We present the surprising result that the combination of the monotopic benzoate ligand with lanthanide ions leads to a 3D network which also possesses the chiral srs-topology.
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http://dx.doi.org/10.1039/b923998g | DOI Listing |
Chem Commun (Camb)
April 2010
Institut für Anorganische Chemie, Karlsruhe Institute of Technology, Engessertsr. 15, D-76131 Karlsruhe, Germany.
We present the surprising result that the combination of the monotopic benzoate ligand with lanthanide ions leads to a 3D network which also possesses the chiral srs-topology.
View Article and Find Full Text PDFJ Biol Chem
December 2006
Department of Biology and Biochemistry, University of Bath, Bath BA2 7AY, United Kingdom.
Protoporphyrinogen IX oxidase, a monotopic membrane protein, which catalyzes the oxidation of protoporphyrinogen IX to protoporphyrin IX in the heme/chlorophyll biosynthetic pathway, is distributed widely throughout nature. Here we present the structure of protoporphyrinogen IX oxidase from Myxococcus xanthus, an enzyme with similar catalytic properties to human protoporphyrinogen IX oxidase that also binds the common plant herbicide, acifluorfen. In the native structure, the planar porphyrinogen substrate is mimicked by a Tween 20 molecule, tracing three sides of the macrocycle.
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