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dc.contributor.authorKlünemann, Thomas
dc.contributor.authorPreuß, Arne
dc.contributor.authorAdamczack, Julia
dc.contributor.authorRosa, Luis F M
dc.contributor.authorHarnisch, Falk
dc.contributor.authorLayer, Gunhild
dc.contributor.authorBlankenfeldt, Wulf
dc.date.accessioned2019-07-09T13:40:06Z
dc.date.available2019-07-09T13:40:06Z
dc.date.issued2019-06-04
dc.identifier.citationJ Mol Biol. 2019 Jun 4. pii: S0022-2836(19)30336-5. doi: 10.1016/j.jmb.2019.05.046.en_US
dc.identifier.issn1089-8638
dc.identifier.pmid31173777
dc.identifier.doi10.1016/j.jmb.2019.05.046
dc.identifier.urihttp://hdl.handle.net/10033/621855
dc.description.abstractMany bacteria can switch from oxygen to nitrogen oxides, such as nitrate or nitrite, as terminal electron acceptors in their respiratory chain. This process is called "denitrification" and enables biofilm formation of the opportunistic human pathogen Pseudomonas aeruginosa, making it more resilient to antibiotics and highly adaptable to different habitats. The reduction of nitrite to nitric oxide is a crucial step during denitrification. It is catalyzed by the homodimeric cytochrome cd1 nitrite reductase (NirS), which utilizes the unique isobacteriochlorin heme d1 as its reaction center. Although the reaction mechanism of nitrite reduction is well understood, far less is known about the biosynthesis of heme d1. The last step of its biosynthesis introduces a double bond in a propionate group of the tetrapyrrole to form an acrylate group. This conversion is catalyzed by the dehydrogenase NirN via a unique reaction mechanism. To get a more detailed insight into this reaction, the crystal structures of NirN with and without bound substrate have been determined. Similar to the homodimeric NirS, the monomeric NirN consists of an eight-bladed heme d1-binding β-propeller and a cytochrome c domain, but their relative orientation differs with respect to NirS. His147 coordinates heme d1 at the proximal side, whereas His323, which belongs to a flexible loop, binds at the distal position. Tyr461 and His417 are located next to the hydrogen atoms removed during dehydrogenation, suggesting an important role in catalysis. Activity assays with NirN variants revealed the essentiality of His147, His323 and Tyr461, but not of His417.en_US
dc.language.isoenen_US
dc.publisherElsevieren_US
dc.rightsAttribution-NonCommercial-ShareAlike 4.0 International*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/4.0/*
dc.subjectNirNen_US
dc.subjectdenitrificationen_US
dc.subjectheme d(1)en_US
dc.subjecttetrapyrrole biosynthesisen_US
dc.subjectx-ray structureen_US
dc.titleCrystal Structure of Dihydro-Heme d Dehydrogenase NirN from Pseudomonas aeruginosa Reveals Amino Acid Residues Essential for Catalysis.en_US
dc.typeArticleen_US
dc.contributor.departmentHZI,Helmholtz-Zentrum für Infektionsforschung GmbH, Inhoffenstr. 7,38124 Braunschweig, Germany.en_US
dc.identifier.journalJournal of Molecular Biologyen_US
dc.source.journaltitleJournal of molecular biology


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