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

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    <dc:creator>Kroneck, Peter M. H.</dc:creator>
    <dc:language>eng</dc:language>
    <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2021-12-20T09:22:06Z</dc:date>
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    <dcterms:title>Nature's nitrite-to-ammonia expressway, with no stop at dinitrogen</dcterms:title>
    <dc:contributor>Kroneck, Peter M. H.</dc:contributor>
    <dc:rights>Attribution 4.0 International</dc:rights>
    <dcterms:issued>2022-02</dcterms:issued>
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    <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>
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