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        <title>Coordination Chemistry Reviews via MedWorm.com</title>
        <description>MedWorm.com provides a medical RSS filtering service. Over 6000 RSS medical sources are combined and output via different filters. This feed contains the latest items from the 'Coordination Chemistry Reviews' source.</description>
        <link><![CDATA[http://www.medworm.com/rss/search.php?qu=Coordination+Chemistry+Reviews&t=Coordination+Chemistry+Reviews&s=Search&f=source]]></link>
        <lastBuildDate>Thu, 30 Jun 2011 05:26:34 +0100</lastBuildDate>
        <item>
            <title>Pterin chemistry and its relationship to the molybdenum cofactor.</title>
            <link>http://www.medworm.com/index.php?rid=4893956&amp;cid=s_37313_51_f&amp;fid=37313&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21607119%26dopt%3DAbstract</link>
            <description>This article describes the basic nomenclature of pterin, their biological roles, structure, chemical synthesis and redox reactivity. In addition, the biosynthesis of pterins and current models of the molybdenum cofactor are discussed.
    PMID: 21607119 [PubMed - as supplied by publisher] (Source: Coordination Chemistry Reviews)</description>
            <author>Coordination Chemistry Reviews</author>
            <type>journals</type>
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            <pubDate>Sat, 30 Apr 2011 23:00:00 +0100</pubDate>
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        <item>
            <title>Molybdenum enzymes in higher organisms.</title>
            <link>http://www.medworm.com/index.php?rid=4791917&amp;cid=s_37313_51_f&amp;fid=37313&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21516203%26dopt%3DAbstract</link>
            <description>Authors: Hille R, Nishino T, Bittner F
    Recent progress in our understanding of the structural and catalytic properties of molybdenum-containing enzymes in eukaryotes is reviewed, along with aspects of the biosynthesis of the cofactor and its insertion into apoprotein.
    PMID: 21516203 [PubMed - as supplied by publisher] (Source: Coordination Chemistry Reviews)</description>
            <author>Coordination Chemistry Reviews</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4791917</comments>
            <pubDate>Sat, 30 Apr 2011 23:00:00 +0100</pubDate>
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            <title>The History of the Discovery of the Molybdenum Cofactor and Novel Aspects of its Biosynthesis in Bacteria.</title>
            <link>http://www.medworm.com/index.php?rid=4791916&amp;cid=s_37313_51_f&amp;fid=37313&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21528011%26dopt%3DAbstract</link>
            <description>Authors: Leimkühler S, Wuebbens MM, Rajagopalan KV
    Biosynthesis of the molybdenum cofactor in bacteria is described with a detailed analysis of each individual reaction leading to the formation of stable intermediates during the synthesis of molybdopterin from GTP. As a starting point, the discovery of molybdopterin and the elucidation of its structure through the study of stable degradation products are described. Subsequent to molybdopterin synthesis, the molybdenum atom is added to the molybdopterin dithiolene group to form the molybdenum cofactor. This cofactor is either inserted directly into specific molybdoenzymes or is further modified by the addition of nucleotides to the molybdopterin phosphate group or the replacement of ligands at the molybdenum center.
    PMID: 21528011 ...</description>
            <author>Coordination Chemistry Reviews</author>
            <type>journals</type>
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            <pubDate>Sat, 30 Apr 2011 23:00:00 +0100</pubDate>
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            <title>Biosynthesis of Nitrogenase FeMoco.</title>
            <link>http://www.medworm.com/index.php?rid=4739829&amp;cid=s_37313_51_f&amp;fid=37313&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21503270%26dopt%3DAbstract</link>
            <description>Authors: Hu Y, Ribbe MW
    Biosynthesis of nitrogenase FeMoco is a highly complex process that requires, minimally, the participation of nifS, nifU, nifB, nifE, nifN, nifV, nifH, nifD and nifK gene products. Previous genetic analyses have identified the essential factors for the assembly of FeMoco; however, the exact functions of these factors and the precise sequence of events during the assembly process had remained unclear until recently, when a number of the biosynthetic intermediates of FeMoco were identified and characterized by combined biochemical, spectroscopic and structural analyses. This review gives a brief account of the recent progress toward understanding the assembly process of FeMoco, which has identified some important missing pieces of this biosynthetic puzzle.
    PMI...</description>
            <author>Coordination Chemistry Reviews</author>
            <type>journals</type>
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            <pubDate>Fri, 22 Apr 2011 23:15:14 +0100</pubDate>
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            <title>The H93G Myoglobin Cavity Mutant as a Versatile Scaffold for Modeling Heme Iron Coordination Structures in Protein Active Sites and Their Characterization with Magnetic Circular Dichroism Spectroscopy.</title>
            <link>http://www.medworm.com/index.php?rid=4627070&amp;cid=s_37313_51_f&amp;fid=37313&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D21423881%26dopt%3DAbstract</link>
            <description>Authors: Du J, Sono M, Dawson JH
    Preparation of heme model complexes is a challenging subject of long-standing interest for inorganic chemists. His93Gly sperm whale myoglobin (H93G Mb) has the proximal His replaced with the much smaller non-coordinating Gly. This leaves a cavity on the proximal side of the heme into which a wide variety of exogenous ligands can be delivered. The end result is a remarkably versatile scaffold for the preparation of model heme adducts to mimic the heme iron coordination structure of native heme proteins. In this review, we first summarize the quantitative evidence for differential ligand binding affinities of the proximal and distal pockets of the H93G Mb cavity mutant that facilitates the preparation of mixed-ligand derivatives. Then we review our use of...</description>
            <author>Coordination Chemistry Reviews</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=4627070</comments>
            <pubDate>Thu, 24 Mar 2011 08:00:19 +0100</pubDate>
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            <title>Porphyrins as Molecular Electronic Components of Functional Devices.</title>
            <link>http://www.medworm.com/index.php?rid=4056833&amp;cid=s_37313_51_f&amp;fid=37313&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20936084%26dopt%3DAbstract</link>
            <description>Authors: Jurow M, Schuckman AE, Batteas JD, Drain CM
    The proposal that molecules can perform electronic functions in devices such as diodes, rectifiers, wires, capacitors, or serve as functional materials for electronic or magnetic memory, has stimulated intense research across physics, chemistry, and engineering for over 35 years. Because biology uses porphyrins and metalloporphyrins as catalysts, small molecule transporters, electrical conduits, and energy transducers in photosynthesis, porphyrins are an obvious class of molecules to investigate for molecular electronic functions. Of the numerous kinds of molecules under investigation for molecular electronics applications, porphyrins and their related macrocycles are of particular interest because they are robust and their electroni...</description>
            <author>Coordination Chemistry Reviews</author>
            <type>journals</type>
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            <pubDate>Thu, 30 Sep 2010 23:00:00 +0100</pubDate>
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            <title>Metal-Carbon Bonds in Enzymes and Cofactors.</title>
            <link>http://www.medworm.com/index.php?rid=3896752&amp;cid=s_37313_51_f&amp;fid=37313&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20729977%26dopt%3DAbstract</link>
            <description>Authors: Ragsdale S
    
    PMID: 20729977 [PubMed - as supplied by publisher] (Source: Coordination Chemistry Reviews)</description>
            <author>Coordination Chemistry Reviews</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3896752</comments>
            <pubDate>Wed, 25 Aug 2010 03:18:05 +0100</pubDate>
            <guid isPermaLink="false">3896752</guid>        </item>
        <item>
            <title>Coordination chemistry of poly(thioether)borate ligands.</title>
            <link>http://www.medworm.com/index.php?rid=3741210&amp;cid=s_37313_51_f&amp;fid=37313&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20607091%26dopt%3DAbstract</link>
            <description>Authors: Riordan CG
    This review traces the development and application of the tris(thioether)borate ligands, tripodal ligands with highly polarizable thioether donors. Areas of emphasis include the basic coordination chemistry of the mid-to-late first row transition metals (Fe, Ni, Co, Cu), and the role of the thioether substituent in directing complex formation, the modeling of zinc thiolate protein active sites, high-spin organo-iron and organo-cobalt chemistry, the preparation of monovalent complexes of Fe, Co and Ni, and dioxygen and sulfur activation by monovalent nickel complexes.
    PMID: 20607091 [PubMed - as supplied by publisher] (Source: Coordination Chemistry Reviews)</description>
            <author>Coordination Chemistry Reviews</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3741210</comments>
            <pubDate>Sat, 10 Jul 2010 20:15:05 +0100</pubDate>
            <guid isPermaLink="false">3741210</guid>        </item>
        <item>
            <title>Electrochemistry of redox-active self-assembled monolayers.</title>
            <link>http://www.medworm.com/index.php?rid=3688102&amp;cid=s_37313_51_f&amp;fid=37313&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20563297%26dopt%3DAbstract</link>
            <description>Authors: Eckermann AL, Feld DJ, Shaw JA, Meade TJ
    Redox-active self-assembled monolayers (SAMs) provide an excellent platform for investigating electron transfer kinetics. Using a well-defined bridge, a redox center can be positioned at a fixed distance from the electrode and electron transfer kinetics probed using a variety of electrochemical techniques. Cyclic voltammetry, AC voltammetry, electrochemical impedance spectroscopy, and chronoamperometry are most commonly used to determine the rate of electron transfer of redox-activated SAMs. A variety of redox species have been attached to SAMs, and include transition metal complexes (e.g., ferrocene, ruthenium pentaammine, osmium bisbipyridine, metal clusters) and organic molecules (e.g., galvinol, C(60)). SAMs offer an ideal environme...</description>
            <author>Coordination Chemistry Reviews</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3688102</comments>
            <pubDate>Thu, 24 Jun 2010 00:33:07 +0100</pubDate>
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            <title>Electron tunneling through sensitizer wires bound to proteins.</title>
            <link>http://www.medworm.com/index.php?rid=3284207&amp;cid=s_37313_51_f&amp;fid=37313&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20161508%26dopt%3DAbstract</link>
            <description>We report a quantitative theoretical analysis of long-range electron transfer through sensitizer wires bound in the active-site channel of cytochrome P450cam. Each sensitizer wire consists of a substrate group with high binding affinity for the enzyme active site connected to a ruthenium-diimine through a bridging aliphatic or aromatic chain. Experiments have revealed a dramatic dependence of electron transfer rates on the chemical composition of both the bridging group and the substrate. Using combined molecular dynamics simulations and electronic coupling calculations, we show that electron tunneling through perfluorinated aromatic bridges is promoted by enhanced superexchange coupling through virtual reduced states. In contrast, electron flow through aliphatic bridges occurs by hole-med...</description>
            <author>Coordination Chemistry Reviews</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3284207</comments>
            <pubDate>Mon, 01 Feb 2010 00:00:00 +0100</pubDate>
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            <title>The tumor proteasome as a novel target for gold(III) complexes: implications for breast cancer therapy.</title>
            <link>http://www.medworm.com/index.php?rid=3146525&amp;cid=s_37313_51_f&amp;fid=37313&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D20047011%26dopt%3DAbstract</link>
            <description>Authors: Milacic V, Dou QP
    Although cisplatin plays a vital role in the treatment of several types of human cancer, its wide use is limited by the development of drug resistance and associated toxic side effects. Gold and gold complexes have been used to treat a wide range of ailments for many centuries. In recent years, the use of gold(III) complexes as an alternative to cisplatin treatment was proposed due to the similarities of gold and platinum. Gold(III) is isoelectronic with platinum(II) and gold(III) complexes have the same square-planar geometries as platinum(II) complexes, such as cisplatin. Although it was originally thought that gold(III) complexes might have the same molecular target as cisplatin, several lines of data indicated that proteins, rather than DNA, are targeted ...</description>
            <author>Coordination Chemistry Reviews</author>
            <type>journals</type>
        <comments>http://www.medworm.com/rss/comments.php?id=3146525</comments>
            <pubDate>Thu, 01 Jan 2009 00:00:00 +0100</pubDate>
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            <title>Coordination and transport of alkali metal cations through phospholipid bilayer membranes by hydraphile channels.</title>
            <link>http://www.medworm.com/index.php?rid=2135202&amp;cid=s_37313_51_f&amp;fid=37313&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19169375%26dopt%3DAbstract</link>
            <description>Authors: Gokel GW, Daschbach MM
    Hydraphiles are synthetic ionophores that were designed to mimic some properties of protein channels that conduct such cations as sodium. They use macrocyclic (crown) polyethers as amphiphilic headgroups and as entry and exit portals. Their overall length is controlled by covalent links between the two headgroups (distal macrocycles) and the &quot;central relay&quot; unit, typically also an azacrown. The hydraphiles insert in the bilayer membranes of synthetic phospholipid vesicles or vital cells and mediate the transport of cations. The hydraphiles were intended to be models but they are functional channels. Because they are symmetric, they are non-rectifying but they show open-close behavior characteristic of natural channels. Because they are non-rectifying, wh...</description>
            <author>Coordination Chemistry Reviews</author>
            <type>journals</type>
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            <pubDate>Tue, 01 Apr 2008 04:00:00 +0100</pubDate>
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            <title>Reflections on Small Molecule Manganese Models that Seek to Mimic Photosynthetic Water Oxidation Chemistry.</title>
            <link>http://www.medworm.com/index.php?rid=2041734&amp;cid=s_37313_51_f&amp;fid=37313&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D19081816%26dopt%3DAbstract</link>
            <description>Authors: Mullins CS, Pecoraro VL
    Recent advances in the study of the Oxygen Evolving Complex (OEC) of Photosystem II (PSII) include structural information attained from several X-ray crystallographic (XRD) and spectroscopic (XANES and EXAFS) investigations. The possible structural features gleaned from these studies have enabled synthetic chemists to design more accurate model complexes, which in turn, offer better insight into the possible pathways used by PSII to drive photosynthetic water oxidation catalysis. Mononuclear model compounds have been used to advance the knowledge base regarding the physical properties and reactivity of high-valent (Mn(IV) or Mn(V)) complexes. Such investigations have been especially important in regard to the manganyl (Mn(IV)=O or Mn(V) identical withO)...</description>
            <author>Coordination Chemistry Reviews</author>
            <type>journals</type>
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            <pubDate>Fri, 01 Feb 2008 05:00:00 +0100</pubDate>
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            <title>Protein Ligation of the Photosynthetic Oxygen-Evolving Center.</title>
            <link>http://www.medworm.com/index.php?rid=1570472&amp;cid=s_37313_51_f&amp;fid=37313&amp;url=http%3A%2F%2Fwww.ncbi.nlm.nih.gov%2Fentrez%2Fquery.fcgi%3Ftmpl%3DNoSidebarfile%26db%3DPubMed%26cmd%3DRetrieve%26list_uids%3D18496594%26dopt%3DAbstract</link>
            <description>Authors: Debus RJ
    Photosynthetic water oxidation is catalyzed by a unique Mn(4)Ca cluster in Photosystem II. The ligation environment of the Mn(4)Ca cluster optimizes the cluster's reactivity at each step in the catalytic cycle and minimizes the release of toxic, partly oxidized intermediates. However, our understanding of the cluster's ligation environment remains incomplete. Although the recent X-ray crystallographic structural models have provided great insight and are consistent with most conclusions of earlier site-directed mutagenesis studies, the ligation environments of the Mn(4)Ca cluster in the two available structural models differ in important respects. Furthermore, while these structural models and the earlier mutagenesis studies agree on the identity of most of the Mn(4)C...</description>
            <author>Coordination Chemistry Reviews</author>
            <type>journals</type>
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            <pubDate>Fri, 01 Feb 2008 05:00:00 +0100</pubDate>
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