School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, United Kingdom.
School of Environmental Sciences, University of East Anglia, Norwich NR4 7TJ, United Kingdom.
FEMS Microbiol Lett. 2023 Jan 17;370. doi: 10.1093/femsle/fnad093.
Ammonia oxidizers are key players in the global nitrogen cycle and are responsible for the oxidation of ammonia to nitrite, which is further oxidized to nitrate by other microorganisms. Their activity can lead to adverse effects on some human-impacted environments, including water pollution through leaching of nitrate and emissions of the greenhouse gas nitrous oxide (N2O). Ammonia monooxygenase (AMO) is the key enzyme in microbial ammonia oxidation and shared by all groups of aerobic ammonia oxidizers. The AMO has not been purified in an active form, and much of what is known about its potential structure and function comes from studies on its interactions with inhibitors. The archaeal AMO is less well studied as ammonia oxidizing archaea were discovered much more recently than their bacterial counterparts. The inhibition of ammonia oxidation by aliphatic alcohols (C1-C8) using the model terrestrial ammonia oxidizing archaeon 'Candidatus Nitrosocosmicus franklandus' C13 and the ammonia oxidizing bacterium Nitrosomonas europaea was examined in order to expand knowledge about the range of inhibitors of ammonia oxidizers. Methanol was the most potent specific inhibitor of the AMO in both ammonia oxidizers, with half-maximal inhibitory concentrations (IC50) of 0.19 and 0.31 mM, respectively. The inhibition was AMO-specific in 'Ca. N. franklandus' C13 in the presence of C1-C2 alcohols, and in N. europaea in the presence of C1-C3 alcohols. Higher chain-length alcohols caused non-specific inhibition and also inhibited hydroxylamine oxidation. Ethanol was tolerated by 'Ca. N. franklandus' C13 at a higher threshold concentration than other chain-length alcohols, with 80 mM ethanol being required for complete inhibition of ammonia oxidation.
氨氧化菌是全球氮循环中的关键角色,负责将氨氧化为亚硝酸盐,然后被其他微生物进一步氧化为硝酸盐。它们的活动可能对一些受人类影响的环境产生不利影响,包括通过硝酸盐浸出和温室气体氧化亚氮(N2O)排放导致的水污染。氨单加氧酶(AMO)是微生物氨氧化的关键酶,存在于所有好氧氨氧化菌中。氨单加氧酶尚未以活性形式被纯化,并且关于其潜在结构和功能的大部分知识来自于对其与抑制剂相互作用的研究。由于氨氧化古菌比它们的细菌对应物发现得晚得多,因此对其氨单加氧酶的研究较少。本研究使用模式陆地氨氧化古菌“Candidatus Nitrosocosmicus franklandus”C13 和氨氧化细菌 Nitrosomonas europaea 考察了脂肪醇(C1-C8)对氨氧化的抑制作用,以扩展对氨氧化菌抑制剂范围的认识。甲醇是两种氨氧化菌中 AMO 的最有效特异性抑制剂,其半最大抑制浓度(IC50)分别为 0.19 和 0.31 mM。在 C1-C2 醇存在的情况下,抑制作用是“Ca. N. franklandus”C13 中的 AMO 特异性的,而在 C1-C3 醇存在的情况下,抑制作用是 N. europaea 中的 AMO 特异性的。较长链长的醇引起非特异性抑制,并且还抑制羟胺氧化。与其他链长的醇相比,乙醇在“Ca. N. franklandus”C13 中被更高的阈值浓度耐受,需要 80 mM 乙醇才能完全抑制氨氧化。