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Albrecht Messerschmidt
Researcher at Max Planck Society
Publications - 115
Citations - 8541
Albrecht Messerschmidt is an academic researcher from Max Planck Society. The author has contributed to research in topics: Azurin & Active site. The author has an hindex of 46, co-authored 115 publications receiving 8241 citations. Previous affiliations of Albrecht Messerschmidt include University of Leeds & Hoechst Schering AgrEvo GmbH.
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Reference EntryDOI
Handbook of metalloproteins
TL;DR: Volume 1 IRON Heme Proteins: Oxygen Storage and Oxygen Transport Proteinology Volume 2 IRON continued Non-Heme Protesins: Dinuclear Iron ProteINs Non-heme ProteINS: Iron Storage Non- Heme Protins: Iron Transport NICKEL MANGANESE COBALT MOLYBDENUM/TUNGSTEN COPPER Cupredoxins
Journal ArticleDOI
Crystal structure analysis of oxidized Pseudomonas aeruginosa azurin at pH 5.5 and pH 9.0. A pH-induced conformational transition involves a peptide bond flip.
TL;DR: The X-ray crystal structure of recombinant wild-type azurin from Pseudomonas aeruginosa was determined by difference Fourier techniques using phases derived from the structure of the mutant His35Leu, which involves a concomitant Pro36-Gly37 main-chain peptide bond flip.
Journal ArticleDOI
Refined crystal structure of ascorbate oxidase at 1.9 A resolution.
Albrecht Messerschmidt,Rudolf Ladenstein,Robert Huber,Martino Bolognesi,Luciana Avigliano,Raffaele Petruzzelli,Antonello Rossi,Alessandro Finazzi-Agrò +7 more
TL;DR: The crystal structure of the fully oxidized form of ascorbate oxidase from Zucchini has been refined at 1.90 A (1 A = 0.1 nm) resolution, using an energy-restrained least-squares refinement procedure.
Journal ArticleDOI
The blue oxidases, ascorbate oxidase, laccase and ceruloplasmin. Modelling and structural relationships.
TL;DR: The relationships suggest that laccase, like ascorbate oxidase, has a mononuclear blue copper in domain 3 and a trinuclear copper between domain 1 and 3 and ceruloplasmin has mon onuclear copper ions in domains 2, 4 and 6 and atrinuclear Copper between domains 1 and 6.
Journal ArticleDOI
X-ray crystal structure of the blue oxidase ascorbate oxidase from zucchini. Analysis of the polypeptide fold and a model of the copper sites and ligands.
Albrecht Messerschmidt,Antonello Rossi,Rudolf Ladenstein,Robert Huber,Martino Bolognesi,Guiseppina Gatti,Augusto Marchesini,Raffaele Petruzzelli,Alessandro Finazzi-Agrò +8 more
TL;DR: Two crystal forms of the multi-copper protein ascorbate oxidase from Zucchini have been analysed at 2.5 A resolution and a model of the polypeptide chain and the copper ions and their ligands has been built.