Crystal structure of protoporphyrinogen IX oxidase: a key enzyme in haem and chlorophyll biosynthesis
- Michael Koch, C. Breithaupt, R. Kiefersauer, J. Freigang, R. Huber, A. Messerschmidt
- Biology, ChemistryEMBO Journal
- 21 April 2004
This modelled transmembrane complex provides a structural explanation for the uncoupling of haem biosynthesis observed in variegate porphyria patients and in plants after inhibiting PPO.
Determinants of Enzymatic Specificity in the Cys-Met-Metabolism PLP-Dependent Enzyme Family: Crystal Structure of Cystathionine γ-Lyase from Yeast and Intrafamiliar Structure Comparison
The crystal structure of cystathionine γ-lyase (CGL) from yeast has been solved by molecular replacement at a resolution of 2.6 å and a structure comparison with other family members revealed surprising insights into the tuning of enzymatic specificity between the different family members.
The blue oxidases, ascorbate oxidase, laccase and ceruloplasmin. Modelling and structural relationships.
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.
Refined crystal structure of ascorbate oxidase at 1.9 A resolution.
Structure of cytochrome c nitrite reductase
By comparing the haem arrangement of this nitrite reductase with that of other multihaem cytochromes, this work has been able to identify a family of proteins in which the orientation of haem groups is conserved whereas structure and function are not.
- A. Messerschmidt
- Biology, Chemistry
- 1 June 1997
Earlier times in multi-copper oxidase research versus recent results from Goteborg, B. Malmstrom spatial structures of the multi-copper oxidases ascorbate oxidase, laccase and related proteins -…
Crystal structure of the pyridoxal-5'-phosphate dependent cystathionine beta-lyase from Escherichia coli at 1.83 A.
- T. Clausen, R. Huber, B. Laber, H. Pohlenz, A. Messerschmidt
- ChemistryJournal of Molecular Biology
- 20 September 1996
The crystal structure of CBL from E. coli has been solved using MIR phases in combination with density modification and suggests that Lys210, the PLP-binding residue, mediates the proton transfer between C alpha and S gamma.
Crystal structure of the catalytic domain of human atypical protein kinase C-iota reveals interaction mode of phosphorylation site in turn motif.
Mechanism of the six-electron reduction of nitrite to ammonia by cytochrome c nitrite reductase.
- O. Einsle, A. Messerschmidt, R. Huber, P. Kroneck, F. Neese
- ChemistryJournal of the American Chemical Society
- 2 October 2002
A working hypothesis for the reaction mechanism of this multiheme enzyme which carries a novel lysine-coordinated heme group (Fe-Lys) is presented and it is proposed that nitrite reduction starts with a heterolytic cleavage of the N-O bond.
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.