Nature's nitrite-to-ammonia expressway, with no stop at dinitrogen

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KRONECK, Peter M. H., 2022. Nature's nitrite-to-ammonia expressway, with no stop at dinitrogen. In: Journal of Biological Inorganic Chemistry (JBIC). Springer. 27(1), pp. 1-21. ISSN 0949-8257. eISSN 1432-1327. Available under: doi: 10.1007/s00775-021-01921-4

@article{Kroneck2022-02Natur-55930, title={Nature's nitrite-to-ammonia expressway, with no stop at dinitrogen}, year={2022}, doi={10.1007/s00775-021-01921-4}, number={1}, volume={27}, issn={0949-8257}, journal={Journal of Biological Inorganic Chemistry (JBIC)}, pages={1--21}, author={Kroneck, Peter M. H.} }

<rdf:RDF xmlns:dcterms="" xmlns:dc="" xmlns:rdf="" xmlns:bibo="" xmlns:dspace="" xmlns:foaf="" xmlns:void="" xmlns:xsd="" > <rdf:Description rdf:about=""> <dcterms:hasPart rdf:resource=""/> <dspace:isPartOfCollection rdf:resource=""/> <dc:language>eng</dc:language> <dcterms:available rdf:datatype="">2021-12-20T09:22:06Z</dcterms:available> <dc:contributor>Kroneck, Peter M. H.</dc:contributor> <dcterms:issued>2022-02</dcterms:issued> <dspace:hasBitstream rdf:resource=""/> <dc:date rdf:datatype="">2021-12-20T09:22:06Z</dc:date> <bibo:uri rdf:resource=""/> <dcterms:rights rdf:resource=""/> <dc:rights>Attribution 4.0 International</dc:rights> <dcterms:abstract>Since the characterization of cytochrome c552 as a multiheme nitrite reductase, research on this enzyme has gained major interest. Today, it is known as pentaheme cytochrome c nitrite reductase (NrfA). Part of the NH4+ produced from NO2- is released as NH3 leading to nitrogen loss, similar to denitrification which generates NO, N2O, and N2. NH4+ can also be used for assimilatory purposes, thus NrfA contributes to nitrogen retention. It catalyses the six-electron reduction of NO2- to NH4+, hosting four His/His ligated c-type hemes for electron transfer and one structurally differentiated active site heme. Catalysis occurs at the distal side of a Fe(III) heme c proximally coordinated by lysine of a unique CXXCK motif (Sulfurospirillum deleyianum, Wolinella succinogenes) or, presumably, by the canonical histidine in Campylobacter jejeuni. Replacement of Lys by His in NrfA of W. succinogenes led to a significant loss of enzyme activity. NrfA forms homodimers as shown by high resolution X-ray crystallography, and there exist at least two distinct electron transfer systems to the enzyme. In γ-proteobacteria (Escherichia coli) NrfA is linked to the menaquinol pool in the cytoplasmic membrane through a pentaheme electron carrier (NrfB), in δ- and ε-proteobacteria (S. deleyianum, W. succinogenes), the NrfA dimer interacts with a tetraheme cytochrome c (NrfH). Both form a membrane-associated respiratory complex on the extracellular side of the cytoplasmic membrane to optimize electron transfer efficiency. This minireview traces important steps in understanding the nature of pentaheme cytochrome c nitrite reductases, and discusses their structural and functional features.</dcterms:abstract> <dcterms:title>Nature's nitrite-to-ammonia expressway, with no stop at dinitrogen</dcterms:title> <foaf:homepage rdf:resource="http://localhost:8080/jspui"/> <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/> <dcterms:isPartOf rdf:resource=""/> <dc:creator>Kroneck, Peter M. H.</dc:creator> </rdf:Description> </rdf:RDF>

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