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Abstract Two related classes of ligand-binding hemec-containing proteins with a high degree of structural homology have been identified and characterized over recent decades: cytochromes P460 (cyts P460), defined by an unusual heme-lysine cross-link, and cytochromesc′-β (cytsc′-β), containing a canonicalc-heme without the lysine cross-link. The shared protein fold of the cyt P460-cytc′-β superfamily can accommodate a variety of heme environments with entirely different reactivities. On the one hand, cyts P460 with polar distal pockets have been shown to oxidize NH₂OH to NO and/or N₂O via proton-coupled electron transfer. On the other hand, cytsc′-β with hydrophobic distal pockets have a proposed gas binding function similar to the unrelated, but more extensively characterized, alpha helical cytochromesc′. Recent studies have also identified ‘halfway house’ proteins (cyts P460 with non-polar heme pockets and cytsc′-β with polar distal heme pockets) with functions yet to be resolved. Here, we review the structural, spectroscopic and enzymatic properties of the cyt P460-cytc′-β superfamily with a view to understanding the structural determinants of their different functional properties. Graphical abstract 

Cytochromes P460 oxidise hydroxylamine within the nitrogen cycle and contain as their active site an unusual catalyticc-type haem where the porphyrin is crosslinked to the protein via a lysine...