Proceedings of nanoGe Spring Meeting 2022 (NSM22)
DOI: https://doi.org/10.29363/nanoge.nsm.2022.113
Publication date: 7th February 2022
Cytochrome c nitrite reductase (CcNiR) is a multi-heme enzyme that catalyzes the six-electron, seven-proton reduction of nitrite to ammonia as part of the global nitrogen cycle. In this talk, the activity of iron and cobalt complexes that perform the multielectron reduction of nitrite, mimicking the activity of CcNiR, will be described. One complex is a small cobalt-peptide complex (CoGGH) that catalyzes the complete reduction of nitrite to ammonium with an onset potential at -0.65 V vs Ag/AgCl (1 M KCl) at pH 7.2. CoGGH also catalyzes the reduction of proposed intermediates nitric oxide and hydroxylamine to ammonium. The second catalyst is an iron complex featuring a macrocyclic redox-active ligand (FeN5H2), which catalyzes nitrite reduction with an onset potential of -0.90 V to form hydroxylamine. FeN5H2 is unusual for being an iron-based catalyst for multielectron nitrite reduction that functions near neutral pH. CoGGH also catalyzes proton reduction to H2; the study of this reaction yields insights into proton handling by this catalyst relevant to understanding the nitrite reduction mechanism.
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