ChemBioChem

Cover image for Vol. 11 Issue 5

March 22, 2010

Volume 11, Issue 5

Pages 589–727

  1. Cover Picture

    1. Top of page
    2. Cover Picture
    3. Inside Cover
    4. Graphical Abstract
    5. News
    6. Review
    7. Minireview
    8. Highlights
    9. Communications
    10. Full Papers
    11. Book Review
    12. Preview
    1. Cover Picture: Biological Iron-Monosulfide Production for Efficient Electricity Harvesting from a Deep-Sea Metal-Reducing Bacterium (ChemBioChem 5/2010) (page 589)

      Ryuhei Nakamura, Akihiro Okamoto, Nozomi Tajima, Greg J. Newton, Fumiyoshi Kai, Toshihiro Takashima and Kazuhito Hashimoto 

      Version of Record online: 17 MAR 2010 | DOI: 10.1002/cbic.201090015

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      The cover picture shows the microbial ingenuity of the deep-sea Fe-reducing bacterium Shewanella loihica PV-4 for self-organizing an electrically conductive network by using biogenic iron sulfides (FeS) as extracellular electron-transfer conduits. On p. 643 ff., K. Hashimoto et al. show that Shewanella cells exploit Fe 3d electrons in the nanosized FeS colloids for a respiratory electron-transfer reaction. In situ biological production of FeS in electrochemical cells enabled the generation of a microbial current two orders of magnitude higher than in cell cultures lacking the biogenic minerals. This substantial increase in microbial current represents the first example of exploiting the electron-conducting properties of naturally abundant biogenic minerals to efficiently harvest metabolized electrons in an electrochemical cell. The present results therefore shed light on bio- and geoinspired approaches for improving the performance of bioanode materials in biological fuel cells.

  2. Inside Cover

    1. Top of page
    2. Cover Picture
    3. Inside Cover
    4. Graphical Abstract
    5. News
    6. Review
    7. Minireview
    8. Highlights
    9. Communications
    10. Full Papers
    11. Book Review
    12. Preview
    1. Inside Cover: Methods to Study GPI Anchoring of Proteins (ChemBioChem 5/2010) (page 590)

      Yug Varma and Tamara Hendrickson

      Version of Record online: 17 MAR 2010 | DOI: 10.1002/cbic.201090016

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      The inside cover picture highlights the significance of GPI research on genetic disorders, cancer, and parasitic diseases. The GPI anchor structure (white) and a trypanosome (blue) are overlaid on a red blood cell. Examples of important GPI-anchored proteins are shown in magenta, while a cartoon of GPI transamidase illustrates the complexity of this enzyme. For more information, see the Minireview by T. Hendrickson and Y. Varma on p. 623 ff.

  3. Graphical Abstract

    1. Top of page
    2. Cover Picture
    3. Inside Cover
    4. Graphical Abstract
    5. News
    6. Review
    7. Minireview
    8. Highlights
    9. Communications
    10. Full Papers
    11. Book Review
    12. Preview
  4. News

    1. Top of page
    2. Cover Picture
    3. Inside Cover
    4. Graphical Abstract
    5. News
    6. Review
    7. Minireview
    8. Highlights
    9. Communications
    10. Full Papers
    11. Book Review
    12. Preview
  5. Review

    1. Top of page
    2. Cover Picture
    3. Inside Cover
    4. Graphical Abstract
    5. News
    6. Review
    7. Minireview
    8. Highlights
    9. Communications
    10. Full Papers
    11. Book Review
    12. Preview
    1. Adenosyl Radical: Reagent and Catalyst in Enzyme Reactions (pages 604–621)

      E. Neil G. Marsh, Dustin P. Patterson and Lei Li

      Version of Record online: 28 FEB 2010 | DOI: 10.1002/cbic.200900777

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      Primordial molecules: An adenosyl radical is generated as a reactive intermediate by two families of enzymes that use either adenosylcobalamin or S-adenosylmethionine as cofactors. We review and contrast the wide range of unusual reactions catalyzed by these enzyme families and discuss the likelihood that the highly oxygen-sensitive radical S-adenosylmethionine enzymes are also active in aerobic organisms.

  6. Minireview

    1. Top of page
    2. Cover Picture
    3. Inside Cover
    4. Graphical Abstract
    5. News
    6. Review
    7. Minireview
    8. Highlights
    9. Communications
    10. Full Papers
    11. Book Review
    12. Preview
    1. Methods to Study GPI Anchoring of Proteins (pages 623–636)

      Yug Varma and Tamara Hendrickson

      Version of Record online: 8 FEB 2010 | DOI: 10.1002/cbic.200900704

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      Dropping anchor: Glycosylphosphatidylinositol (GPI) membrane-anchored proteins noncovalently associate with the plasma membrane and can have an impact on oncogenesis and some infectious diseases. The GPI anchor biosynthetic machinery and GPI-T, the transamidase that attaches them to proteins, are complicated, membrane-associated enzymes that are only beginning to be understood.

  7. Highlights

    1. Top of page
    2. Cover Picture
    3. Inside Cover
    4. Graphical Abstract
    5. News
    6. Review
    7. Minireview
    8. Highlights
    9. Communications
    10. Full Papers
    11. Book Review
    12. Preview
    1. Activation Instead of Inhibition: Targeting Proenzymes for Small-Molecule Intervention (pages 637–639)

      Christian Ottmann, Patrick Hauske and Markus Kaiser

      Version of Record online: 8 FEB 2010 | DOI: 10.1002/cbic.201000024

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      Switching on pro-proteases: Direct small-molecule activation of proenzymes such as pro-proteases has recently be achieved for procaspase-3. This success opens up new possibilities for small-molecule intervention in biology, and reveals proenzymes as a whole new class of potential targets.

    2. Turning Riboswitches Loose (pages 640–641)

      Jörg S. Hartig

      Version of Record online: 16 FEB 2010 | DOI: 10.1002/cbic.201000045

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      The discovery of combined RNA-based regulatory mechanisms composed of a ligand-dependent riboswitch and an antisense RNA acting in trans is discussed.

  8. Communications

    1. Top of page
    2. Cover Picture
    3. Inside Cover
    4. Graphical Abstract
    5. News
    6. Review
    7. Minireview
    8. Highlights
    9. Communications
    10. Full Papers
    11. Book Review
    12. Preview
    1. Biological Iron-Monosulfide Production for Efficient Electricity Harvesting from a Deep-Sea Metal-Reducing Bacterium (pages 643–645)

      Ryuhei Nakamura, Akihiro Okamoto, Nozomi Tajima, Greg J. Newton, Fumiyoshi Kai, Toshihiro Takashima and Kazuhito Hashimoto 

      Version of Record online: 9 FEB 2010 | DOI: 10.1002/cbic.200900775

      Thumbnail image of graphical abstract

      FeS source: A metal-reducing bacterium, Shewanella loihica PV-4, has evolved the ability to utilize Fe 3d electrons from biogenic FeS as a long-distance electron-transfer conduit. Self-organizing, electron-conducting cellular networks enable the generation of a microbial current two orders of magnitude higher than in cell cultures lacking the biogenic minerals.

    2. Noncovalent-Interaction-Promoted Ligation for Protein Labeling (pages 646–648)

      Yuichiro Hori, Yuka Egashira, Ryosuke Kamiura and Kazuya Kikuchi

      Version of Record online: 19 FEB 2010 | DOI: 10.1002/cbic.201000007

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      Stapler for protein labeling: A novel protein labeling technique was developed by utilizing a coiled-coil tag and intein. The technique enables covalent labeling of a protein of interest (POI) with a fluorescein-conjugated peptide in vitro and in cell lysate. The small size of the coiled-coil tag, and the specificity and stability of the labeling are attractive characteristics for protein detection and visualization in biological studies.

    3. Sugar-Selective Enrichment of a D-Glucose-Substituted Ruthenium Bipyridyl Complex Inside HepG2 Cancer Cells (pages 649–652)

      Michael Gottschaldt, Ulrich S. Schubert , Sven Rau, Shigenobu Yano, Johannes G. Vos, Torsten Kroll, Joachim Clement and Ingrid Hilger

      Version of Record online: 15 FEB 2010 | DOI: 10.1002/cbic.200900769

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      Ru sugar balls: RuII bipyridyl complexes bearing different sugar units were synthesized. Incubation of these compounds with HepG2 cells shows for the first time that cellular uptake of equally substituted ruthenium bipyridyl complexes can be controlled by the type of sugar attached. Preferential internalization of the D-glucose-bearing complex was observed and verified by confocal laser scanning microscopy (CLSM) and flow cytometry.

  9. Full Papers

    1. Top of page
    2. Cover Picture
    3. Inside Cover
    4. Graphical Abstract
    5. News
    6. Review
    7. Minireview
    8. Highlights
    9. Communications
    10. Full Papers
    11. Book Review
    12. Preview
    1. You have free access to this content
      Photocontrol of Protein Activity in Cultured Cells and Zebrafish with One- and Two-Photon Illumination (pages 653–663)

      Deepak Kumar Sinha, Pierre Neveu, Nathalie Gagey, Isabelle Aujard, Chouaha Benbrahim-Bouzidi, Thomas Le Saux, Christine Rampon, Carole Gauron, Bernard Goetz, Sylvie Dubruille, Marc Baaden, Michel Volovitch, David Bensimon, Sophie Vriz and Ludovic Jullien

      Version of Record online: 24 FEB 2010 | DOI: 10.1002/cbic.201000008

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      The inner light: We have implemented a photochemical method to control the activity of proteins linked to the ERT2 receptor in live zebrafish embryos. Using fluorescent proteins inactivated by association with endogenous chaperone complex (CC), we showed that photoreleasing the cyclofen inducer led to fast protein photoactivation. Colocalization experiments suggest that light-induced activation can be restricted to a few targeted cells.

    2. 2-(1-Ethynylpyrene)-Adenosine as a Folding Probe for RNA—Pyrene in or out (pages 664–672)

      Ute Förster, Katharina Lommel, Daniel Sauter, Christian Grünewald, Joachim W. Engels and Josef Wachtveitl

      Version of Record online: 22 FEB 2010 | DOI: 10.1002/cbic.200900778

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      Pyrene hokey pokey: 1-Ethynylpyrene attached to the 2-position of an adenine base acts as a sensitive microenvironment probe. Intercalation is dependent on the bases flanking the pyrene-modified adenine. Fluorescence evolution of pyrene exciplexes with temperature allows to distinguish between local and global melting of an RNA duplex.

    3. Structural Investigation of the Binding of 5-Substituted Swainsonine Analogues to Golgi α-Mannosidase II (pages 673–680)

      Douglas A. Kuntz, Shinichi Nakayama, Kayla Shea, Hitoshi Hori, Yoshihiro Uto, Hideko Nagasawa  and David. R. Rose

      Version of Record online: 5 MAR 2010 | DOI: 10.1002/cbic.200900750

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      Reaching for specificity: X-ray crystallographic data indicates potent 5α-substituted swainsonine analogues bind in a novel fashion to Golgi α-mannosidase II by inserting in a water cluster and by forming new hydrophobic interactions. These offer the potential of being extended into the GlcNAc binding site to improve selectivity and reduce harmful side effects.

    4. Redesigning the Active Site of Transaldolase TalB from Escherichia coli: New Variants with Improved Affinity towards Nonphosphorylated Substrates (pages 681–690)

      Sarah Schneider, Mariana Gutiérrez, Tatyana Sandalova, Gunter Schneider, Pere Clapés, Georg A. Sprenger and Anne K. Samland

      Version of Record online: 10 FEB 2010 | DOI: 10.1002/cbic.200900720

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      Superior biocatalyst: By using structure based saturation mutagenesis a transaldolase B variant was developed with an improved affinity towards nonphosphorylated aldehydes. It catalyses the stereoselective synthesis of D-fructose, L-sorbose and D-xylulose to >90 % conversion from simple and cheap educts, like dihydroxyacetone, glyceraldehyde and glycolaldehyde.

    5. Directed Evolution of an Antitumor Drug (Arginine Deiminase PpADI) for Increased Activity at Physiological pH (pages 691–697)

      Leilei Zhu , Kang Lan Tee, Danilo Roccatano, Burcu Sonmez, Ye Ni, Zhi-Hao Sun and Ulrich Schwaneberg 

      Version of Record online: 15 FEB 2010 | DOI: 10.1002/cbic.200900717

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      Not so acid test: Mutations in residues His405 and Glu44 shifted the pH optimum of a Pseudomonas plecoglossicida arginine deiminase to physiological pH and increased the ADI's activity up to fourfold.

    6. An Expeditious Route to Fluorinated Rapamycin Analogues by Utilising Mutasynthesis (pages 698–702)

      Rebecca J. M. Goss, Simon Lanceron, Abhijeet Deb Roy, Simon Sprague, Mohammed Nur-e-Alam, David L. Hughes, Barrie Wilkinson and Steven J. Moss

      Version of Record online: 23 FEB 2010 | DOI: 10.1002/cbic.200900723

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      Rapping it up: A series of fluorinated rapamycin analogues may be readily accessed by using a combined synthetic and biosynthetic approach.

    7. Click-Chemistry-Derived Tetracycline–Amino Acid Conjugates Exhibiting Exceptional Potency and Exclusive Recognition of the Reverse Tet Repressor (pages 703–712)

      Igor Usai, Marcus Krueger, Jürgen Einsiedel, Wolfgang Hillen and Peter Gmeiner

      Version of Record online: 10 FEB 2010 | DOI: 10.1002/cbic.200900710

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      TetRis: Applying click chemistry, a series of doxycycline–amino acid conjugates was synthesized. The C-terminally linked phenylalanine derivative emerged as a highly selective effector for the reverse phenotype revTetR(B), and did not activate TetR. Interestingly, the test compound proved to be almost devoid of any antibacterial activity; which will be highly beneficial for future applications to control gene expression in bacterial systems.

    8. Towards Preparative Scale Steroid Hydroxylation with Cytochrome P450 Monooxygenase CYP106A2 (pages 713–721)

      Daniela Zehentgruber, Frank Hannemann, Sabrina Bleif, Rita Bernhardt and Stephan Lütz 

      Version of Record online: 22 FEB 2010 | DOI: 10.1002/cbic.200900706

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      Four proteins join forces: CYP106A2-catalyzed 15β-hydroxylation of progesterone and testosterone could be improved towards higher productivities through the identification of reaction-limiting steps.

  10. Book Review

    1. Top of page
    2. Cover Picture
    3. Inside Cover
    4. Graphical Abstract
    5. News
    6. Review
    7. Minireview
    8. Highlights
    9. Communications
    10. Full Papers
    11. Book Review
    12. Preview
    1. Amino Acids, Peptides and Proteins in Organic Chemistry. Vol. 1: Origins and Synthesis of Amino Acids. Edited by Andrew B. Hughes. (page 722)

      Günther Jung

      Version of Record online: 3 NOV 2010 | DOI: 10.1002/cbic.201000095

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      Wiley-VCH, Weinheim Hoboken 2009, 701 pp., hardcover € 140.00.—ISBN 978-3-527-32096-7

  11. Preview

    1. Top of page
    2. Cover Picture
    3. Inside Cover
    4. Graphical Abstract
    5. News
    6. Review
    7. Minireview
    8. Highlights
    9. Communications
    10. Full Papers
    11. Book Review
    12. Preview
    1. You have free access to this content
      Preview: ChemBioChem 6/2010 (page 727)

      Version of Record online: 17 MAR 2010 | DOI: 10.1002/cbic.201090019

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