Outer coordination sphere influences on cofactor maturation and substrate oxidation by cytochrome P460.

ABSTRACT: Product selectivity of ammonia oxidation by ammonia-oxidizing bacteria (AOB) is tightly controlled by metalloenzymes. Hydroxylamine oxidoreductase (HAO) is responsible for the oxidation of hydroxylamine (NH₂OH) to nitric oxide (NO). The non-metabolic enzyme cytochrome (cyt) P460 also oxidizes NH₂OH, but instead produces nitrous oxide (N₂O). While both enzymes use a heme P460 cofactor, they selectively oxidize NH₂OH to different products. Previously reported structures of Nitrosomonas sp. AL212 cyt P460 show that a capping phenylalanine residue rotates upon ligand binding, suggesting that this Phe may influence substrate and/or product binding. Here, we show via substitutions of the capping Phe in Nitrosomonas europaea cyt P46

SUBMITTER: Bollmeyer MM 

PROVIDER: S-EPMC10411619 | biostudies-literature | 2023 Aug

REPOSITORIES: biostudies-literature