ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTSynthesis and Structure of Platinum-Tungsten and -Molybdenum Heterodinuclear Complexes with Alkyl and Aryl Ligands: Mechanistic Study of the Migration of Alkyl and Aryl Groups from Platinum to Tungsten and MolybdenumAtsushi Fukuoka, Takanori Sadashima, Isao Endo, Nobutoshi Ohashi, Yutaka Kambara, Takeshi Sugiura, Kunio Miki, Nobutami Kasai, and Sanshiro KomiyaCite this: Organometallics 1994, 13, 10, 4033–4044Publication Date (Print):October 1, 1994Publication History Published online1 May 2002Published inissue 1 October 1994https://pubs.acs.org/doi/10.1021/om00022a046https://doi.org/10.1021/om00022a046research-articleACS PublicationsRequest reuse permissionsArticle Views170Altmetric-Citations44LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the Altmetric Attention Score and how the score is calculated. Share Add toView InAdd Full Text with ReferenceAdd Description ExportRISCitationCitation and abstractCitation and referencesMore Options Share onFacebookTwitterWechatLinked InRedditEmail Other access optionsGet e-AlertscloseSupporting Info (1)»Supporting Information Supporting Information Get e-Alerts
Abstract SoxR, a member of the MerR (mercury resistance regulator) family, is a transcriptional activator that contains a [2Fe‐2S] cluster. In entric bacteria, SoxR functions as an oxidative‐stress sensor. However, in other nonentric bacteria, its physiological role appears to be different. SoxR is activated by reversible one‐electron oxidation of the [2Fe‐2S] cluster. In the active state, SoxR and other MerR family proteins activate transcription from unique promoters, which have a long 19 or 20 bp spacer between the −35 and −10 operator elements, by untwisting the promoter DNA. The crystal structures of SoxR and its complex with the target promoter in the oxidized (active) state have been reported. The structure of SoxR monomer consists of a winged helix‐turn helix DNA‐binding domain, a dimerization helix, and a Fe‐S cluster‐binding domain. The SoxR dimer is formed by an antiparallel long coiled coil. The [2Fe‐2S] cluster of SoxR is completely solvent‐exposed and surrounded by an asymmetric environment stabilized by interaction with the other subunit. The asymmetrically charged environment of the [2Fe‐2S] cluster probably causes redox‐dependent conformational changes of SoxR. The structure of the SoxR‐DNA complex provides a structural framework of the transcriptional activation by DNA distortion in the MerR family.
Formaldehyde dismutase (FDM) exhibits the catalysis of the dismutation of aldehydes and alcohol: aldehyde oxdoreduction in the absence of an exogenous electron acceptor.The crystal structure of FDM was determined at 2.3 Å resolution by multi-wavelength anomalous dispersion method.FDM is composed of four identical subunits with a molecular weight of 44,000.Each subunit contains 2 zinc atoms.Preliminary intensity data were collected using CuKα radiation from a rotating-anode X-ray generator (Rigaku ultraX 18HF) operated at 40kV 100mA.Crystals of FDM belong to the space group I41 with unit-cell dimensions of a = b = 89.74Å, c = 226.77Å and there are two molecules per asymetric unit.Intensity data of native crystal and anomalous dispersion data were collected using Synchrotron Radiation at SPring-8 BL38B1.Experimental phases were obtained with MAD method using 3 wavelengths.
General IncorporatedAssociationbiLelLes ln summary we found that the fibri1 stmctmes and fibnllanon kmetics m thL prese"Le of bice"s were difTereni stgroihcantfy fiom those m tlie absence ot blLells 2p-lo2 ra"{!asa{igts),
An entry from the Cambridge Structural Database, the world’s repository for small molecule crystal structures. The entry contains experimental data from a crystal diffraction study. The deposited dataset for this entry is freely available from the CCDC and typically includes 3D coordinates, cell parameters, space group, experimental conditions and quality measures.
