9CCK
Multi-copper oxidase with a C-terminal cupredoxin domain from Nitrosopumilus maritimus
Summary for 9CCK
| Entry DOI | 10.2210/pdb9cck/pdb |
| Descriptor | Copper-containing nitrite reductase, COPPER (II) ION, ... (4 entities in total) |
| Functional Keywords | copper, trinuclear, hydroxylamine, cupredoxin, oxidoreductase |
| Biological source | Nitrosopumilus maritimus More |
| Total number of polymer chains | 12 |
| Total formula weight | 510880.12 |
| Authors | |
| Primary citation | Voland, R.W.,Wang, H.,Abruna, H.D.,Lancaster, K.M. Nitrous oxide production via enzymatic nitroxyl from the nitrifying archaeon Nitrosopumilus maritimus. Proc.Natl.Acad.Sci.USA, 122:e2416971122-e2416971122, 2025 Cited by PubMed Abstract: Ammonia oxidizing archaea (AOA) are among the most abundant microorganisms on earth and are known to be a major source of nitrous oxide (NO) emissions, although biochemical origins of this NO remain unknown. Enzymological details of AOA nitrogen metabolism are broadly unavailable. We report the recombinant expression, purification, and characterization of a multicopper oxidase, Nmar_1354, from the AOA . We show that Nmar_1354 selectively produces nitroxyl (HNO) by coupling the oxidation of the obligate nitrification intermediate hydroxylamine (NHOH) to dioxygen (O) reduction. This HNO undergoes several downstream reactions, although the major fates are production of N via reaction with NHOH and dimerization with itself to yield NO. These results afford one plausible enzymatic origin for NO release by AOA. Moreover, these results reveal a physiologically relevant enzymatic reaction for producing HNO, an enigmatic nitrogen oxide speculated to be operative in cellular signaling and in energy transduction. PubMed: 39823305DOI: 10.1073/pnas.2416971122 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.84 Å) |
Structure validation
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