《世界科技研究与发展》2006年总目录

第一期院士论坛发展循环经济,建设有中国特色的生态工业园区……………………………………………程会强左铁镛(1)专题:生物工程血红素蛋白结构及功能的相互转换……………………………………………………………林英武黄仲贤(8)以DNA为模板构筑纳米材料与分子器件………………………………姜辉李洪祥杨贤金胡文平等(14)基于DNA分子的逻辑门与计算机……………………………………………………俞洋宋世平樊春海(23)科技前沿与学术评论应用于微结构制造自治系统的流程自动生成……………………………………………………………严利人(27)串珠…     

不同电子受体诱导活性污泥生物质内源减量

活性污泥法是世界上应用最广泛的污水处理工艺.该工艺在净化水质的同时会产生大量的剩余污泥,而剩余污泥处理处置已成为该工艺发展的瓶颈.尽管现有污泥减量技术能够降低污泥产量,但是这些技术自身涉及能量和化学品的消耗,有悖于可持续污水处理的理念.在新陈代谢中,细菌合成取决于电子传递过程中所产生的能量(三磷酸腺苷ATP).不同电子受体因电子传递路径差异导致能量产率不同而影响细菌产率.本研究基于上述分析,以低溶解氧活性污泥工艺为研究对象开展不同电子受体诱导污泥减量性能与机制研究.在低溶解氧下的活性污泥微生物种群结构中, 29.7%的微生物为缺氧菌,这些缺氧菌能够利用NO_x~-为电子受体.基于热力学电子当量模型及电子传递模型推导出:微生物利用NO_x~-作为电子受体时的能量(ATP)产量仅为以O_2为电子受体时的2/3.胞外蛋白质组学揭示:低溶解氧系统中,微生物胞外蛋白中涉及电子传递和质子传递的蛋白丰度为8%和4%;而传统活性污泥系统中这个比例仅为2.9%和2%. NO_x~-作为电子受体时,更多的蛋白参与了电子传递过程.在低溶解氧系统和常规活性污泥系统中具有氧化还原催化活性的蛋白占23.7%和10.7%.这证实微生物以NO_x~-作为电子受体时电子传递活性更加活跃.电子受体的改变诱导了分解代谢与合成代谢之间的基质分配发生变化,微生物以NO_x~-作为电子受体参与细胞合成的电子供体fs明显小于O_2为电子受体的值.微生物以NO_x~-作为电子受体时,更少的能量和物质用于细胞合成,更多的能量被耗散掉.在无需额外的能量和资源消耗下,低溶解氧活性污泥系统获得15.4%的污泥减量效率.本研究成功地诱导微生物转换电子受体实现污泥减量.     

漫透射光谱电化学研究活菌细胞色素c蛋白介导的胞外电子传递过程

微生物膜蛋白(细胞色素c)介导的微生物胞外电子传递过程,是元素生物地球化学循环、微生物修复、微生物燃料电池等领域的研究热点与重要科学问题.阐明细胞色素c的氧化还原变化规律是从分子层面解析该过程的基础.然而,由于技术手段限制,活菌细胞色素c氧化态和还原态的含量及其电位难以同时测定,其氧化还原状态的变化规律仍知之甚少.本文构建了漫透射光谱电化学联用装置,原位测试了活菌细胞色素c及电子受体的氧化态和还原态含量变化,并同时在线监测了反应体系的氧化还原电位值,从而实现了实测电位与各反应物计算电位之间相互关系的系统研究.结合动力学与热力学的分析,定量阐明了细胞色素c所处的氧化还原状态因电子受体的电位不同而发生变化的规律;解释了不同电子受体存在时,细胞色素c所处的平衡状态截然不同的原因.该技术手段在活菌层面实现了细胞色素c蛋白的动力学与热力学分析,可为胞外电子传递微观机制的研究提供新的方法与理论基础.     

蜻蜓翅膀功能特性及其仿生研究进展

蜻蜓是自然界最优秀的飞行者之一,其通过翅膀的形态、构形、结构、材料等多个因素的相互耦合协同作用,展现出优异的功能特性,为航空航天飞行器和仿生微扑翼飞行器等的设计、研制和开发提供了天然的生物蓝本.近年来,国内外学者在蜻蜓翅翼的几何结构、材料特性、飞行机理及翅翼飞行时的控制方式等方面的研究取得了一定进展,有力助推了蜻蜓翅翼不同层面的仿生应用.本文简述了蜻蜓翅膀的飞行、自清洁、抗疲劳、消振降噪等功能特性,阐释了蜻蜓翅膀的形态、构形、结构、材料等与其功能特性之间的内在关系,分析了蜻蜓翅膀功能特性仿生研究的态势并展望了其应用前景.     

以镍/碳纳米管催化剂制备碳纳米管

碳纳米管由于具有较大的比表面积, 一定的化学稳定性, 其表面性质可以通过不同的酸或碱处理改变, 这决定了纳米碳管能够作为催化剂的载体材料. 通过对比碳纳米管负载的镍基催化剂和硅藻土负载的镍基催化剂在合成碳纳米管试验中的活性和选择性, 发现镍/碳纳米管催化剂合成的碳管直径均匀, 中空较大, 与镍/硅藻土催化剂合成的碳管质量相当, 但产量提高了1.5倍. 碳纳米管载体优异表现应归因于其较大的比表面积和合适的孔分布和孔结构.     

GeO2纳米线的原位热氧化法制备与发光性质

以Au作催化剂通过金属锗与纯氧在600～800℃的氧化反应,在单质锗表面原位大面积生长出了GeO2纳米线．采用X射线衍射仪、扫描电镜和透射电镜对产物进行了表征分析．结果表明,GeO2纳米线为六方相单晶结构,其直径在65～600nm范围内,长度达50gm．研究了反应温度和喷金时间对纳米线直径的影响,提出了可能的生长机理．实现了不同直径GeO2纳米线的可控合成．发现发光峰位于355nm强的紫外光发光和发光峰位于400nm和485nm弱的蓝光发光,这两种发光可能分别起源于GeO2纳米线中氧空位与间隙氧之间的跃迁和氧空位中的电子与锗．氧空穴中心的空穴复合．     

常重力和低重力条件下气液两相流实验研究

实验研究了常重力和低重力条件下水平方管内水气两相流型特征及其相互转换条件, 实验中均观察到了泡状流、弹状流、弹-环状过度流及环状流等流型. 发展了半理论Weber数模型以计入截面形状对弹状流-环状流转换的影响, 较好预测了实验观测结果. 此外, 滑移流率模型可成功预测大Froude数水平两相泡状流-弹状流间的转换边界.     

计量单位制及基本单位

一种计量单位制的核心是此种单位制所采用的基本单位。基本单位之间是互相独立的，而其他的所有单位均可由基本单位的适当组合来导出。本文论述了如何决定一种单位制中需要多少个相互独立的基本单位，不同的单位制之间如何相互转换这样一些有关单位制的基本问题。     

交叉学科研究推动了生物无机化学学科的发展

本文分为七部分，第一部分对生物无机化学学科发展进行历史回顾；第二部分从回顾史实中用实例表明生物无机化学的研究始终瞄准金属离子和生物配体控制生命过程中的化学问题；第三部分是介绍当今国际上研究核酸领域的争论焦点；第四部分是报导我们设计和合成了作为人工核酸酶的一系列新的配体以及许多不同金属的功能配合物；第五部分是讨论用动力学、热力学和DFT计算方法研究配合物和DNA相互作用的键合机制以及十多种影响因素；第六部分进一步报导配合物的生物功能和它们的应用探索，最后一部分提出在核酸领域的某些新的发展方向和途径。我们进一步提出了配合物的结构与DNA的作用机制以及它们的生物功能之间的规律性。通过配合物的结构改变去调控和改变配合物对DNA键合性质和生物功能。     

生物耦合功能特性及其实现模式

生物在大自然优胜劣汰的法则下, 进化出与自身生长和生存环境高度适应的功能特性. 生物通过两个或两个以上不同部分的协同作用或不同因素的耦合作用有效地实现生物的各种功能, 充分展现其对生境的最佳适应性. 本文从仿生学角度, 分析了生物耦合功能、特性及其类别, 初步揭示了生物耦合功能实现的机制与模式, 最后, 展望了生物耦合功能仿生实现的工程技术前景     

生物催化的Baeyer-Villiger氧化反应研究

生物转化具有底物选择性、立构选择性、化学选择性、对映选择性等一般化学反应中不具备的优点，在精细化工中占有很大的优势，其中Baeyer-Villiger氧化反应在生物转化中占有很重要的地位，产生的许多中间体或产物可以被用来生产多种化学产品和药物，在工业生物催化中有很好的应用前景。本文主要对生物转化中的Baeyer-Villiger氧化反应在利用酶或细胞作为催化剂时存在的问题和解决方法以及基因技术的运用近况进行了综述。     

Interaction of BW755C, a potent inhibitor of lipoxygenase and cyclo-oxygenase, with mitochondrial cytochrome oxidase

The interaction between BW755C (3-amino-1-[m-(trifluoromethyl)phenyl]-2-pyrazoline), a potent inhibitor of both lipoxygenase and cyclo-oxygenase, and respiratory chain in mitochondria and electron transport particles (ETP) from rat livers was examined. BW755C accelerated the oxygen uptake by mitochondria without the addition of substrate for the respiratory chain. Spectrophotometric study revealed that BW755C was quickly oxidized by cytochrome oxidase in mitochondria to a compound possessing an absorption maximum at 524 nm. p-Phenylenediamine (p-diaminobenzene, PPDA), which, like BW755C, serves as an electron donor to cytochrome oxidase, was shown to inhibit the generation of active oxygen in macrophages; the inhibition was stronger than that of BW755C. These results strongly suggest that the oxidative conversion of BW755C by mitochondrial cytochrome oxidase is associated with its potentially inhibitory action on the active oxygen-generating system in phagocytes.     

Structure and function of eukaryotic NAD(P)H:nitrate reductase

Pyridine nucleotide-dependent nitrate reductases (NRs; EC 1.6.6.1–3) are molybdenum-containing enzymes found in eukaryotic organisms which assimilate nitrate. NR is a homodimer with an ∼100 kDa polypeptide which folds into stable domains housing each of the enzyme's redox cofactors—FAD, heme-Fe molybdopterin (Mo-MPT) and the electron donor NAD(P)H—and there is also a domain for the dimer interface. NR has two active sites: the nitrate-reducing Mo-containing active site and the pyridine nucleotide active site formed between the FAD and NAD(P)H domains. The major barriers to defining the mechanism of catalysis for NR are obtaining the detailed three-dimensional structures for oxidized and reduced enzyme and more in-depth analysis of electron transfer rates in holo-NR. Recombinant expression of holo-NR and its fragments, including site-directed mutagenesis of key acative site and domain interface residues, are expected to make large contributions to this effort to understand the catalytic mechanism of NR.     

Zum Mechanismus der Propandioldehydrase-Reaktion

Summary Investigation of the propanediol dehydrase reaction with¹⁸O-labelled substrates indicates that the conversion of propane-1,2-diol to propionaldehyde involves transfer of the oxygen atom from C-2 to C-1. The dehydration of the so formed propane-1,1-diol is sterically controlled by the enzyme.     

Atom transfer mechanisms in oxidation processes

The emphasis placed on electron transfer in connection with oxidation reactions has often resulted in these processes being considered as a group apart from the main class of chemical reactions. Although some oxidations, for example certain exchange reactions between ions in solution, can be reasonably described as electron transfer processes, there are very many other oxidations, whose mechanisms are much better described in the familiar terms of modern organic chemistry.The use of isotopes as tracers has shown, that many oxidations proceed with transfer of atoms or groups from oxidant to reductant andvice versa; the use of the kinetic isotope effect has shown that such transfer is seldom an incidental process, but is almost always a part of the slow step of the reaction. In this paper, oxidations involving the transfer of such species as oxygen atoms, hydride ions, hydrogen atoms, chlorine atoms, and hydroxyl radicals are discussed in terms of mechanism. An attempt is made to show that a graded series of mechanisms is possible ranging from what appear to be pure electron transfer processes at one end to certain atom transfer processes at the other. The latter group belong, in fact, in the familiar realm of ordinary chemical raactions, in which strong bonds are being broken and formed in the activated complex.Contribution from Department of Chemistry, University of British Columbia, Vancouver. — Presented at the Organic Chemistry Symposium of the Chemical Institute of Canada, Ottawa, Dec. 8–9, 1958.     

Interaction of BW755C,a potent inhibitor of lipoxygenase and cyclo-oxygenase,with mitochondrial cytochrome oxidase

Summary The interaction between BW755C (3-amino-1-[m-(trifluoromethyl)phenyl]-2-pyrazoline), a potent inhibitor of both lipoxygenase and cyclo-oxygenase, and respiratory chain in mitochondria and electron transport particles (ETP) from rat livers was examined. BW755C accelerated the oxygen uptake by mitochondria without the addition of substrate for the respiratory chain. Spectrophotometric study revealed that BW755C was quickly oxidized by cytochrome oxidase in mitochondria to a compound possessing an absorption maximum at 524 nm. p-Phenylenediamine (p-diaminobenzene, PPDA), which, like BW755C, serves as an electron donor to cytoschrome oxidase, was shown to inhibit the generation of active oxygen in macrophages; the inhibition was stronger than that of BW755C. These results strongly suggest that the oxidative conversion of BW755C by mitochondrial cytochrome oxidase is associated with its potentially inhibitory action on the active oxygen-generating system in phagocytes.The authors are indebted to Dr M. Hori, Gifu College of Pharmacy and to Dr Y. Orii, Kyoto University for their kind supplies of BW755C and pure cytochrome oxidase, respectively.     

Type-2 copper-containing enzymes

Type-2 Cu sites are found in all the major branches of life and are often involved in the catalysis of oxygen species. Four type-2 Cu protein families are selected as model systems for review: amine oxidases, Cu monooxygenases, nitrite reductase/multicopper oxidase, and CuZn superoxide dismutase. For each model protein, the availability of multiple crystal structures and detailed enzymological studies provides a detailed molecular view of the type-2 Cu site and delineation of the mechanistic role of the Cu in biological function. Comparison of these model proteins leads to the identification of common properties of the Cu sites and insight into the evolution of the trinuclear active site found in multicopper oxidases. Received 6 July 2007; accepted 18 July 2007     

La biologie des hématinoprotéides oxygénables

Summary The author reviews a series of biological aspects of the study of oxygenable hematinoproteids, particularly with respect to evolution and adaptation. After a statement of some fundamental concepts of comparative biochemistry and of possible evolutionary relations between oxidation catalysts and oxygen carriers, the natural distribution of hemoglobins is reviewed and their specific characters are enumerated.A review is made of the data relating to the shape of the oxygen-dissociation curves and to the affinity of hæmoglobin for oxygen. It appears, generally speaking, that hyperbolic or almost hyperbolic curves and high affinity for oxygen are characteristic of primitive or embryonic hæmoglobins.A study of the function of hæmoglobin in the respiratory cycle of several animal species shows the vital importance of the oxygen carrier as well as the adaptation of the shape and position of the dissociation curve to the character of the respiratory function in the animal considered.The function of hæmoglobin in invertebrates, as oxygen carrier as well as providing a store of oxygen, is emphasized by a review of experimental data.The function of oxygen in the transport of carbon dioxide is reviewed from the standpoint of comparative biochemistry, and the lack of our knowledge is deplored.The characteristics of chlorocruorin show it to be a chemical mutation of an Annelid hæmoglobin.Our lack of knowledge in the field of the comparative biochemistry of hæmoglobin and chlorocruorin metabolism is pointed out.

---

---

Conférence principale, présentée à la Société suisse de biologie médicale lors de la 127^e Assemblée générale de la Société helvétique des sciences naturelles à Genève, le 31 août 1947.     

Structure to function relationships in ceruloplasmin: a 'moonlighting' protein

Specialised copper sites have been recruited during evolution to provide long-range electron transfer reactivity and oxygen binding and activation in proteins destined to cope with oxygen reactivity in different organisms. Ceruloplasmin is an ancient multicopper oxidase evolved to insure a safe handling of oxygen in some metabolic pathways of vertebrates. The presently available knowledge of its structure provides a glimpse of its plasticity, revealing a multitude of binding sites that point to an elaborate mechanism of multifunctional activity. Ceruloplasmin represents an example of a 'moonlighting' protein that overcomes the one gene-one structure-one function concept to follow the changes of the organism in its physiological and pathological conditions. Received 19 February 2002; received after revision 29 March 2002; accepted 2 April 2002 RID="*" ID="*"Corresponding author.     

On and beyond O2 binding: Hemoglobin and myoglobin revisited

The past decade of our laboratory's investigations into some aspects of heme proteins at first glance may seem marginal to the primary biological function of these proteins in O₂ binding and transport. But in fact, understanding long-range electron transfer mechanisms and the participation of hemoglobin and myoglobin in the generation of oxidative stress may provide relevant new biochemical insights.