P
Petra Stach
Researcher at University of Konstanz
Publications - 5
Citations - 665
Petra Stach is an academic researcher from University of Konstanz. The author has contributed to research in topics: Cytochrome c nitrite reductase & Nitrite. The author has an hindex of 5, co-authored 5 publications receiving 628 citations. Previous affiliations of Petra Stach include Goethe University Frankfurt.
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Journal ArticleDOI
Structure of cytochrome c nitrite reductase
Oliver Einsle,Albrecht Messerschmidt,Petra Stach,Gleb Bourenkov,Hans D. Bartunik,Robert Huber,Peter M. H. Kroneck +6 more
TL;DR: 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.
Journal ArticleDOI
Cytochrome c nitrite reductase from Wolinella succinogenes. Structure at 1.6 A resolution, inhibitor binding, and heme-packing motifs.
Oliver Einsle,Oliver Einsle,Petra Stach,Albrecht Messerschmidt,Jörg Simon,Achim Kröger,Robert Huber,Peter M. H. Kroneck +7 more
TL;DR: Based on sequence comparison and secondary structure prediction, it is demonstrated that cytochromec nitrite reductases constitute a protein family of high structural similarity.
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Binding and reduction of sulfite by cytochrome c nitrite reductase.
Peer Lukat,Marc Rudolf,Petra Stach,Albrecht Messerschmidt,Peter M. H. Kroneck,Jörg Simon,Oliver Einsle +6 more
TL;DR: The active site variant Y218F of ccNiR that exhibited an almost complete loss of nitrite reductase activity, while sulfite reduction remained unaffected is characterized, providing a first direct insight into the role of the first sphere of protein ligands at the active site in cc NiR catalysis.
Journal ArticleDOI
Bacterial cytochrome c nitrite reductase: new structural and functional aspects
TL;DR: A paramagnetic Fe(II)-NO, S = 1/2 adduct was identified by rapid freeze EPR spectroscopy under turnover conditions with nitrite and exhibited a remarkably high sulfite reductase activity, with hydrogen sulfide as the product.
Journal ArticleDOI
Crystallization and preliminary X-ray analysis of the membrane-bound cytochrome c nitrite reductase complex (NrfHA) from Wolinella succinogenes
Oliver Einsle,Oliver Einsle,Petra Stach,Albrecht Messerschmidt,Oliver Klimmek,Jörg Simon,Achim Kröger,Peter M. H. Kroneck +7 more
TL;DR: Crystals of the complex between the enzyme cytochrome c nitrite reductase (NrfA) and the membrane-bound quinol oxidase and electron carrier NrfH were grown by vapour diffusion using ammonium sulfate as a precipitant.