An Explanation on the Electron Ionization Mass Spectra of Crown Ethers by MNDO Computational Method

ＡｎＥｘｐｌａｎａｔｉｏｎｏｎｔｈｅＥｌｅｃｔｒｏｎＩｏｎｉｚａｔｉｏｎＭａｓｓＳｐｅｃｔｒａｏｆＣｒｏｗｎＥｔｈｅｒｓｂｙＭＮＤＯＣｏｍｐｕｔａｔｉｏｎａｌＭｅｔｈｏｄＹＵＡＮＨｕ－ｓｈａｎ，ＴＡＮＧＭｉｎｇ－ｓｈｅｎｇａｎｄＷＵＹａｎｇ－ｊｉｅ（...     

The Electrochemistry of Cytochrome c at a Viologen-thiol Self-Assembled Monolayer

ＴｈｅＥｌｅｃｔｒｏｃｈｅｍｉｓｔｒｙｏｆＣｙｔｏｃｈｒｏｍｅｃａｔａＶｉｏｌｏｇｅｎ－ｔｈｉｏｌＳｅｌｆ－ＡｓｓｅｍｂｌｅｄＭｏｎｏｌａｙｅｒＬＩＪｉｎｇ－ｈｏｎｇ,ＣＨＥＮＧＧｕａｎｇ－ｊｉｎ,ＤＯＮＧＳｈａｏ－ｊｕｎ（ＬａｂｏｒａｔｏｒｙｏｆＥ...     

Permselectivity of 4－Aminophenol，Paracetanol and Phenacetin on the Self－Assembled n－Alkanethiol Monolayer Modified Gold Electrode

Ｐｅｒｍｓｅｌｅｃｔｉｖｉｔｙｏｆ４－Ａｍｉｎｏｐｈｅｎｏｌ，ＰａｒａｃｅｔａｎｏｌａｎｄＰｈｅｎａｃｅｔｉｎｏｎｔｈｅＳｅｌｆ－Ａｓｓｅｍｂｌｅｄｎ－ＡｌｋａｎｅｔｈｉｏｌＭｏｎｏｌａｙｅｒＭｏｄｉｆｉｅｄＧｏｌｄＥｌｅｃｔｒｏｄｅＬｉＪｉｎｇ－ｈ...     

Study on the Application of Polysiloxane with N－decanyltartrimide Moieties in Capillary Electrophoresis

ＳｔｕｄｙｏｎｔｈｅＡｐｐｌｉｃａｔｉｏｎｏｆＰｏｌｙｓｉｌｏｘａｎｅｗｉｔｈＮ－ｄｅｃａｎｙｌｔａｒｔｒｉｍｉｄｅＭｏｉｅｔｉｅｓｉｎＣａｐｉｌｌａｒｙＥｌｅｃｔｒｏｐｈｏｒｅｓｉｓＳｔｕｄｙｏｎｔｈｅＡｐｐｌｉｃａｔｉｏｎｏｆＰｏｌｙｓｉｌｏｘａ...     

An Oscillation Condition for an Electrode－separated Piezoelectric Sensor in Non－electrolyte Liquid

ＡｎＯｓｃｉｌｌａｔｉｏｎＣｏｎｄｉｔｉｏｎｆｏｒａｎＥｌｅｃｔｒｏｄｅ－ｓｅｐａｒａｔｅｄＰｉｅｚｏｅｌｅｃｔｒｉｃＳｅｎｓｏｒｉｎＮｏｎ－ｅｌｅｃｔｒｏｌｙｔｅＬｉｑｕｉｄＳＨＥＮＤａ－ｚｈｏｎｇ，ＨＵＡＮＧＭｉｎｇ－ｓｈａｎ，ＬＩＮＳｏｎｇ，Ｎ...     

A Study on Molybdenite Electronic Structure

ＡＳｔｕｄｙｏｎＭｏｌｙｂｄｅｎｉｔｅＥｌｅｃｔｒｏｎｉｃＳｔｒｕｃｔｕｒｅＬＯＮＧＸｉａｎｇ－ｙｕｎａｎｄＷＡＮＧＦｅｎｇ－ｚｈｅｎ（Ｄｅｐｔ．ｏｆＣｈｅｍ．，ＣｅｎｔｒａｌＳｏｕｔｈＵｎｉｖｅｒｓｉｔｙｏｆＴｅｃｈｎｏｌｏｇｙ，Ｃｈａｎｇｓｈａｈ...     

Electron Ionization Mass Spectrometry of Some Ferrocenyl Thia-crown Ethers

ＥｌｅｃｔｒｏｎＩｏｎｉｚａｔｉｏｎＭａｓＳｐｅｃｔｒｏｍｅｔｒｙｏｆＳｏｍｅＦｅｒｒｏｃｅｎｙｌＴｈｉａ┐ｃｒｏｗｎＥｔｈｅｒｓＳＵＪｉｎｇ－ｚｈｅａｎｄＪＵＹｉｎｇ（ＢｅｉｊｉｎｇＩｎｓｔｉｔｕｔｅｏｆＣｈｅｍｉｃａｌＲｅａｇｅｎｔｓ，Ｂｅｉｊｉ...     

Quantum Chemistry Studies on the Heteropoly Blues of Molybdosilic Series with α-Keggin Structure

ＱｕａｎｔｕｍＣｈｅｍｉｓｔｒｙＳｔｕｄｉｅｓｏｎｔｈｅＨｅｔｅｒｏｐｏｌｙＢｌｕｅｓｏｆＭｏｌｙｂｄｏｓｉｌｉｃＳｅｒｉｅｓｗｉｔｈα－ＫｅｇｇｉｎＳｔｒｕｃｔｕｒｅＦＵＱｉａｎｇ,ＹＡＮＧＭｉｎｇ,ＣＨＥＮＢｉｎ,ＷＡＮＣＥｎ－Ｂｏ,ＸＩＥＤｅ－...     

’96贵金属电镀技术研讨会与青年电镀工作者学术交流会胜利闭幕

’９６贵金属电镀技术研讨会与青年电镀工作者学术交流会胜利闭幕’９６ＳｙｍｐｏｓｉｕｍｏｎＥｌｅｃｔｒｏｐｌａｔｉｎｇｏｆＮｏｂｌｅＭｅｔａｌｓ＆ＡｃａｄｅｍｉｃＭｅｅｔｉｎｇｏｆＹｏｕｔｈＥｌｅｃｔｒｏｐｌａｔｅｒｓｈａｓＣｏｍｅｔｏＡＳｕｃｅｓｆｕ...     

THE TESTS AND MECHANISM ABOUT SODIUM IONS FROM AN ANION EXCHANGER

ＴＨＥＴＥＳＴＳＡＮＤＭＥＣＨＡＮＩＳＭＡＢＯＵＴＳＯＤＩＵＭＩＯＮＳＦＲＯＭＡＮＡＮＩＯＮＥＸＣＨＡＮＧＥＲＺｈｕＸｉｎｇｂａｏ；ＬｉｕＺｈｏｎｇｘｉｕ（ＥｌｅｃｔｒｉｃＰｏｗｅｒＴｅｓｔａｎｄＲｅｓｅａｒｃｈＩｎｓｔｉｔｕｔｅｏｆＨｕｂｅｉＰｒｏ...     

Amperometric enzyme-modified electrodes based on tetrathiafulvalene derivatives for the determination of glucose

A number of tetrathiafulvalene (TTF) derivatives have been synthesized and tested as electron transfer mediators in glucose oxidase-based amperometric biosensors. Using cyclic voltammetry and stationary potential experiments, it is shown that several of these derivatives can effectively mediate electron transfer from the reduced flavin adenine dinucleotide redox centers of glucose oxidase to a conventional carbon paste electrode. An insoluble polymeric electron relay system, based on the covalent attachment of TTF moieties to a highly flexible siloxane polymer, is also shown to facilitate a flow of electrons from the enzyme to the electrode. The resulting glucose biosensors function efficiently over a clinically relevant range of glucose concentrations.     

Redox dependent conformational changes in the mixed valence form of the cytochrome c oxidase from p. The reorganization of glutamic acid 278 is coupled to the electron transfer from/to heme a and the binuclear center. denitrificans

In this work we present the separation of FTIR difference signals induced by electron transfer to/from the redox centers of the cytochrome c oxidase from P. denitrificans and compare electrochemically induced FTIR difference spectra with those induced by CO photolysis. FTIR difference spectra of rebinding of CO to the half reduced (mixed valence) form of the cytochrome c oxidase after photolysis reflect the conformational changes induced by the rebinding of CO and by electron transfer reactions from heme a3 to heme a and further on to CUA. During this process, heme a3 (and CUB) are oxidized, whereas heme a and CuA are reduced. By subtracting these difference spectra from an electrochemically induced FTIR difference spectrum, where all four cofactors are reduced, the contributions for heme a3 (and CuB) could be separated. Correspondingly, the spectral contributions of heme a and CuA have been separated. The comparison of these spectra with the spectra calculated for the hemes on the basis of their redox dependent changes previously published in Hellwig et al., (Biochemistry 38, (1999) 1685-1694) show a high degree of similarity, except for additional signals coupled to the reorganization of the binuclear center upon CO rebinding. The separated spectra clearly show that the signals attributed to Glu278, an amino acid discussed to be crucial for proton pumping, is coupled to electron transfer to/from heme a and the binuclear heme a3-CuB center.     

Basic and applied features of multicopper oxidases, CueO, bilirubin oxidase, and laccase

Multicopper oxidases (MCOs) such as CueO, bilirubin oxidase, and laccase contain four Cu centers, type 1 Cu, type II Cu, and a pair of type III Cu's in a protein molecule consisting of three domains with homologous structure to cupredoxin containing only type I Cu. Type I Cu mediates electron transfer between the substrate and the trinuclear Cu center formed by a type II Cu and a pair of type III Cu's, where the final electron acceptor O(2) is converted to H(2)O without releasing activated oxygen species. During the process, O(2) is reduced by MCOs such as lacquer laccase and bilirubin oxidase; the reaction intermediate II with a possible doubly OH(-)-bridged structure in the trinuclear Cu center has been detected. The preceding reaction intermediate I has been detected by the reaction of the lacquer laccase in a mixed valence state, at which type I Cu was cuprous and the trinuclear Cu center was fully reduced, and by the reaction of the Cys --> Ser mutant for the type I Cu site in bilirubin oxidase and CueO. An acidic amino acid residue located adjacent to the trinuclear Cu center was proved to function as a proton donor to these reaction intermediates. The substrate specificity of MCO for organic substrates is produced by the integrated effects of the shape of the substrate-binding site and the specific interaction of the substrate with the amino acid located adjacent to the His residue coordinating to the type I Cu. In contrast, the substrate specificity of the cuprous oxidase, CueO, is produced by the segment covering the Cu(I)-binding site so as to obstruct the access of organic substrates. Truncating the segment spanning helix 5 to helix 7 greatly reduced the specificity of CueO for Cu(I) and prominently enhanced the low oxidizing activity for the organic substrates, indicating the success of protein engineering to modify the substrate specificity of MCO.     

Effect of Gold Nanoparticles on the Structure and Electron‐Transfer Characteristics of Glucose Oxidase Redox Polyelectrolyte‐Surfactant Complexes

Efficient electrical communication between redox proteins and electrodes is a critical issue in the operation and development of amperometric biosensors. The present study explores the advantages of a nanostructured redox‐active polyelectrolyte–surfactant complex containing [Os(bpy)₂Clpy]²⁺ (bpy=2,2′‐bipyridine, py= pyridine) as the redox centers and gold nanoparticles (AuNPs) as nanodomains for boosting the electron‐transfer propagation throughout the assembled film in the presence of glucose oxidase (GOx). Film structure was characterized by grazing‐incidence small‐angle X‐ray scattering (GISAXS) and atomic force microscopy (AFM), GOx incorporation was followed by surface plasmon resonance (SPR) and quartz‐crystal microbalance with dissipation (QCM‐D), whereas Raman spectroelectrochemistry and electrochemical studies confirmed the ability of the entrapped gold nanoparticles to enhance the electron‐transfer processes between the enzyme and the electrode surface. Our results show that nanocomposite films exhibit five‐fold increase in current response to glucose compared with analogous supramolecular AuNP‐free films. The introduction of colloidal gold promotes drastic mesostructural changes in the film, which in turn leads to a rigid, amorphous interfacial architecture where nanoparticles, redox centers, and GOx remain in close proximity, thus improving the electron‐transfer process.     

Biosensors based on direct electron transfer in redox proteins

In biosensors based on direct electron transfer in redox proteins, efficient electron-transfer pathways between the immobilized redox protein and the electrode surface have to be established so to allow a fast electron transfer and concomitantly avoiding free-diffusing redox species. In this review, prerequisites for the direct electron transfer of redox proteins and immobilization of redox proteins on the electrode surfaces are addressed. Based on the specific nature of different proteins and non-manual immobilization procedures, possible biosensor designs are discussed, namely biosensors based on (1) ferritin; (2) cytochrome c; (3) myoglobin; (4) hemoglobin; (5) horseradish peroxidase; (6) catalase; (7) glucose oxidase; and (8) xanthine oxidase.     

TRIPLET STATE STUDIES OF FLAVlNS BY ELECTRON PARAMAGNETIC RESONANCE—II

Abstract— The triplet states of proteins, bovine serum albumin, ovalbumin and d-amino acid oxidase, were observed by electron paramagnetic resonance at 77°K.
The triplet state of aromatic amino acids, tryptophan, tyrosine and phenylalanine was also detected.
The protein triplet originates from the tryptophan residues of these proteins.
It is suggested that an energy transfer takes place between tyrosine and tryptophan.     

Atomic structure of the highest molecular orbitals of small tetra-heme cytochrome <Emphasis Type="Italic">c</Emphasis> 1M1P

The atomic structure of the highest molecular orbitals (MO) of small tetra-heme cytochrome (STC) c 1M1P is studied in large-scale ab initio all-electrons Hartree–Fock calculations. It is shown that the highest MOs of STC are mainly formed by atomic orbitals of negatively charged amino acid atoms whose types and corresponding numbers are determined. The results obtained permit the conclusion that these amino acids can be considered as possible active centers in the electron transfer reaction between STC and an external electron acceptor.     

Quinone-modified polymers as electron transfer relay systems in amperometric glucose sensors

A polysiloxane and an acrylonitrile–ethylene copolymer with covalently attached p-hydroquinone/benzoquinone moieties were prepared and tested as electron transfer relay systems in amperometric glucose biosensors. Using experiments involving cyclic voltammetry and stationary potential measurements, it was shown that the polysiloxane relay system can efficiently mediate electron transfer from reduced glucose oxidase to a conventional carbon-paste electrode. Sensors containing this polymeric relay system and glucose oxidase respond rapidly to low (<0.1 mm) glucose concentrations, with steady state current responses achieved in less than 1 min. The acrylonitrile–ethylene copolymer was found to be less efficient than the polysiloxane system at mediating the electron transfer from reduced glucose oxidase to the electrode. The dependence of the sensor response on the nature of the polymer backbone is discussed.     

Electrochemical approach to the dynamics of molecular recognition of redox enzyme sites by artificial cosubstrates in solution and in integrated systems

Application of antigen-antibody technology allows the attachment to an electrode surface of an enzyme monolayer structure to which both the enzyme and the mediator are bound. As illustrated with the example of glucose oxidase and a ferrocene mediator, the enzyme preserves its full activity in such structures, which may be easily reproduced. In spite of their fixation to the structure, the mobility of the ferrocene heads is sufficient to ensure that its transport to the enzyme prosthetic group is not rate determining. The reaction is rather controlled by the prior formation of a complex between the ferrocenium ion and the flavin required for electron transfer to occur. The efficiency of this step is affected by steric hindrance and the various observations made with free-moving and attached ferrocene-ended poly(ethylene glycol) chains may be rationalized by the interplay of factors controlling their distribution and shape. Analyzing the dynamics of this system, in comparison with previous systems, was thus an occasion to shed further light on the recognition phenomenon. The enzyme monolayer integrated system is a good starting point for the step-by-step construction of spatially ordered multilayered assemblies with strong catalytic efficiencies. Fast responding systems are expected both in terms of electron transport and electron transfer between the mediator and the enzyme. The spatial order resulting from the step-by-step construction should allow a much more precise analysis of electron transport and electron transfer than in conventional assemblies of redox centers. Mastering both the construction and the functioning of such systems should help the design of more complex systems, integrating additional functionalities electrically controlled by means of their electron transport/electron transfer connection to the electrode surface.     

基于蛋白质直接电子转移的全胆固醇传感器

以壳聚糖为载体, 将血红蛋白、胆固醇氧化酶及胆固醇酯酶固定在玻碳电极表面, 在不使用任何电子媒介体的条件下, 利用血红蛋白和电极之间的直接电子转移, 制备出高选择性的全胆固醇生物传感器, 并用于测定血清中总胆固醇含量. 利用循环伏安法和恒电位法研究了该传感器的电化学特性. 在优化的实验条件下, 该传感器对胆固醇响应的线性范围为10~110 mg/dL, 检出限为5 mg/dL(信噪比的3倍), 响应时间为60 s. 对人血清中总胆固醇的测定表明, RSD小于6.2%, 回收率为95%~106%.