6M0P

Hydroxylamine oxidoreductase in complex with juglone

Summary for 6M0P

• Entry DOI: 10.2210/pdb6m0p/pdb
• Descriptor: Aerobic hydroxylamine oxidoreductase, Uncharacterized protein, HEME C, ... (8 entities in total)
• Functional Keywords: enhancer, complex, oxidoreductase
• Biological source: Nitrosomonas europaea; More
• Total number of polymer chains: 6
• Total formula weight: 238113.02

Authors

Fujiwara, T.,Fujimoto, Z.,Nishigaya, Y.,Yamazaki, T. (deposition date: 2020-02-22, release date: 2021-03-10, Last modification date: 2024-05-08)

Primary citation

Akutsu, Y.,Fujiwara, T.,Suzuki, R.,Nishigaya, Y.,Yamazaki, T.
Juglone, a plant-derived 1,4-naphthoquinone, binds to hydroxylamine oxidoreductase and inhibits the electron transfer to cytochrome c 554.
Appl.Environ.Microbiol., 89:e0129123-e0129123, 2023

PubMed Abstract: Nitrification, the microbial conversion of ammonia to nitrate via nitrite, plays a pivotal role in the global nitrogen cycle. However, the excessive use of ammonium-based fertilizers in agriculture has disrupted this cycle, leading to groundwater pollution and greenhouse gas emissions. In this study, we have demonstrated the inhibitory effects of plant-derived juglone and related 1,4-naphthoquinones on the nitrification process in . Notably, the inhibition mechanism is elucidated in which 1,4-naphthoquinones interact with hydroxylamine oxidoreductase, disrupting the electron transfer to cytochrome , a physiological electron acceptor. These findings support the notion that phytochemicals can impede nitrification by interfering with the essential electron transfer process in ammonia oxidation. The findings presented in this article offer valuable insights for the development of strategies aimed at the management of nitrification, reduction of fertilizer utilization, and mitigation of greenhouse gas emissions.

PubMed: 38009977
DOI: 10.1128/aem.01291-23

Experimental method

X-RAY DIFFRACTION (2.78 Å)