high-temperature thermal polymerization, resulting in the formation of N-doped graphene. This N-doped graphene can be grafted onto the terminal amino group, forming a potential electron transfer pathway. Additionally, N-doped graphene, because of its good electrical conductivity, guides the photogenerated electrons toward the anchored Rh sites. The catalyst achieves exclusive regeneration of 1,4-NADH with only a 0.12% Rh atomic ratio and realizes 80% NADH regeneration in 20 min. The competitive relationship between hydrogen production and NADH regeneration is also elucidated. Combined with formate dehydrogenase immobilized on a hydrophobic membrane, CO 2 reduction to formate is accomplished efficiently, and the formate concentration can accumulate to 7 mmol L −1 within 48 h.
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