9CCK

Multi-copper oxidase with a C-terminal cupredoxin domain from Nitrosopumilus maritimus

9CCK の概要

• エントリーDOI: 10.2210/pdb9cck/pdb
• 分子名称: Copper-containing nitrite reductase, COPPER (II) ION, ... (4 entities in total)
• 機能のキーワード: copper, trinuclear, hydroxylamine, cupredoxin, oxidoreductase
• 由来する生物種: Nitrosopumilus maritimus; 詳細
• タンパク質・核酸の鎖数: 12
• 化学式量合計: 510880.12

構造登録者

Voland, R.W.,Lancaster, K.M. (登録日: 2024-06-21, 公開日: 2025-02-05)

主引用文献

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

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: 39823305
DOI: 10.1073/pnas.2416971122

実験手法

X-RAY DIFFRACTION (1.84 Å)