Cytochrome P460 Cofactor Maturation Involves a Peroxide- Dependent Post-Translational Modification

11 January 2022, Version 1
This content is a preprint and has not undergone peer review at the time of posting.


Cytochrome P460s are heme enzymes that oxidize hydroxylamine to nitrous oxide as part of the biogeochemical nitrogen cycle. They bear unique “heme P460” cofactors that are cross-linked to their host polypeptides by a post-translationally modified lysine residue. Wild-type N. europaea cytochrome P460 may be isolated as a cross-link deficient proenzyme following anaerobic overexpression in E. coli. When treated with peroxide, This proenzyme undergoes complete maturation to active enzyme with spectroscopic properties that match wild-type cyt P460. Together, these data indicate that the cofactor is primed to undergo this covalent modification by virtue of the protein fold. A putative mechanism analogous to that used by heme oxygenases to degrade hemes is proposed.


post-translational modification
bioinorganic chemistry

Supplementary materials

Supporting Information
Supplementary text (materials and methods) as well as data including kinetics traces.


Comments are not moderated before they are posted, but they can be removed by the site moderators if they are found to be in contravention of our Commenting Policy [opens in a new tab] - please read this policy before you post. Comments should be used for scholarly discussion of the content in question. You can find more information about how to use the commenting feature here [opens in a new tab] .
This site is protected by reCAPTCHA and the Google Privacy Policy [opens in a new tab] and Terms of Service [opens in a new tab] apply.