AI Article Synopsis
- - Cytochrome P460s are heme enzymes that convert hydroxylamine into nitrous oxide, relying on unique heme P460 cofactors linked to their proteins by a modified lysine.
- - The wild-type version of cytochrome P460 can exist as an inactive form (proenzyme) after being produced in low-oxygen conditions, but it can mature into an active enzyme upon treatment with peroxide.
- - This maturation process is inherent to the enzyme itself, requiring no additional help from other proteins, and involves the formation of a ferryl species, which is significant for the overall function and reactivity of the enzyme.
Article Abstract
Cytochrome P460s are heme enzymes that oxidize hydroxylamine to nitrous oxide. They bear specialized "heme P460" cofactors that are cross-linked to their host polypeptides by a post-translationally modified lysine residue. Wild-type cytochrome P460 may be isolated as a cross-link-deficient proenzyme following anaerobic overexpression in . When treated with peroxide, this proenzyme undergoes maturation to active enzyme with spectroscopic and catalytic properties that match wild-type cyt P460. This maturation reactivity requires no chaperones─it is intrinsic to the protein. This behavior extends to the broader cytochrome c' superfamily. Accumulated data reveal key contributions from the secondary coordination sphere that enable selective, complete maturation. Spectroscopic data support the intermediacy of a ferryl species along the maturation pathway.
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Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10431212 | PMC |
| http://dx.doi.org/10.1021/jacs.3c03608 | DOI Listing |
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