Search Results - (Author, Cooperation:C. S. Bond)

Showing 1 - 2 results of 2, query time: 0.08s Refine Results
  1. 1
    C. E. Conn ; R. Bythell-Douglas ; D. Neumann ; S. Yoshida ; B. Whittington ; J. H. Westwood ; K. Shirasu ; C. S. Bond ; K. A. Dyer ; D. C. Nelson
    American Association for the Advancement of Science (AAAS)
    Published 2015
    Staff View
    Publication Date:
    2015-08-01
    Publisher:
    American Association for the Advancement of Science (AAAS)
    Print ISSN:
    0036-8075
    Electronic ISSN:
    1095-9203
    Topics:
    Biology
    Chemistry and Pharmacology
    Computer Science
    Medicine
    Natural Sciences in General
    Physics
    Keywords:
    Arabidopsis/*metabolism/*parasitology ; Arabidopsis Proteins/*classification/genetics/metabolism ; *Biological Evolution ; Gene Dosage ; Germination ; Heterocyclic Compounds, 1-Ring/*metabolism ; Host-Parasite Interactions ; Hydrolases/*classification/genetics/metabolism ; Lactones/*metabolism ; Orobanchaceae/*enzymology/genetics/growth & development ; Phylogeny ; Plant Growth Regulators/*metabolism ; Plant Roots/metabolism/parasitology ; Plants, Genetically Modified/genetics/metabolism
    Published by:
    http://www.aaas.org/

    Latest Papers from Table of Contents or Articles in Press
  2. 2
    Staff View
    ISSN:
    1432-1327
    Keywords:
    Key words Reduction potential ; Rubredoxin ; Square wave voltammetry ; X-ray crystallography
    Source:
    Springer Online Journal Archives 1860-2000
    Topics:
    Biology
    Chemistry and Pharmacology
    Notes:
    Abstract  The Pri sidechains of two adjacent valine residues, V8 and V44, define the surface of the rubredoxin from Clostridium pasteurianum and control access to its Fe(S-Cys)4 active site. To assess the effect of systematic change of the steric bulk of the alkyl sidechains, eight single and three double mutant proteins have been isolated which vary G (H), A (Me), V (Pri), L (Bui) and I (Bus) at those positions. X-ray crystal structures of the FeIII forms of the V44A and V44I proteins are reported. Positive shifts in reversible potential of up to 116 mV are observed and attributed to increased polarity around the Fe(S-Cys)4 site induced by (1) changes in protein backbone conformation driven by variation of the steric demands of the sidechain substituents and (2) changes in solvent access to the sidechains of ligands C9 and C42. Data for the V44A mutant show that a minor change in the steric requirements of a surface residue can introduce a NH···Sγ hydrogen bond at the active site and lead to a shift in potentialof +50 mV.
    Type of Medium:
    Electronic Resource
    URL:
    http://dx.doi.org/10.1007/PL00010656

    Articles: DFG German National Licenses