26 results on '"Yue Zou"'
Search Results
2. Constructing a Stabilized Cathode Electrolyte Interphase for High-Voltage LiCoO2 Batteries via the Phenylmaleic Anhydride Additive
- Author
-
Xi Liu, Ang Fu, Jiande Lin, Yue Zou, Gaopan Liu, Weitong Wang, De-Yin Wu, Yong Yang, Jianming Zheng, and Liyi Ye
- Subjects
Materials Chemistry ,Electrochemistry ,Energy Engineering and Power Technology ,Chemical Engineering (miscellaneous) ,Electrical and Electronic Engineering - Published
- 2023
3. Substantially Promoted Energy Density of Li||CFx Primary Battery Enabled by Li+-DMP Coordinated Structure
- Author
-
Yukang Xiao, Junhua Jian, Ang Fu, Chao Tang, Yue Zou, Xunxin Chen, Jiuzhou Wang, Yong Yang, and Jianming Zheng
- Subjects
Renewable Energy, Sustainability and the Environment ,General Chemical Engineering ,Environmental Chemistry ,General Chemistry - Published
- 2022
4. Synergistical Stabilization of Li Metal Anodes and LiCoO2 Cathodes in High-Voltage Li∥LiCoO2 Batteries by Potassium Selenocyanate (KSeCN) Additive
- Author
-
Ang Fu, Jiande Lin, Zhengfeng Zhang, Chuanjing Xu, Yue Zou, Chengyong Liu, Pengfei Yan, De-Yin Wu, Yong Yang, and Jianming Zheng
- Subjects
Fuel Technology ,Renewable Energy, Sustainability and the Environment ,Chemistry (miscellaneous) ,Materials Chemistry ,Energy Engineering and Power Technology - Published
- 2022
5. Boosting the Energy Density of Li||CFx Primary Batteries Using a 1,3-Dimethyl-2-imidazolidinone-Based Electrolyte
- Author
-
Lin Huang, Yong Yang, Jianming Zheng, Chao Tang, Yue Zou, Yukang Xiao, Jiuzhou Wang, Xunxin Chen, Ang Fu, and Junhua Jian
- Subjects
Materials science ,law ,Donor number ,Energy density ,Analytical chemistry ,General Materials Science ,Electrolyte ,2-imidazolidinone ,Current density ,Cathode ,Voltage ,law.invention - Abstract
Elevating the discharge voltage plateau is regarded as the most effective strategy to improve the energy density of Li||CFx batteries in consideration of the finite capacity of CFx (x ∼ 1) cathodes. Here, an electrolyte, with LiBF4 in 1,3-dimethyl-2-imidazolidinone (DMI)/1,2-dimethoxyethane (DME), is developed for the first time to substantially promote the discharge voltage of CFx without compromising the available discharge capacity. DME possesses the property of low viscosity, while DMI functions to increase the voltage plateau during discharge owing to its moderate nucleophilicity and donor number, which decreases the energy barrier for breaking C-F bonds. The optimized electrolyte exhibits a significantly high average discharge voltage of 2.69 V at a current density of 10 mA g-1, which is 11.6% higher than the control electrolyte (2.41 V). In addition, a high energy density of 2099 Wh kg-1 is achieved in the optimized electrolyte (vs 1905 Wh kg-1 in the control electrolyte), showing great potential for practical applications.
- Published
- 2021
6. Stabilizing the LiCoO2 Interface at High Voltage with an Electrolyte Additive 2,4,6-Tris(4-fluorophenyl)boroxin
- Author
-
Jianming Zheng, Ang Fu, Yue Zou, Jing Zhang, Tianpeng Jiao, and Yong Yang
- Subjects
Tris ,chemistry.chemical_compound ,Materials science ,Chemical engineering ,chemistry ,Renewable Energy, Sustainability and the Environment ,General Chemical Engineering ,Interface (computing) ,Environmental Chemistry ,High voltage ,General Chemistry ,Electrolyte - Published
- 2021
7. Electrolyte Additive cis-1,2,3,6-Tetrahydrophthalic Anhydride Enhanced the Cycle Life of Nickel-Rich LiNi0.9Co0.05Mn0.05O2
- Author
-
Yong Cheng, Ming-Sheng Wang, Yue Zou, Gaopan Liu, Tianpeng Jiao, Xiaozhen Zhang, Jianming Zheng, and Yong Yang
- Subjects
Nickel ,Materials science ,chemistry ,Inorganic chemistry ,Materials Chemistry ,Electrochemistry ,Energy Engineering and Power Technology ,Chemical Engineering (miscellaneous) ,chemistry.chemical_element ,Electrolyte ,Electrical and Electronic Engineering - Published
- 2021
8. Enhanced Interfacial Stability of a LiNi0.9Co0.05Mn0.05O2 Cathode by a Diboron Additive
- Author
-
Jing Zhang, Gaopan Liu, Tianpeng Jiao, Jianming Zheng, Ke Zhou, Yue Zou, Yong Yang, and Xiaozhen Zhang
- Subjects
Materials science ,Chemical engineering ,law ,Materials Chemistry ,Electrochemistry ,Energy Engineering and Power Technology ,Chemical Engineering (miscellaneous) ,Electrical and Electronic Engineering ,Stability (probability) ,Cathode ,law.invention - Published
- 2021
9. Interfacial Enhancement of Silicon-Based Anode by a Lactam-Type Electrolyte Additive
- Author
-
Jianming Zheng, Yong Cheng, Gaopan Liu, Yong Yang, Tianpeng Jiao, Ke Zhou, Yue Zou, and Ming-Sheng Wang
- Subjects
chemistry.chemical_compound ,Materials science ,chemistry ,Chemical engineering ,Materials Chemistry ,Electrochemistry ,Lactam ,Energy Engineering and Power Technology ,Chemical Engineering (miscellaneous) ,Electrolyte ,Electrical and Electronic Engineering ,Silicon based ,Anode - Published
- 2021
10. Enhanced Cycle Life and Rate Capability of Single-Crystal, Ni-Rich LiNi0.9Co0.05Mn0.05O2 Enabled by 1,2,4-1H-Triazole Additive
- Author
-
Yong Yang, Ke Zhou, Gaopan Liu, Yue Zou, Ningbo Xu, Jianming Zheng, Jing Zhang, and Xiaozhen Zhang
- Subjects
Materials science ,Thermal decomposition ,chemistry.chemical_element ,02 engineering and technology ,Electrolyte ,010402 general chemistry ,021001 nanoscience & nanotechnology ,01 natural sciences ,Cathode ,0104 chemical sciences ,law.invention ,Nickel ,Chemical engineering ,chemistry ,law ,Electrode ,General Materials Science ,Interphase ,0210 nano-technology ,Ternary operation ,Single crystal - Abstract
Ternary LiNixCoyMnzO2 oxides with extremely high nickel (Ni) contents (x ≥ 0.9) are promising cathode candidates developed for higher-energy-density lithium-ion batteries, with an aim to relieve mileage anxiety. However, the structural and interfacial instability still restrict their application in electric vehicles. In this work, a novel electrolyte additive 1,2,4-1H-Triazole (HTZ) is introduced to improve the interfacial stability of LiNi0.9Co0.05Mn0.05O2 (NCM90), promoting cycle life both at 30 °C and a harsh condition of 60 °C, as well as rate capability. The NCM90||Li cells with 0.3% HTZ-added electrolyte retain 86.6% of their original capacity after 150 cycles at 1C and 30 °C, well exceeding 74.8% obtained with the baseline electrolyte. It is revealed that the additive HTZ could inhibit the thermal decomposition of LiPF6 salt and suppress the generation of HF acidic species. More importantly, additive HTZ is preferentially oxidized to construct a compact and dense cathode electrolyte interphase (CEI) layer, which is beneficial for stabilizing the electrode/electrolyte interface and suppressing unwanted side reactions.
- Published
- 2021
11. Stabilizing Ni-Rich LiNi0.83Co0.12Mn0.05O2 with Cyclopentyl Isocyanate as a Novel Electrolyte Additive
- Author
-
Yue Zou, Yong Yang, Ke Zhou, Ningbo Xu, Xuerui Yang, Gaopan Liu, Jianming Zheng, Tianpeng Jiao, and Wu Yang
- Subjects
chemistry.chemical_classification ,Materials science ,Thermal decomposition ,Salt (chemistry) ,02 engineering and technology ,Electrolyte ,010402 general chemistry ,021001 nanoscience & nanotechnology ,Hydrogen fluoride ,Electrochemistry ,01 natural sciences ,Isocyanate ,Cathode ,0104 chemical sciences ,law.invention ,chemistry.chemical_compound ,chemistry ,Chemical engineering ,law ,General Materials Science ,0210 nano-technology ,Bifunctional - Abstract
Ni-rich layered structure materials are appealing cathodes for high-energy-density lithium-ion batteries developed for electric vehicles, drones, power tools, etc. However, poor interfacial stability between a Ni-rich cathode and carbonate electrolyte, especially at high temperatures, and fast capacity fading still hinder their mass market penetration. Here, we investigate cyclopentyl isocyanate (CPI) with a single isocyanate (-NCO) functional group as a bifunctional electrolyte additive for the first time to improve the interfacial stability of Ni-rich cathode LiNi0.83Co0.12Mn0.05O2 (NCM83). With an electrolyte containing 2 wt % CPI, the NCM83 cathode shows capacity retention of up to 92.3% after 200 cycles at 1C and 30 °C, much higher than that with the standard electrolyte (78.6%). It is demonstrated that the -NCO of CPI could largely inhibit the thermal decomposition of LiPF6 salt and scavenge water and hydrogen fluoride (HF) species, improving electrolyte stability. More importantly, the additive CPI could be preferentially oxidized, forming a stabilized and protective cathode electrolyte interphase (CEI) layer on the surface of NCM83, which effectively suppresses the parasitic side reactions and maintains the superior interfacial charge-transfer and lithium-ion diffusion kinetics. Both functions enable a significant improvement in electrochemical performance at both 30 and 60 °C.
- Published
- 2021
12. Visible-Light-Promoted C2 Selective Arylation of Quinoline and Pyridine N-Oxides with Diaryliodonium Tetrafluoroborate
- Author
-
Ce Liang, Jiang Zaixing, Wang-Tao Zhuo, Jinzhu Song, Dazhi Li, Guo-Lin Gao, Fan-Yue Zou, Junzheng Zhang, and Wan-Peng Wang
- Subjects
Tetrafluoroborate ,010405 organic chemistry ,Organic Chemistry ,Quinoline ,Regioselectivity ,010402 general chemistry ,01 natural sciences ,Combinatorial chemistry ,0104 chemical sciences ,chemistry.chemical_compound ,chemistry ,Reagent ,Functional group ,Pyridine ,Photocatalysis ,Eosin Y - Abstract
A protocol of visible-light-promoted C2 selective arylation of quinoline and pyridine N-oxides, with diaryliodonium tetrafluoroborate as an arylation reagent, using eosin Y as a photocatalyst for the construction of N-heterobiaryls was presented. This methodology provided an efficient way for the synthesis of 2-aryl-substituted quinoline and pyridine N-oxides. This strategy has the following advantages: specific regioselectivity, simple operation, good functional group tolerance, and high to moderate yields under mild conditions.
- Published
- 2020
13. Sequential Diels–Alder Reaction/Rearrangement Sequence: Synthesis of Functionalized Bicyclo[2.2.1]heptane Derivatives and Revision of Their Relative Configuration
- Author
-
Andreas Goeke, Demin Liang, Quanrui Wang, and Yue Zou
- Subjects
Heptane ,Magnetic Resonance Spectroscopy ,Molecular Structure ,Bicyclic molecule ,Chemistry ,Stereochemistry ,Organic Chemistry ,Nuclear magnetic resonance spectroscopy ,Chiral Lewis acid ,Heptanone ,Bridged Bicyclo Compounds ,chemistry.chemical_compound ,Enantiomer ,Two-dimensional nuclear magnetic resonance spectroscopy ,Diels–Alder reaction - Abstract
A sequential Diels-Alder reaction/rearrangement sequence was developed for the synthesis of diverse functionalized bicyclo[2.2.1]heptanes as novel floral and woody odorants. The outcome of the rearrangement depended on the substitution pattern of the dienes. 2D NMR analysis has established the correct relative configuration of the bicyclo[2.2.1]heptanone, which was originally misassigned. Furthermore, when the initiating DA reaction was catalyzed by a chiral Lewis acid, the bicyclo[2.2.1]heptane derivatives including (+)-herbanone can be obtained in an enantiomeric ratio (er) up to 96.5:3.5.
- Published
- 2014
14. Spectroscopic and Theoretical Insights into Sequence Effects of Aminofluorene-Induced Conformational Heterogeneity and Nucleotide Excision Repair
- Author
-
M. Paul Chiarelli, Wang Lee, Lan Gao, Steven M. Shell, Yue Zou, Srinivasarao Meneni, Jiri Sponer, Petr Jurečka, and Bongsup P. Cho
- Subjects
Circular dichroism ,education.field_of_study ,Magnetic Resonance Spectroscopy ,Base Sequence ,DNA Repair ,Chemistry ,Stereochemistry ,Base pair ,Circular Dichroism ,Population ,Temperature ,Nuclear magnetic resonance spectroscopy ,2-Acetylaminofluorene ,Models, Biological ,Biochemistry ,Adduct ,DNA Adducts ,Crystallography ,chemistry.chemical_compound ,Nucleic Acid Conformation ,Spectrophotometry, Ultraviolet ,education ,Conformational isomerism ,DNA ,Nucleotide excision repair - Abstract
A systematic spectroscopic and computational study was conducted in order to probe the influence of base sequences on stacked (S) versus B-type (B) conformational heterogeneity induced by the major dG adduct derived from the model carcinogen 7-fluoro-2-aminofluorene (FAF). We prepared and characterized eight 12-mer DNA duplexes (-AG*N- series, d[CTTCTAG*NCCTC]; -CG*N- series, d[CTTCTCG*NCCTC]), in which the central guanines (G*) were site-specifically modified with FAF with varying flanking bases (N = G, A, C, T). S/B heterogeneity was examined by CD, UV, and dynamic 19F NMR spectroscopy. All the modified duplexes studied followed a typical dynamic exchange between the S and B conformers in a sequence dependent manner. Specifically, purine bases at the 3'-flanking site promoted the S conformation (G > A > C > T). Simulation analysis showed that the S/B energy barriers were in the 14-16 kcal/mol range. The correlation times (tau = 1/kappa) were found to be in the millisecond range at 20 degrees C. The van der Waals energy force field calculations indicated the importance of the stacking interaction between the carcinogen and neighboring base pairs. Quantum mechanics calculations showed the existence of correlations between the total interaction energies (including electrostatic and solvation effects) and the S/B population ratios. The S/B equilibrium seems to modulate the efficiency of Escherichia coli UvrABC-based nucleotide excision repair in a conformation-specific manner: i.e., greater repair susceptibility for the S over B conformation and for the -AG*N- over the -CG*N- series. The results indicate a novel structure-function relationship, which provides insights into how bulky DNA adducts are accommodated by UvrABC proteins.
- Published
- 2007
15. Conformation-Specific Recognition of Carcinogen−DNA Adduct in Escherichia coli Nucleotide Excision Repair
- Author
-
Yue Zou, Steven M. Shell, Srinivasarao Meneni, and Bongsup P. Cho
- Subjects
education.field_of_study ,Magnetic Resonance Spectroscopy ,Base Sequence ,DNA Repair ,biology ,Base pair ,Chemistry ,Stereochemistry ,Population ,Molecular Conformation ,Active site ,General Medicine ,Toxicology ,Adduct ,DNA Adducts ,chemistry.chemical_compound ,DNA adduct ,Carcinogens ,Escherichia coli ,biology.protein ,Thermodynamics ,education ,Conformational isomerism ,DNA ,Nucleotide excision repair - Abstract
We report a systematic and quantitative structure-function relationship study of the major N-[deoxyguanosin-8-yl]-2-aminofluorene adduct (AF) derived from the prototype carcinogen 2-aminofluorene and its derivatives. The AF adduct is known to exist in two distinct conformational motifs, depending upon the location of the hydrophobic fluorine moiety: major groove binding "B type" (B) conformation (AF-dG anti ) and base-displaced "stacked" (S) conformation (AF-dG syn ). The AF-induced S/B conformational heterogeneity is sequence-dependent and follows a typical two-site dynamic chemical exchange. The population of S conformation decreases in the order of 3'-G > A » C > T, indicating the importance of the purine flanking bases in promoting the stacking structure. Line-shape analysis showed that the S/B interconversion energy barriers (ΔG ‡ ) are in the narrow 14-16 kcal/mol range. The energy differences of the two conformers are relatively small (
- Published
- 2006
16. Specific and Efficient Binding of Xeroderma Pigmentosum Complementation Group A to Double-Strand/Single-Strand DNA Junctions with 3‘- and/or 5‘-ssDNA Branches
- Author
-
Thomas M. Harris, Constance M. Harris, Yiyong Liu, Laureen C. Colis, Yue Zou, Steven M. Shell, Ashis K. Basu, Zhengguan Yang, Phillip R. Musich, and Marina Roginskaya
- Subjects
endocrine system ,Xeroderma pigmentosum ,DNA Repair ,DNA repair ,DNA damage ,Molecular Sequence Data ,DNA, Single-Stranded ,Plasma protein binding ,Spodoptera ,Biology ,Biochemistry ,DNA-binding protein ,Article ,Cell Line ,DNA Adducts ,chemistry.chemical_compound ,medicine ,Animals ,Humans ,Replication protein A ,Base Sequence ,medicine.disease ,Molecular biology ,humanities ,Xeroderma Pigmentosum Group A Protein ,DNA-Binding Proteins ,enzymes and coenzymes (carbohydrates) ,chemistry ,Nucleic Acid Conformation ,Baculoviridae ,DNA ,DNA Damage ,Protein Binding ,Nucleotide excision repair - Abstract
Human XPA is an important DNA damage recognition protein in nucleotide excision repair (NER). We previously observed that XPA binds to the DNA lesion as a homodimer [Liu, Y., Liu, Y., Yang, Z., Utzat, C., Wang, G., Basu, A. K., and Zou, Y. (2005) Biochemistry 44, 7361-7368]. Herein we report that XPA recognized undamaged DNA double-strand/single-strand (ds-ssDNA) junctions containing ssDNA branches with binding affinity (Kd = 49.1 +/- 5.1 nM) much higher than its ability to bind to DNA damage. The recognized DNA junction structures include the Y-shape junction (with both 3'- and 5'-ssDNA branches), 3'-overhang junction (with a 3'-ssDNA branch), and 5'-overhang junction (with a 5'-ssDNA branch). Using gel filtration chromatography and gel mobility shift assays, we showed that the highly efficient binding appeared to be carried out by the XPA monomer and that the binding was largely independent of RPA. Furthermore, XPA efficiently bound to six-nucleotide mismatched DNA bubble substrates with or without DNA adducts including C8 guanine adducts of AF, AAF, and AP and the T[6,4]T photoproducts. Using a set of defined DNA substrates with varying degrees of DNA bending, we also found that the XPC-HR23B complex recognized DNA bending, whereas neither XPA nor the XPA-RPA complex could bind to bent DNA. We propose that, besides DNA damage recognition, XPA may also play a novel role in stabilizing, via its high affinity to ds-ssDNA junctions, the DNA strand opening surrounding the lesion for stable formation of preincision NER intermediates. Our results provide a plausible mechanistic interpretation for the indispensable requirement of XPA for both global genome and transcription-coupled repairs. Since ds-ssDNA junctions are common intermediates in many DNA metabolic pathways, the additional potential role of XPA in cellular processes is discussed.
- Published
- 2006
17. Recognition and Incision of Oxidative Intrastrand Cross-Link Lesions by UvrABC Nuclease
- Author
-
Qibin Zhang, Yue Zou, Yinsheng Wang, Yuesong Wang, Chunang Gu, and Zhengguan Yang
- Subjects
Pyrimidine ,Molecular Sequence Data ,Pyrimidine dimer ,medicine.disease_cause ,Biochemistry ,Article ,Substrate Specificity ,chemistry.chemical_compound ,Escherichia coli ,medicine ,Pyrimidone ,Endodeoxyribonucleases ,Base Sequence ,Molecular Structure ,biology ,Escherichia coli Proteins ,DNA ,Molecular biology ,chemistry ,Pyrimidine Dimers ,Duplex (building) ,biology.protein ,Nucleic Acid Conformation ,Oxidation-Reduction ,Nucleotide excision repair - Abstract
Nucleotide excision repair (NER) is a repair pathway that removes a variety of bulky DNA lesions in both prokaryotic and eukaryotic cells. The perturbation of DNA helix structure caused by the oxidative intrastrand lesions could render them good substrates for the NER pathway. Here we employed Escherichia coli (E. coli) NER enzymes, i.e., UvrA, UvrB and UvrC, to examine the incision efficiency of duplex DNA carrying three different oxidative intrastrand cross-link lesions, that is, G[8-5]C, G[8-5m]mC, and G[8-5m]T, and two dithymine photoproducts, namely, the cis,syn-cyclobutane pyrimidine dimer (T[c,s]T) and pyrimidine(6-4)pyrimidone product (T[6-4]T). Our results showed that T[6-4]T was the best substrate for UvrA binding, followed by G[8-5]C, G [8-5m]mC and G[8-5m]T, and then by T[c,s]T. The efficiencies of the UvrABC incisions of these lesions were consistent with their UvrA binding affinities: The stronger the binding to UvrA, the higher the incision rate. In addition, flanking DNA sequences appeared to have little effect on the binding affinity of UvrA toward G[8-5]C as AG[8-5]CA was only slightly preferred over CG[8-5] CG. Consistently, these two sequences exhibited almost no difference in incision rates. Furthermore, we investigated the thermal stability of dodecameric duplexes containing a G[8-5m]mC or G[8-5m] T and our results revealed that these two lesions destabilized the duplex, due to an increase in free energy for duplex formation at 37°C, by approximately 5.4 kcal/mol and 3.6 kcal/mol, respectively. The destabilizations to DNA helix caused by those lesions, for the most part, are correlated with the binding affinities of UvrA and incision rates of UvrABC. Taken together, the results from this study suggest that oxidative intrastrand lesions might be substrates for NER enzymes in vivo.
- Published
- 2006
18. Recognition and Incision of γ-Radiation-Induced Cross-Linked Guanine−Thymine Tandem Lesion G[8,5-Me]T by UvrABC Nuclease
- Author
-
Yue Zou, Ashis K. Basu, Laureen C. Colis, and Zhengguan Yang
- Subjects
Guanine ,Molecular Sequence Data ,Toxicology ,medicine.disease_cause ,Article ,Substrate Specificity ,chemistry.chemical_compound ,Escherichia coli ,medicine ,A-DNA ,Nucleotide ,Endodeoxyribonucleases ,Chromatography, High Pressure Liquid ,chemistry.chemical_classification ,Base Sequence ,biology ,Escherichia coli Proteins ,DNA ,General Medicine ,Thymine ,chemistry ,Biochemistry ,Gamma Rays ,biology.protein ,Nucleic Acid Conformation ,Nucleotide excision repair - Abstract
Nucleotide excision repair (NER) plays an important role in maintaining the integrity of DNA by removing various types of bulky or distorting DNA adducts in both prokaryotic and eukaryotic cells. In Escherichia coli, the excision repair proteins UvrA, UvrB, and UvrC recognize and incise the bulky DNA damages induced by UV light and chemical carcinogens. In this process, when a putative lesion in DNA is identified initially by UvrA, a subsequent strand opening is carried out by UvrB that not only ensures that the distortion is indeed due to a damaged nucleotide but also recognizes the chemical structure of the modified nucleotides with varying efficiencies. UvrB also recruits UvrC that catalyzes both the 3'- and the 5'-incisions. Herein, we examined the interaction of UvrABC with a DNA substrate containing a single G[8,5-Me]T cross-link and compared it with T[6,4]T (the 6-4 pyrimidine-pyrimidone photoproduct) and the C8 guanine adduct of N-acetyl-2-aminofluorene (AAF). The intrastrand vicinal cross-link G[8,5-Me]T containing a covalent bond between the C8 position of guanine and the 5-methyl carbon of the 3'-thymine is formed by X-radiation, while T[6,4]T is a vicinal cross-link induced by the UV light. We also selected the AAF adduct for comparison because it represents a highly distorting monoadduct containing a covalent linkage at the C8 position of guanine. The dissociation constants (K(d)) for UvrA protein binding to DNA substrates containing the G[8,5-Me]T, T[6,4]T, and AAF adducts, as determined by gel mobility shift assays, were 3.1 +/- 1.3, 2.8 +/- 0.9, and 8.2 +/- 1.9, respectively. Although UvrA had a considerably higher affinity for G[8,5-Me]T than for the AAF adduct, the G[8,5-Me]T intrastrand cross-link was incised by UvrABC much less efficiently than the T[6,4]T intrastrand cross-link and the AAF adduct. Similar incision results also were obtained with the DNA substrates containing the adducts in a six-nucleotide bubble, indicating that the inefficient incision of G[8,5-Me]T cross-link by UvrABC was probably due to the lack of efficient recognition of the adduct by UvrB at the second step of DNA damage recognition in the E. coli NER. Indeed, as compared to T[6,4]T and AAF substrates, which clearly showed UvrB-DNA complex formation, very little UvrB complex was detectable with the G[8,5-Me]T substrate. Our result suggests that G[8,5-Me]T intrastrand cross-link is more resistant to excision repair in comparison with the T[6,4]T and AAF adducts and thus will likely persist longer in E. coli cells.
- Published
- 2005
19. Mass Spectrometric Identification of Lysines Involved in the Interaction of Human Replication Protein A with Single-Stranded DNA
- Author
-
Mamuka Kvaratskhelia, Yue Zou, Steven M. Shell, and Sonja Hess
- Subjects
HMG-box ,DNA damage ,Molecular Sequence Data ,DNA, Single-Stranded ,complex mixtures ,Biochemistry ,DNA-binding protein ,Article ,Mass Spectrometry ,Single-stranded binding protein ,chemistry.chemical_compound ,Replication Protein A ,Humans ,Amino Acid Sequence ,Replication protein A ,Sequence Homology, Amino Acid ,biology ,Protein footprinting ,Lysine ,Binding protein ,DNA-Binding Proteins ,enzymes and coenzymes (carbohydrates) ,chemistry ,biology.protein ,Electrophoresis, Polyacrylamide Gel ,DNA ,Protein Binding - Abstract
Human replication protein A (hRPA), a heterotrimeric single-stranded DNA (ssDNA) binding protein, is required for many cellular pathways including DNA damage repair, recombination, and replication as well as the ATR-mediated DNA damage response. While extensive effort has been devoted to understanding the structural relationships between RPA and ssDNA, information is currently limited to the RPA domains, the trimerization core, and a partial cocrystal structure. In this work, we employed a mass spectrometric protein footprinting method of single amino acid resolution to investigate the interactions of the entire heterotrimeric hRPA with ssDNA. In particular, we monitored surface accessibility of RPA lysines with NHS-biotin modification in the contexts of the free protein and the nucleoprotein complex. Our results not only indicated excellent agreement with the available crystal structure data for RPA70 DBD-AB-ssDNA complex but also revealed new protein contacts in the nucleoprotein complex. In addition to two residues, K263 and K343 of p70, previously identified by cocrystallography as direct DNA contacts, we observed protection of five additional lysines (K183, K259, K489, K577, and K588 of p70) upon ssDNA binding to RPA. Three residues, K489, K577, and K588, are located in ssDNA binding domain C and are likely to establish the direct contacts with cognate DNA. In contrast, no ssDNA-contacting lysines were identified in DBD-D. In addition, two lysines, K183 and K259, are positioned outside the putative ssDNA binding cleft. We propose that the protection of these lysines could result from the RPA interdomain structural reorganization induced by ssDNA binding.
- Published
- 2004
20. Effects of DNA Adduct Structure and Sequence Context on Strand Opening of Repair Intermediates and Incision by UvrABC Nuclease
- Author
-
Ashis K. Basu, Christopher Utzat, Charlie Luo, Nicholas E. Geacintov, Zhengguan Yang, Yue Zou, and Steven M. Shell
- Subjects
chemistry.chemical_classification ,Endodeoxyribonucleases ,Base Sequence ,DNA Repair ,DNA repair ,Stereochemistry ,DNA damage ,Escherichia coli Proteins ,Molecular Sequence Data ,Electrophoretic Mobility Shift Assay ,Context (language use) ,Biochemistry ,Molecular biology ,Article ,Adduct ,DNA Adducts ,chemistry.chemical_compound ,chemistry ,DNA adduct ,Nucleotide ,DNA ,Nucleotide excision repair - Abstract
DNA damage recognition of nucleotide excision repair (NER) in Escherichia coli is achieved by at least two steps. In the first step, a helical distortion is recognized, which leads to a strand opening at the lesion site. The second step involves the recognition of the type of chemical modification in the single-stranded region of DNA during the processing of the lesions by UvrABC. In the current work, by comparing the efficiencies of UvrABC incision of several types of different DNA adducts, we show that the size and position of the strand opening are dependent on the type of DNA adducts. Optimal incision efficiency for the C8-guanine adducts of 2-aminofluorene (AF) and N-acetyl-2-aminofluorene (AAF) was observed in a bubble of three mismatched nucleotides, whereas the same for C8-guanine adduct of 1-nitropyrene and N(2)-guanine adducts of benzo[a]pyrene diol epoxide (BPDE) was noted in a bubble of six mismatched nucleotides. This suggests that the size of the aromatic ring system of the adduct might influence the extent and number of bases associated with the opened strand region catalyzed by UvrABC. We also showed that the incision efficiency of the AF or AAF adduct was affected by the neighboring DNA sequence context, which, in turn, was the result of differential binding of UvrA to the substrates. The sequence context effect on both incision and binding disappeared when a bubble structure of three bases was introduced at the adduct site. We therefore propose that these effects relate to the initial step of damage recognition of DNA structural distortion. The structure-function relationships in the recognition of the DNA lesions, based on our results, have been discussed.
- Published
- 2003
21. Dimerization of Human XPA and Formation of XPA2−RPA Protein Complex
- Author
-
Leslie Y. Mao, Yue Zou, Yang Liu, Zheng guan Yang, and Jian-Ting Zhang
- Subjects
DNA Replication ,endocrine system ,DNA Repair ,Macromolecular Substances ,DNA repair ,DNA damage ,Dimer ,Plasma protein binding ,Spodoptera ,Biochemistry ,Article ,chemistry.chemical_compound ,Replication Protein A ,Escherichia coli ,Animals ,Humans ,Replication protein A ,Fluorocarbons ,Molecular mass ,Chemistry ,DNA replication ,Recombinant Proteins ,Xeroderma Pigmentosum Group A Protein ,DNA-Binding Proteins ,Molecular Weight ,Spectrometry, Fluorescence ,Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ,Chromatography, Gel ,Electrophoresis, Polyacrylamide Gel ,Caprylates ,Dimerization ,Protein Processing, Post-Translational ,Protein Binding ,Nucleotide excision repair - Abstract
XPA plays an important role in the DNA damage recognition during human nucleotide excision repair. Here we report that the XPA is a homodimer either in the free state or as a complex with human RPA in solution under normal conditions. The human XPA protein purified from baculovirus-infected sf21 insect cells has a molecular mass of 36 317 Da, as determined by mass spectroscopy. However, the apparent molecular mass of XPA determined by the native gel filtration chromatography was about 71 kDa, suggesting that XPA is a dimer. This observation was supported by a native PFO-PAGE and fluorescence spectroscopy analysis. XPA formed a dimer (XPA2) in a broad range of XPA and NaCl concentrations, and the dimerization was not due to the disulfide bond formation. Furthermore, a titration analysis of the binding of XPA to the human RPA indicated that it was the XPA2 that formed the complex with RPA. Finally, the difference between the mass spectrometric and the calculated masses of XPA implies that the protein contains posttranslational modifications. Taken together, our data suggest that the dimerization of XPA may play an important role in the DNA damage recognition of nucleotide excision repair.
- Published
- 2002
22. Intrastrand DNA Cross-Links as Tools for Studying DNA Replication and Repair: Two-, Three-, and Four-Carbon Tethers between the N2 Positions of Adjacent Guanines
- Author
-
Yue Zou, Bennett Van Houten, Constance M. Harris, Thomas M. Harris, R. Stephen Lloyd, Agnieszka Kowalczyk, and J. Russ Carmical
- Subjects
DNA Replication ,inorganic chemicals ,Endodeoxyribonucleases ,Guanine ,Base Sequence ,DNA Repair ,Oligonucleotide ,Stereochemistry ,Escherichia coli Proteins ,Oligonucleotides ,DNA replication ,chemistry.chemical_element ,DNA-Directed DNA Polymerase ,Templates, Genetic ,Biochemistry ,DNA Adducts ,chemistry.chemical_compound ,Cross-Linking Reagents ,chemistry ,Nucleic Acid Conformation ,Carbon ,DNA - Abstract
A general protocol for preparation of oligonucleotides containing intrastrand cross-links between the exocyclic amino groups of adjacent deoxyguanosines has been developed. A series of 2, 3, and 4 methylene cross-links was incorporated site-specifically into an 11-mer (5'-GGCAGGTGGTG-3', cross-linked positions are underlined) via a reaction between oligonucleotide containing 2-fluoro-O(6)-trimethylsilylethyl deoxyinosines and the appropriate diamine (ethylenediamine, 1,3-diaminopropane, 1,4-diaminobutane). These cross-linked-oligonucleotides were studied for their ability to bend DNA by the method of Koo and Crothers [Koo, H. S., and Crothers, D. M. (1988) Proc. Natl. Acad. Sci. U.S.A. 85, 1763-1767] in which the mobility of ligated oligomers in nondenaturing polyacrylamide gels is evaluated. It was found that all cross-links induced bending (2-carbon cross-link, 30.0 +/- 4.0 deg/turn; 3-carbon cross-link, 11.7 +/- 1.6 deg/turn; 4-carbon cross-link, 7.4 +/- 1.0 deg/turn). Despite the differing extent of helical distortion exhibited by the cross-links, all appeared to be equally blocking to replication by the Escherichia coli polymerases, pol I, pol II, and pol III. In contrast, when incision of the cross-links by the E. coli UvrABC nucleotide incision complex was studied, the extent of incision of the cross-link was found to correlate closely with the degree of bending measured in the gel mobility assay, i.e., the efficiency of incision was 2-carbon3-carbon4-carbon.
- Published
- 2002
23. Effects of Geometric Isomerism and Ligand Substitution in Bifunctional Dinuclear Platinum Complexes on Binding Properties and Conformational Changes in DNA
- Author
-
Yue Zou, Ana Paula Soares Fontes, K A Skov, Yun Qu, Philip K. Wu, Nicholas Farrell, T G Appleton, and John D. Roberts
- Subjects
inorganic chemicals ,Steric effects ,Coordination sphere ,Base Sequence ,Ligand ,Stereochemistry ,Molecular Sequence Data ,Platinum Compounds ,DNA ,Ligands ,Biochemistry ,chemistry.chemical_compound ,Isomerism ,chemistry ,Diamine ,parasitic diseases ,Pyridine ,Nucleic Acid Conformation ,Bifunctional ,Cis–trans isomerism ,Derivative (chemistry) ,Protein Binding - Abstract
The DNA binding profile of a series of dinuclear platinum complexes [{trans-PtCl-(L)2}2H2N(CH2)nNH2]2+ (L = NH3 or py; 1,1/t,t/NH3 and 1,1/t,t/py, respectively) and [{cis-PtCl-(NH3)2H2N(CH2)nNH2]2+ (1,1/c,c/NH3) was examined to compare the effects of geometrical isomerism and the presence of ligands other than NH3 in the coordination sphere. Steric effects, because of the geometry of the leaving groups cis to the diamine bridge or the presence of planar pyridine ligands, result in diminished binding to calf thymus DNA for these isomers. In contrast, the pyridine derivative shows a distinct binding preference for poly(dG-dC).poly(dG-dC) in comparison to both NH3 isomers. Both NH3 complexes induced the B-->Z transition in poly(dG-dC).poly(dG-dC), but the presence of a pyridine ligand stabilized the B conformation. The bifunctional binding of the NH3 isomers results in unwinding of supercoiled pUC19 plasmid DNA equivalent to cis-DDP, while the unwinding of the pyridine derivative is approximately twice that of the mononuclear trans-[PtCl2(py)2]. DNA-DNA interstrand cross-linking is very efficient for all three agents, but sequencing studies indicated that only the 1,1/t,t/NH3 derivative is capable of forming a (Pt,Pt) intrastrand cross-link to the adjacent guanines of a d(GpG) sequence. The effects on DNA caused by bifunctional binding of dinuclear complexes are compared with those from the mononuclear [PtCl2(NH3)2] isomers. The results are discussed with respect to the antitumor activity of the dinuclear series.
- Published
- 1995
24. Sequence Specificity of DNA-DNA Interstrand Cross-Link Formation by Cisplatin and Dinuclear Platinum Complexes
- Author
-
Yue Zou, B. Van Houten, and Nicholas Farrell
- Subjects
Exonuclease ,Binding Sites ,Base Sequence ,Organoplatinum Compounds ,biology ,Stereochemistry ,Oligonucleotide ,Chemistry ,Base pair ,Molecular Sequence Data ,DNA ,Biochemistry ,DNA Adducts ,chemistry.chemical_compound ,Cross-Linking Reagents ,biology.protein ,A-DNA ,Cisplatin ,Primer (molecular biology) ,Binding site ,Polymerase - Abstract
The sequence specificity of interstrand cross-links induced in DNA by mononuclear and dinuclear platinum complexes in a 49-base-pair DNA duplex has been determined directly. This new assay takes advantage of the fact that 3'-->5' exonuclease digestion of randomly platinated DNA produces a pool of fragments of different lengths. This treatment allows identification of the spectrum of adducts impeding the exonuclease scission. Interstrand cross-linked adducts produce fragments that may remain complementary in the proximity of the binding site. As a result, these fragments may act as primer templates for extension upon subsequent treatment with a DNA polymerase. This extension increases the size of the oligonucleotide fragments, which may be evidenced by a more slowly migrating band on a sequencing gel. Concomitantly, the original band corresponding to the digested cross-link decreases in intensity. Therefore, comparison of a sequencing gel after digestion only and after the "digestion-extension" treatment should show the disappearance, or diminished band intensity, of only those fragments with interstrand cross-links. This approach was applied to the analysis of DNA interstrand cross-links formed by cis-[PtCl2(NH3)2] (cis-DDP) and [(trans-PtCl(NH3)2)2H2N(CH2)4NH2]Cl2. Cis-DDP was confirmed to form interstrand cross-links at d(GC) sequences but, interestingly, interstrand cross-links predominated in a sequence GCGG, with possible 1,3-intrastrand but no 1,2-intrastrand cross-links forming. The dinuclear compound formed 1,2, 1,3, and 1,4 DNA interstrand cross-links between guanines on opposite strands. In 1,3 and 1,4 cross-links, the guanines are separated by one and two base pairs, respectively, whereas a 1,2 cross-link is formed from guanines on neighboring base pairs.(ABSTRACT TRUNCATED AT 250 WORDS)
- Published
- 1994
25. DNA Damage Recognition of Mutated Forms of UvrB Proteins in Nucleotide Excision Repair
- Author
-
Nicholas E. Geacintov, Zhengguan Yang, Irina G. Minko, Youxing Qu, Steven M. Shell, R. Stephen Lloyd, Yue Zou, Ying Xu, and Huaxian Ma
- Subjects
Models, Molecular ,DNA Repair ,DNA repair ,DNA damage ,Molecular Sequence Data ,Biology ,Biochemistry ,Article ,DNA Glycosylases ,Substrate Specificity ,DNA Adducts ,chemistry.chemical_compound ,DNA Repair Protein ,Uracil-DNA Glycosidase ,Adenosine Triphosphatases ,Genetics ,Endodeoxyribonucleases ,Base Sequence ,Escherichia coli Proteins ,Mutagenesis ,DNA Helicases ,Tryptophan ,DNA-Binding Proteins ,Cross-Linking Reagents ,Spectrometry, Fluorescence ,Amino Acid Substitution ,chemistry ,Structural Homology, Protein ,DNA glycosylase ,Uracil-DNA glycosylase ,Mutagenesis, Site-Directed ,Tyrosine ,DNA ,DNA Damage ,Protein Binding ,Nucleotide excision repair - Abstract
The DNA repair protein UvrB plays an indispensable role in the stepwise and sequential damage recognition of nucleotide excision repair in Escherichia coli. Our previous studies suggested that UvrB is responsible for the chemical damage recognition only upon a strand opening mediated by UvrA. Difficulties were encountered in studying the direct interaction of UvrB with adducts due to the presence of UvrA. We report herein that a single point mutation of Y95W in which a tyrosine is replaced by a tryptophan results in an UvrB mutant that is capable of efficiently binding to structure-specific DNA adducts even in the absence of UvrA. This mutant is fully functional in the UvrABC incisions. The dissociation constant for the mutant-DNA adduct interaction was less than 100 nM at physiological temperatures as determined by fluorescence spectroscopy. In contrast, similar substitutions at other residues in the beta-hairpin with tryptophan or phenylalanine do not confer UvrB such binding ability. Homology modeling of the structure of E. coli UvrB shows that the aromatic ring of residue Y95 and only Y95 directly points into the DNA binding cleft. We have also examined UvrB recognition of both "normal" bulky BPDE-DNA and protein-cross-linked DNA (DPC) adducts and the roles of aromatic residues of the beta-hairpin in the recognition of these lesions. A mutation of Y92W resulted in an obvious decrease in the efficiency of UvrABC incisions of normal adducts, while the incision of the DPC adduct is dramatically increased. Our results suggest that Y92 may function differently with these two types of adducts, while the Y95 residue plays an unique role in stabilizing the interaction of UvrB with DNA damage, most likely by a hydrophobic stacking.
- Published
- 2004
26. An EPR study of copper(II) complexes of poly(L-ornithine) and poly(L-2,4-diaminobutyric acid)
- Author
-
Jonathon P. Pease, Yue Zou, and Frederick T. Greenaway
- Subjects
Aqueous solution ,Polymers and Plastics ,Chemistry ,Organic Chemistry ,chemistry.chemical_element ,Copper ,law.invention ,Inorganic Chemistry ,law ,Sequestrant ,Polymer chemistry ,Materials Chemistry ,Molecule ,Organic chemistry ,Chelation ,Poly-L-ornithine ,Electron paramagnetic resonance - Published
- 1989
Catalog
Discovery Service for Jio Institute Digital Library
For full access to our library's resources, please sign in.