Recent mechanistic developments for cytochrome c nitrite reductase, the key enzyme in the dissimilatory nitrate reduction to ammonium pathway.

Julius O Campeciño, Nicolai Lehnert, Eric L Hegg, Krystina Hird

Journal: Journal of inorganic biochemistry 2024;256():112542

PMID: 38631103

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Abstract

Cytochrome c nitrite reductase, NrfA, is a soluble, periplasmic pentaheme cytochrome responsible for the reduction of nitrite to ammonium in the Dissimilatory Nitrate Reduction to Ammonium (DNRA) pathway, a vital reaction in the global nitrogen cycle. NrfA catalyzes this six-electron and eight-proton reduction of nitrite at a single active site with the help of its quinol oxidase partners. In this review, we summarize the latest progress in elucidating the reaction mechanism of ammonia production, including new findings about the active site architecture of NrfA, as well as recent results that elucidate electron transfer and storage in the pentaheme scaffold of this enzyme.

Address: Department of Biochemistry & Molecular Biology, Michigan State University, East Lansing, MI, USA.; Department of Chemistry, University of Michigan, Ann Arbor, MI, USA.; Department of Biochemistry & Molecular Biology, Michigan State University, East Lansing, MI, USA. Electronic address: [email protected].

DOI: 10.1016/j.jinorgbio.2024.112542

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MeSH Terms: Nitrates, Oxidation-Reduction, Ammonium Compounds, Cytochromes c1, Nitrate Reductases, Catalytic Domain, Electron Transport, Nitrites, Cytochromes a1