In last five decades, organophosphorus compounds have become significant because of the widespread uses as pesticides abutting a clear threat to people from the potential use of chemical weapon as nerve agents in the cold wars and terrorist activities. Sarin, tabun, soman, cyclosarin belong to organophosphorus compounds called nerve agents due to their biological interaction as powerful inhibitor of enzyme acetylcholinesterase (AChE) and rendered its neurological function, the underlying mechanism is discussed. The identification and detection of such toxic nerve agents using spectrometry, sensors including enzymatic assays is the prime target of recent researchers. Typically some antidotes like oxime derivatives are most common and are the light of hope for nerve gas exposure. The modern techniques applied for the discovery of new antidote and their way of action by reactivating the blocked nerve enzyme and the hidden mechanism of reactivation of AchE are explained.

Platinum group metals mediated thiolato compounds are highly susceptible for S-centered reactivity owing to high nucleophilicity and which is enormously significant in the point of its bioactivity and photoactivity. A series of oxygenation reactions of thiolate sulfur attached with platinum metals occurred with molecular O2 in varying conditions. A variety of sulfenates and sulfinates are produced depending on nature of starting substrate thiolato and the oxygenations are facile under harshly oxygen environment. There are numerous mechanistic paths for the oxygenation of platinum metals bonded thiolate S-center unlike the oxygenation reaction of organic sulphides. It is assumed that S-oxygenation occurs via the intramolecular and intermolecular dioxygen addition pathways. A number of mysterious photo-induced sulphur oxygenation and self-sensitization reactions of metal-thiolato to analogous oxygenate are also mentioned. These compounds show enzymatic catalytic activity and remarkable bioactivity also interaction with the biomolecules like DNA, which opens a new area for the researchers for designing novel heavier metals-sulfur-oxygenates compounds as metallodrugs.

Transition metal mediated thiolato compounds are highly vulnerable for S-centered oxidation due to its high nucleophilicity and which is immensely important in the point of its bio-activity. It is generally noticeable that a range of chemical changes occurred with molecular O2 and ruthenium thiolato metalloligands in varying conditions. These oxygenations are facile under strictly oxygen environment and produce mono and di sulfenato and/or sulfinato depending on the substrate thiolato. The numerous heteroatomic substituents of thiolato-S ligand have performed a vital task during the course of oxygenation producing oxygenated products as sulfenates, sulfinates and sulfones. There appear to be numerous mechanisms that are involved in the oxygenation process are considerably more complex. Some bizarre photo-induced S-center oxygenation of metal-thiolato to the sulfonated compound is also mentioned. The ruthenium sulfur compounds jointly with the S-oxygenates show remarkable bioactivity as well as enzymatic catalytic activity and interaction with the bio-molecules like DNA that opens a new theme for the researcher for design novel Ru-sulfur-oxygenates compounds as metallodrugs.

Correction for 'Iridium-mediated C-S bond activation and transformation: organoiridium(III) thioether, thiolato, sulfinato and thiyl radical compounds. Synthesis, mechanistic, spectral, electrochemical and theoretical aspects' by Ujjwal Das et al., Dalton Trans., 2015, 44, 8625-8639, DOI: 10.1039/C5DT00448A.

Herein, we report the effects of different electron-withdrawing groups (EWG) (-F) and electron-donating groups (EDG) (-OMe and -NH2) on main ligands (ppy) and ancillary (acac) of [Ir(ppy)(2)(acac)] [ppy = 2-phenylpyridine; acac = acetylacetonato] using seven complexes by DFT and TDDFT calculations. We find that irrespective of the substituents, absorption of ppy-substituted complexes is blue-shifted, while for the acac-substituted complexes, it is red-shifted. The calculations also show that the substitution of EWGs causes an overall drop in the frontier molecular orbital energy levels; however, we observed a reverse effect for EDGs. To calculate the radiative rate k(r), we considered the spin-orbit coupling matrix element (SOCME) (< T-1 vertical bar H-SOC|S-n >) between S-n (n = 1, 2, etc.) excited state and T-1, transition dipole moment (mu(S-n)), and the energy difference between excited singlet states S-n and T-1 state (Delta E(S-n - T-1)). To compare the temperature-independent nonradiative process, we considered SOC between T-1 and S-0 (< T-1 vertical bar H-SOC vertical bar S-0 >) and the energy gap between optimized T-1 and S-0 states. Furthermore, to formulate the temperature-dependent nonradiative rate, we computed the activation barrier (E-1) for the metal-to-ligand state ((MLCT)-M-3) to a metal-centered state ((MC)-M-3) conversion. The emission peaks show that the changes of triplet state T-1 from (MLCT)-M-3. (MC)-M-3 via transition states ((TS)-T-3) and (MLCT)-M-3 -> (1)GS (GS = ground state) via the (MC)-M-3/(1)GS minimum energy crossing point are not much affected by the nature of substituents in the ancillary and the main ligand. The order of E-1 for the investigated complexes indicates that electron-donating substituents -OMe at both ppy and acac ligands can cause a decrease in nonradiative rate constants. Natural transition orbitals of the complexes show that they are mainly localized on the main ligand ppy and the Ir atoms and hardly on the ancillary ligand acac.

Reactions of alkyl/aryl (2-pyridylimine)phenyl thioether (LSR) with RuCl2(PPh3)3 in ethanolic medium afford thioether complexes of type [Ru(L-SR)Cl(PPh3)(2)]PF6 (R = benzyl, phenyl). The ligands behave as tridentate neutral NpyNimineSthioether donor retaining the C-S bond and bind to the metal atom in meridional fashion. The complexes were characterized by spectroscopic (IR, UV-Vis, and NMR) techniques. Crystallographic analysis reveals the octahedral geometry around ruthenium(H) with N2SP2Cl coordination. Complexes display rich optoelectronic features including luminescence. The complexes are electro-active and show quasi-reversible response near 1.1 V vs SCE. Theoretical (DFT) analyses were performed to explore the electronic transition and electron transfer behaviour.

InterPro (http://www.ebi.ac.uk/interpro/) is a database that integrates diverse information about protein families, domains and functional sites, and makes it freely available to the public via Web-based interfaces and services. Central to the database are diagnostic models, known as signatures, against which protein sequences can be searched to determine their potential function. InterPro has utility in the large-scale analysis of whole genomes and meta-genomes, as well as in characterizing individual protein sequences. Herein we give an overview of new developments in the database and its associated software since 2009, including updates to database content, curation processes and Web and programmatic interfaces.

The InterPro database (http://www.ebi.ac.uk/interpro/) integrates together predictive models or 'signatures' representing protein domains, families and functional sites from multiple, diverse source databases: Gene3D, PANTHER, Pfam, PIRSF, PRINTS, ProDom, PROSITE, SMART, SUPERFAMILY and TIGRFAMs. Integration is performed manually and approximately half of the total approximately 58,000 signatures available in the source databases belong to an InterPro entry. Recently, we have started to also display the remaining un-integrated signatures via our web interface. Other developments include the provision of non-signature data, such as structural data, in new XML files on our FTP site, as well as the inclusion of matchless UniProtKB proteins in the existing match XML files. The web interface has been extended and now links out to the ADAN predicted protein-protein interaction database and the SPICE and Dasty viewers. The latest public release (v18.0) covers 79.8% of UniProtKB (v14.1) and consists of 16 549 entries. InterPro data may be accessed either via the web address above, via web services, by downloading files by anonymous FTP or by using the InterProScan search software (http://www.ebi.ac.uk/Tools/InterProScan/).

The ligating properties of alkyl 2-(phenylazo)phenyl thioether 1 (HL(R); R = Me, CH(2)Ph) toward Rh(III) have been examined. A novel hexacoordinated orthometalated rhodium(III) thiolato complex trans-[Rh(L)Cl(PPh3)2] 5 has been synthesized from 1 and RhCl(3).3H(2)O in the presence of excess PPh(3) via in situ C(sp(2))-H and C(sp(3))-S bond scissions, which is the first example for a coordination compound of [L](2-). We were also able to isolate the intermediate organothioether rhodium(III) compound trans-[Rh(L(R))Cl(2)(PPh(3))] 6 with 1 equiv of PPh(3) relative to both 1 and RhCl(3).3H2O in the course of the synthesis of the S-dealkylated product. PPh(3) plays a crucial role in the C(sp(3))-S cleavage process. A plausible mechanistic pathway is presented for C-S bond cleavage, and reductive cleavage by single-electron transfer mechanism is likely to be operative. The electronically and coordinatively saturated thiolato complex 5, indefinitely stable in the solid state, undergoes spontaneous self-dimerization in solution via dissociation of one coordinated PPh3 molecule to afford edge-shared bioctahedral anti-[Rh(L)Cl(PPh(3))]2 7 and syn-[Rh(L)Cl(PPh(3))]2 8 isomers. All the synthesized organosulfur rhodium(III) compounds were isolated as both air- and moisture-stable solids and spectroscopically characterized in both solution and solid states. In addition, all the representative members have been authenticated by single-crystal X-ray structure analyses. Availability of the isomeric dimers provides an opportunity to recognize the presence of noncovalent intramolecular "metallochelate-metallochelate" interaction in the sterically encumbered syn isomer. Unlike other organosulfur rhodium complexes, the monomeric thiolato complex 5 exhibits a fully reversible oxidative wave at 0.82 V vs Ag/AgCl, which is supposed to be primarily centered on the thiolato sulfur atom, and such perception is consistent with the DFT study. Formation of rhodium-bound thiyl radical cation 5(*+) by electrochemical oxidation was scrutinized by EPR spectroscopy.

InterPro is an integrated resource for protein families, domains and functional sites, which integrates the following protein signature databases: PROSITE, PRINTS, ProDom, Pfam, SMART, TIGRFAMs, PIRSF, SUPERFAMILY, Gene3D and PANTHER. The latter two new member databases have been integrated since the last publication in this journal. There have been several new developments in InterPro, including an additional reading field, new database links, extensions to the web interface and additional match XML files. InterPro has always provided matches to UniProtKB proteins on the website and in the match XML file on the FTP site. Additional matches to proteins in UniParc (UniProt archive) are now available for download in the new match XML files only. The latest InterPro release (13.0) contains more than 13 000 entries, covering over 78% of all proteins in UniProtKB.

InterPro, an integrated documentation resource of protein families, domains and functional sites, was created to integrate the major protein signature databases. Currently, it includes PROSITE, Pfam, PRINTS, ProDom, SMART, TIGRFAMs, PIRSF and SUPERFAMILY. Signatures are manually integrated into InterPro entries that are curated to provide biological and functional information. Annotation is provided in an abstract, Gene Ontology mapping and links to specialized databases. New features of InterPro include extended protein match views, taxonomic range information and protein 3D structure data. One of the new match views is the InterPro Domain Architecture view, which shows the domain composition of protein matches. Two new entry types were introduced to better describe InterPro entries: these are active site and binding site. PIRSF and the structure-based SUPERFAMILY are the latest member databases to join InterPro, and CATH and PANTHER are soon to be integrated. InterPro release 8.0 contains 11 007 entries, representing 2573 domains, 8166 families, 201 repeats, 26 active sites, 21 binding sites and 20 post-translational modification sites. InterPro covers over 78% of all proteins in the Swiss-Prot and TrEMBL components of UniProt. The database is available for text- and sequence-based searches via a webserver ( http://www.ebi.ac.uk/interpro ), and for download by anonymous FTP ( ftp://ftp.ebi.ac.uk/pub/databases/interpro ).

Integr8 is a new web portal for exploring the biology of organisms with completely deciphered genomes. For over 190 species, Integr8 provides access to general information, recent publications, and a detailed statistical overview of the genome and proteome of the organism. The preparation of this analysis is supported through Genome Reviews, a new database of bacterial and archaeal DNA sequences in which annotation has been upgraded (compared to the original submission) through the integration of data from many sources, including the EMBL Nucleotide Sequence Database, the UniProt Knowledgebase, InterPro, CluSTr, GOA and HOGENOM. Integr8 also allows the users to customize their own interactive analysis, and to download both customized and prepared datasets for their own use. Integr8 is available at http://www.ebi.ac.uk/integr8 .

InterPro, an integrated documentation resource of protein families, domains and functional sites, was created in 1999 as a means of amalgamating the major protein signature databases into one comprehensive resource. PROSITE, Pfam, PRINTS, ProDom, SMART and TIGRFAMs have been manually integrated and curated and are available in InterPro for text- and sequence-based searching. The results are provided in a single format that rationalises the results that would be obtained by searching the member databases individually. The latest release of InterPro contains 5629 entries describing 4280 families, 1239 domains, 95 repeats and 15 post-translational modifications. Currently, the combined signatures in InterPro cover more than 74% of all proteins in SWISS-PROT and TrEMBL, an increase of nearly 15% since the inception of InterPro. New features of the database include improved searching capabilities and enhanced graphical user interfaces for visualisation of the data. The database is available via a webserver (http://www.ebi.ac.uk/interpro) and anonymous FTP (ftp://ftp.ebi.ac.uk/pub/databases/interpro).