Heme P460 cofactors are nature's catalysts for the selective, controlled oxidation of the nitrification (biological ammonia oxidation) metabolite hydroxylamine. Hemes P460 are <i>c</i>-hemes that feature additional heme-protein cross-links that dictate function. This lecture will discuss the role and formation of the heme-lysine cross-link in the cytochromes P460, which are soluble mono-heme enzymes that have been implicated in the link between nitrification and nitrous oxide release. The role of the cross-link in imbuing function will be addressed through structural, spectroscopic, and kinetics studies. Evidence will presented that cross-link formation is driven by peroxide, which undergoes secondary coordination-sphere controlled O–O bond cleavage to yield a ferryl intermediate on the path to cross-link formation. Comparisons will be drawn to heme oxygenases, and implications for evolution of c-heme enzymes into P460-like catalysts will also be addressed.

Forging non-canonical heme-protein cross-links: Peroxide-driven maturation of heme P460 cofactors

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