Metal ions in life sciences最新文献

{"title":"Historical Development and Perspectives of the Series. Metal Ions in Life Sciences.","authors":"Astrid Sigel, Helmut Sigel, Roland K O Sigel","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":18698,"journal":{"name":"Metal ions in life sciences","volume":"15 ","pages":"vii-ix"},"PeriodicalIF":0.0,"publicationDate":"2015-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"33274543","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Sustaining Life on Planet Earth:Metalloenzymes Mastering Dioxygen and Other Chewy Gases.","authors":"Peter M H Kroneck, Martha E Sosa Torres","doi":"","DOIUrl":"","url":null,"abstract":"","PeriodicalId":18698,"journal":{"name":"Metal ions in life sciences","volume":"15 ","pages":"vii-ix"},"PeriodicalIF":0.0,"publicationDate":"2015-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"33274544","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Light-dependent production of dioxygen in photosynthesis.","authors":"Junko Yano, Jan Kern, Vittal K Yachandra, Håkan Nilsson, Sergey Koroidov, Johannes Messinger","doi":"10.1007/978-3-319-12415-5_2","DOIUrl":"10.1007/978-3-319-12415-5_2","url":null,"abstract":"<p><p>Oxygen, that supports all aerobic life, is abundant in the atmosphere because of its constant regeneration by photosynthetic water oxidation, which is catalyzed by a Mn₄CaO₅ cluster in photosystem II (PS II), a multi subunit membrane protein complex. X-ray and other spectroscopy studies of the electronic and geometric structure of the Mn₄CaO₅ cluster as it advances through the intermediate states have been important for understanding the mechanism of water oxidation. The results and interpretations, especially from X-ray spectroscopy studies, regarding the geometric and electronic structure and the changes as the system proceeds through the catalytic cycle will be summarized in this review. This review will also include newer methodologies in time-resolved X-ray diffraction and spectroscopy that have become available since the commissioning of the X-ray free electron laser (XFEL) and are being applied to study the oxygen-evolving complex (OEC). The femtosecond X-ray pulses of the XFEL allows us to outrun X-ray damage at room temperature, and the time-evolution of the photo-induced reaction can be probed using a visible laser-pump followed by the X-ray-probe pulse. XFELs can be used to simultaneously determine the light-induced protein dynamics using crystallography and the local chemistry that occurs at the catalytic center using X-ray spectroscopy under functional conditions. Membrane inlet mass spectrometry has been important for providing direct information about the exchange of substrate water molecules, which has a direct bearing on the mechanism of water oxidation. Moreover, it has been indispensable for the time-resolved X-ray diffraction and spectroscopy studies and will be briefly reviewed in this chapter. Given the role of PS II in maintaining life in the biosphere and the future vision of a renewable energy economy, understanding the structure and mechanism of the photosynthetic water oxidation catalyst is an important goal for the future.</p>","PeriodicalId":18698,"journal":{"name":"Metal ions in life sciences","volume":"15 ","pages":"13-43"},"PeriodicalIF":0.0,"publicationDate":"2015-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4688042/pdf/nihms744957.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"33076953","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Respiratory conservation of energy with dioxygen: cytochrome C oxidase.","authors":"Shinya Yoshikawa,&nbsp;Atsuhiro Shimada,&nbsp;Kyoko Shinzawa-Itoh","doi":"10.1007/978-3-319-12415-5_4","DOIUrl":"https://doi.org/10.1007/978-3-319-12415-5_4","url":null,"abstract":"<p><p>Cytochrome c oxidase (CcO) is the terminal oxidase of cell respiration which reduces molecular oxygen (O₂) to H2O coupled with the proton pump. For elucidation of the mechanism of CcO, the three-dimensional location and chemical reactivity of each atom composing the functional sites have been extensively studied by various techniques, such as crystallography, vibrational and time-resolved electronic spectroscopy, since the X-ray structures (2.8 Å resolution) of bovine and bacterial CcO have been published in 1995.X-ray structures of bovine CcO in different oxidation and ligand binding states showed that the O₂reduction site, which is composed of Fe (heme a 3) and Cu (CuB), drives a non-sequential four-electron transfer for reduction of O₂to water without releasing any reactive oxygen species. These data provide the crucial structural basis to solve a long-standing problem, the mechanism of the O₂reduction.Time-resolved resonance Raman and charge translocation analyses revealed the mechanism for coupling between O₂reduction and the proton pump: O₂is received by the O₂reduction site where both metals are in the reduced state (R-intermediate), giving the O₂-bound form (A-intermediate). This is spontaneously converted to the P-intermediate, with the bound O₂fully reduced to 2 O²⁻. Hereafter the P-intermediate receives four electron equivalents from the second Fe site (heme a), one at a time, to form the three intermediates, F, O, and E to regenerate the R-intermediate. Each electron transfer step from heme a to the O₂reduction site is coupled with the proton pump.X-ray structural and mutational analyses of bovine CcO show three possible proton transfer pathways which can transfer pump protons (H) and chemical (water-forming) protons (K and D). The structure of the H-pathway of bovine CcO indicates that the driving force of the proton pump is the electrostatic repulsion between the protons on the H-pathway and positive charges of heme a, created upon oxidation to donate electrons to the O₂reduction site. On the other hand, mutational and time-resolved electrometric findings for the bacterial CcO strongly suggest that the D-pathway transfers both pump and chemical protons. However, the structure for the proton-gating system in the D-pathway has not been experimentally identified. The structural and functional diversities in CcO from various species suggest a basic proton pumping mechanism in which heme a pumps protons while heme a 3 reduces O₂as proposed in 1978.</p>","PeriodicalId":18698,"journal":{"name":"Metal ions in life sciences","volume":"15 ","pages":"89-130"},"PeriodicalIF":0.0,"publicationDate":"2015-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/978-3-319-12415-5_4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"33076954","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Transition metal complexes and the activation of dioxygen.","authors":"Gereon M Yee,&nbsp;William B Tolman","doi":"10.1007/978-3-319-12415-5_5","DOIUrl":"https://doi.org/10.1007/978-3-319-12415-5_5","url":null,"abstract":"<p><p>In order to address how diverse metalloprotein active sites, in particular those containing iron and copper, guide O₂binding and activation processes to perform diverse functions, studies of synthetic models of the active sites have been performed. These studies have led to deep, fundamental chemical insights into how O₂coordinates to mono- and multinuclear Fe and Cu centers and is reduced to superoxo, peroxo, hydroperoxo, and, after O-O bond scission, oxo species relevant to proposed intermediates in catalysis. Recent advances in understanding the various factors that influence the course of O₂activation by Fe and Cu complexes are surveyed, with an emphasis on evaluating the structure, bonding, and reactivity of intermediates involved. The discussion is guided by an overarching mechanistic paradigm, with differences in detail due to the involvement of disparate metal ions, nuclearities, geometries, and supporting ligands providing a rich tapestry of reaction pathways by which O₂is activated at Fe and Cu sites.</p>","PeriodicalId":18698,"journal":{"name":"Metal ions in life sciences","volume":"15 ","pages":"131-204"},"PeriodicalIF":0.0,"publicationDate":"2015-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/978-3-319-12415-5_5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"33076956","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Methane monooxygenase: functionalizing methane at iron and copper.","authors":"Matthew H Sazinsky,&nbsp;Stephen J Lippard","doi":"10.1007/978-3-319-12415-5_6","DOIUrl":"https://doi.org/10.1007/978-3-319-12415-5_6","url":null,"abstract":"<p><p>Methane monooxygenases (MMOs) catalyze the conversion of methane to methanol as the first committed step in the assimilation of this hydrocarbon into biomass and energy by methanotrophs, thus playing a significant role in the biogeochemistry of this potent greenhouse gas. Two distinct enzymes, a copper-dependent membrane protein, particulate methane monooxygenase (pMMO), and an iron-dependent cytosolic protein, soluble methane monooxygenase (sMMO), carry out this transformation using large protein scaffolds that help to facilitate the timely transport of hydrocarbon, O₂, proton, and electron substrates to buried dimetallic active sites. For both enzymes, reaction of the reduced metal centers with O₂leads to intermediates that activate the relatively inert C-H bonds of hydrocarbons to yield oxidized products. Among synthetic and biological catalysts, MMOs are unique because they are the only ones known to hydroxylate methane at ambient temperatures. As a need for new industrial catalysts and green chemical transformations increases, understanding how the different MMO metal centers efficiently accomplish this challenging chemistry has become the focus of intense study. This chapter examines current understanding of the sMMO and pMMO protein structures, their methods for substrate channeling, and mechanisms for the dimetallic activation of O₂and C-H bonds.</p>","PeriodicalId":18698,"journal":{"name":"Metal ions in life sciences","volume":"15 ","pages":"205-56"},"PeriodicalIF":0.0,"publicationDate":"2015-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/978-3-319-12415-5_6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"33076957","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The magic of dioxygen.","authors":"Martha E Sosa Torres,&nbsp;Juan P Saucedo-Vázquez,&nbsp;Peter M H Kroneck","doi":"10.1007/978-3-319-12415-5_1","DOIUrl":"https://doi.org/10.1007/978-3-319-12415-5_1","url":null,"abstract":"<p><p>Oxygen has to be considered one of the most important elements on Earth. Earlier, some dispute arose as to which of the three scientists, Carl Wilhelm Scheele (Sweden), Joseph Priestley (United Kingdom) or Antoine Lavoisier (France), should get credit for the air of life.Today it is agreed that the Swede discovered it first, the fire air in 1772. The British chemist published it first, the dephlogisticated air in 1775, and the Frenchman understood it first, the oxygen in 1775-1778. Surely, there is credit enough for all three to split the \"Nobel Prize\" awarded by Carl Djerassi and Roald Hoffmann in their play Oxygen. Molecular oxygen means life. So-called aerobes - these include humans, animals, and plants - need O2 to conserve the energy they have to gain from their environment. Eliminate O2 and these organisms cannot support an active lifestyle. What makes dioxygen that special? It is a non-metal and oxidizing agent that readily reacts with most elements to form compounds, notably oxides. From a biological point of view, the most important compound of course is water, H2O, which provides an excellent solvent for biomolecules. It influences the climate of the Earth, and it is the source of almost all of the molecular oxygen in the atmosphere. </p>","PeriodicalId":18698,"journal":{"name":"Metal ions in life sciences","volume":"15 ","pages":"1-12"},"PeriodicalIF":0.0,"publicationDate":"2015-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/978-3-319-12415-5_1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"33076952","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The early Earth atmosphere and early life catalysts.","authors":"Sandra Ignacia Ramírez Jiménez","doi":"10.1007/978-94-017-9269-1_1","DOIUrl":"https://doi.org/10.1007/978-94-017-9269-1_1","url":null,"abstract":"<p><p>Homochirality is a property of living systems on Earth. The time, the place, and the way in which it appeared are uncertain. In a prebiotic scenario two situations are of interest: either an initial small bias for handedness of some biomolecules arouse and progressed with life, or an initial slight excess led to the actual complete dominance of the known chiral molecules. A definitive answer can probably never be given, neither from the fields of physics and chemistry nor biology. Some arguments can be advanced to understand if homochirality is necessary for the initiation of a prebiotic homochiral polymer chemistry, if this homochirality is suggesting a unique origin of life, or if a chiral template such as a mineral surface is always required to result in an enantiomeric excess. A general description of the early Earth scenario will be presented in this chapter, followed by a general description of some clays, and their role as substrates to allow the concentration and amplification of some of the building blocks of life. </p>","PeriodicalId":18698,"journal":{"name":"Metal ions in life sciences","volume":"14 ","pages":"1-14"},"PeriodicalIF":0.0,"publicationDate":"2014-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/978-94-017-9269-1_1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"32829905","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Transformations of dimethylsulfide.","authors":"Ulrike Kappler,&nbsp;Hendrik Schäfer","doi":"10.1007/978-94-017-9269-1_11","DOIUrl":"https://doi.org/10.1007/978-94-017-9269-1_11","url":null,"abstract":"<p><p>Dimethylsulfide (DMS) is a naturally occurring chemical that is part of the biogeochemical sulfur cycle and has been implicated in climate-relevant atmospheric processes. In addition, DMS occurs in soil environments as well as in food stuff as a flavor compound and it can also be associated with disease states such as halitosis. A major environmental source of DMS is the marine algal osmoprotectant dimethylsulfoniopropionate (DMSP). A variety of bacterial enzyme systems lead either to the production of DMS from DMSP or dimethylsulfoxide (DMSO) or its oxidation to, e.g., DMSO. The interconversion of DMS and DMSO is catalyzed by molybdenum-containing metalloenzymes that have been very well studied, and recently another enzyme system, an NADH-dependent, flavin-containing monooxygenase, that produces formaldehyde and methanethiol from DMS has also been described.DMS conversions are not limited to a specialized group of bacteria - evidence for DMS-based metabolism exists for heterotrophic, autotrophic and phototrophic bacteria and there is also evidence for the occurrence of this type of sulfur compound conversion in Archaea. </p>","PeriodicalId":18698,"journal":{"name":"Metal ions in life sciences","volume":"14 ","pages":"279-313"},"PeriodicalIF":0.0,"publicationDate":"2014-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/978-94-017-9269-1_11","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"32830853","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Carbon monoxide. Toxic gas and fuel for anaerobes and aerobes: carbon monoxide dehydrogenases.","authors":"Jae-Hun Jeoung,&nbsp;Jochen Fesseler,&nbsp;Sebastian Goetzl,&nbsp;Holger Dobbek","doi":"10.1007/978-94-017-9269-1_3","DOIUrl":"https://doi.org/10.1007/978-94-017-9269-1_3","url":null,"abstract":"<p><p>Carbon monoxide (CO) pollutes the atmosphere and is toxic for respiring organisms including man. But CO is also an energy and carbon source for phylogenetically diverse microbes living under aerobic and anaerobic conditions. Use of CO as metabolic fuel for microbes relies on enzymes like carbon monoxide dehydrogenase (CODH) and acetyl-CoA synthase (ACS), which catalyze conversions resembling processes that eventually initiated the dawn of life.CODHs catalyze the (reversible) oxidation of CO with water to CO2 and come in two different flavors with unprecedented active site architectures. Aerobic bacteria employ a Cu- and Mo-containing CODH in which Cu activates CO and Mo activates water and takes up the two electrons generated in the reaction. Anaerobic bacteria and archaea use a Ni- and Fe-containing CODH, where Ni activates CO and Fe provides the nucleophilic water. Ni- and Fe-containing CODHs are frequently associated with ACS, where the CODH component reduces CO2 to CO and ACS condenses CO with a methyl group and CoA to acetyl-CoA.Our current state of knowledge on how the three enzymes catalyze these reactions will be summarized and the different strategies of CODHs to achieve the same task within different active site architectures compared. </p>","PeriodicalId":18698,"journal":{"name":"Metal ions in life sciences","volume":"14 ","pages":"37-69"},"PeriodicalIF":0.0,"publicationDate":"2014-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/978-94-017-9269-1_3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"32832513","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}