Article(id=1226554097130717322, tenantId=1146029695717560320, journalId=1192105938417971205, issueId=1226554095926952065, articleNumber=null, orderNo=null, doi=10.13343/j.cnki.wsxb.20240858, pmid=null, cstr=null, oa=null, hot=null, price=null, onlineType=0, articleFormat=0, articleType=null, articleTypeStr=research-article, receivedDate=1735574400000, receivedDateStr=2024-12-31, revisedDate=null, revisedDateStr=null, acceptedDate=1741622400000, acceptedDateStr=2025-03-11, onlineDate=1770362885029, onlineDateStr=2026-02-06, pubDate=1751558400000, pubDateStr=2025-07-04, doiRegisterDate=null, doiRegisterDateStr=null, onlineIssueDate=1770362885029, onlineIssueDateStr=2026-02-06, onlineJustAcceptDate=null, onlineJustAcceptDateStr=null, onlineFirstDate=null, onlineFirstDateStr=null, sourceXml=null, magXml=null, createTime=1770362885029, creator=13701087609, updateTime=1770362885029, updator=13701087609, issue=Issue{id=1226554095926952065, tenantId=1146029695717560320, journalId=1192105938417971205, year='2025', volume='65', issue='7', pageStart='2771', pageEnd='3233', issueExtLink='null', onlineDate='null', pubDate='null', beforeIssueId=null, nextIssueId=null, price=null, status=1, issueComplete=1, articleOrder=1, issueType=-1, specialIssue=null, createTime=1770362884741, creator=13701087609, updateTime=1770363575040, updator=13701087609, preIssue=null, nextIssue=null, ext={EN=IssueExt(id=1226556991309529548, tenantId=1146029695717560320, journalId=1192105938417971205, issueId=1226554095926952065, language=EN, specialIssueTitle=, coverIllustrator=null, specialIssueEditor=, specialIssueAbout=), CN=IssueExt(id=1226556991309529549, tenantId=1146029695717560320, journalId=1192105938417971205, issueId=1226554095926952065, language=CN, specialIssueTitle=, coverIllustrator=null, specialIssueEditor=, specialIssueAbout=)}, issueFiles=null}, startPage=2841, endPage=2853, ext={EN=ArticleExt(id=1226554097386569870, articleId=1226554097130717322, tenantId=1146029695717560320, journalId=1192105938417971205, language=EN, title=Research progress in the role of hydroxylamine in the nitrogen cycle and its impact on N₂O emissions, columnId=1192149543727808575, journalTitle=Acta Microbiologica Sinica, columnName=Review, runingTitle=null, highlight=null, articleAbstract=

Hydroxylamine, as an important intermediate product in the nitrogen cycle, connects ammonia oxidation and nitrite oxidation, influencing the velocities and directions of processes like ammonia oxidation, nitrite oxidation, and denitrification. Because of the close associations with the generation of N₂O through enzymatic reactions and self-decomposition or reactions with other substances, hydroxylamine has become a focus and hotspot of research. This paper summarized the generation and transformation of hydroxylamine in autotrophic and heterotrophic ammonia oxidation, the key role of hydroxylamine in the nitrogen cycle, and the promoting effect of hydroxylamine on N₂O emissions. It analyzed the processes of autotrophic and heterotrophic ammonia oxidation and their enzymatic differences, aiming to provide a theoretical reference for in-depth research on the role of hydroxylamine in the microbial nitrogen cycle and for the research and development of measures to reduce N₂O emissions and protect the atmospheric environment.

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羟胺作为氮循环的重要中间产物，连接氨氧化和亚硝态氮氧化过程，影响着氨氧化、亚硝态氮氧化、反硝化等过程的速度与方向，并通过相关酶促反应、自身分解或与其他物质反应与氧化亚氮(nitrous oxide, N₂O)的产生密切相关，已成为研究的重点和热点。本文总结了羟胺在自养和异养氨氧化过程中的生成与转化、在氮循环中的关键作用以及对N₂O排放的促进作用，分析了自养和异养氨氧化过程及其酶学差异，为深入研究羟胺在微生物氮循环中的作用机制、研发N₂O减排措施和保护大气环境提供了理论参考。

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Environmental Science & Technology, 2023, 57(7): 2970-2980., articleTitle=Contribution of ammonium-induced nitrifier denitrification to N₂O in paddy fields, refAbstract=null)], funds=[Fund(id=1227681723299853309, tenantId=1146029695717560320, journalId=1192105938417971205, articleId=1226554097130717322, awardId=42077217, language=EN, fundingSource=National Natural Science Foundation of China(42077217), fundOrder=null, country=null), Fund(id=1227681723417292812, tenantId=1146029695717560320, journalId=1192105938417971205, articleId=1226554097130717322, awardId=42077217, language=CN, fundingSource=国家自然科学基金(42077217), fundOrder=null, country=null)], companyList=[AuthorCompany(id=1227681717754983010, tenantId=1146029695717560320, journalId=1192105938417971205, articleId=1226554097130717322, xref=null, ext=[AuthorCompanyExt(id=1227681717775954532, tenantId=1146029695717560320, journalId=1192105938417971205, articleId=1226554097130717322, companyId=1227681717754983010, language=EN, country=null, province=null, city=null, postcode=null, companyName=null, departmentName=null, remark=Chongqing Key Laboratory of Interface Process and Soil Health, College of Resources and Environment, Southwest University, Chongqing, China), AuthorCompanyExt(id=1227681717780148838, tenantId=1146029695717560320, journalId=1192105938417971205, articleId=1226554097130717322, companyId=1227681717754983010, language=CN, country=null, province=null, city=null, postcode=null, companyName=null, departmentName=null, remark=西南大学 资源环境学院，重庆市界面过程与土壤健康重点实验室，重庆)])], figs=[ArticleFig(id=1227681722272248726, tenantId=1146029695717560320, journalId=1192105938417971205, articleId=1226554097130717322, language=EN, label=Figure 1, caption=Schematic diagram of AMO of autotrophic ammonia oxidizing bacteria. figures A, B, and C respectively show the schematic diagrams of the AMO structures of AOA, AOB, and complete ammonia oxidizers (Comammox). AmoA, AmoB, and AmoC (yellow) are conserved and form a trimer (AmoABC). AmoB and AmoC contain copper ion-binding sites, which are conserved in ammonia-oxidizing archaea (AOA) and ammonia-oxidizing bacteria (AOB). A: AmoX (in red), AmoY (in green), and AmoZ (in purple) are the putative auxiliary proteins of archaeal AMO, respectively. B: AmoD (in blue) and AmoE (in purple) are the auxiliary proteins found in AOB, respectively. C: AmoD′ (in dark blue), and AmoE′ (in dark purple) are the homologues of AmoD and AmoE found in Comammox, respectively., figureFileSmall=OPgH8dqVX2DB5dL/asDBfg==, figureFileBig=jUlQR6HgCUKmswna7dPmDA==, tableContent=null), ArticleFig(id=1227681722385494948, tenantId=1146029695717560320, journalId=1192105938417971205, articleId=1226554097130717322, language=CN, label=图1, caption=自养氨氧化菌AMO结构示意图。A、B、C分别表示AOA、AOB、Comammox的AMO结构示意图。AmoA、AmoB和AmoC (黄色)保守，形成三聚体(AmoABC)。AmoB和AmoC含有铜离子结合位点，在AOA和AOB中是保守的。A：AmoX (红色)、AmoY (绿色)和AmoZ (紫色)是推测的古菌AMO辅助蛋白；B：AmoD (蓝色)和AmoE (紫色)是AOB中发现的辅助蛋白；C：AmoD′ (深蓝色)和AmoE′ (深紫色)是Comammox中发现的AmoD和AmoE的同系物。, figureFileSmall=OPgH8dqVX2DB5dL/asDBfg==, figureFileBig=jUlQR6HgCUKmswna7dPmDA==, tableContent=null), ArticleFig(id=1227681722515518383, tenantId=1146029695717560320, journalId=1192105938417971205, articleId=1226554097130717322, language=EN, label=Figure 2, caption=The generation and transformation processes of hydroxylamine in the aerobic ammonia oxidation by AOA and the related enzymes^[8]., figureFileSmall=D2M/9qJu3xZwaDG4zZbJTA==, figureFileBig=jZPfdLaxo33qL//1LMoGvw==, tableContent=null), ArticleFig(id=1227681722645541820, tenantId=1146029695717560320, journalId=1192105938417971205, articleId=1226554097130717322, language=CN, label=图2, caption=羟胺在AOA好氧氨氧化中的生成与转化过程及相关酶^[8], figureFileSmall=D2M/9qJu3xZwaDG4zZbJTA==, figureFileBig=jZPfdLaxo33qL//1LMoGvw==, tableContent=null), ArticleFig(id=1227681722758788036, tenantId=1146029695717560320, journalId=1192105938417971205, articleId=1226554097130717322, language=EN, label=Figure 3, caption=The generation and transformation of hydroxylamine in ammonia oxidation by AOB and Comammox and the related enzymes., figureFileSmall=HxFVCrVjAT3TKz3KabnGGg==, figureFileBig=J+nSxiiioEcl/Kk7thZIRg==, tableContent=null), ArticleFig(id=1227681722880422864, tenantId=1146029695717560320, journalId=1192105938417971205, articleId=1226554097130717322, language=CN, label=图3, caption=羟胺在AOB和Comammox氨氧化中的生成与转化及相关酶, figureFileSmall=HxFVCrVjAT3TKz3KabnGGg==, figureFileBig=J+nSxiiioEcl/Kk7thZIRg==, tableContent=null), ArticleFig(id=1227681722981086170, tenantId=1146029695717560320, journalId=1192105938417971205, articleId=1226554097130717322, language=EN, label=Table 1, caption=

Hydroxylamine in HAOB and the genes and enzymes related to its generation and transformation

, figureFileSmall=null, figureFileBig=null, tableContent=

Microorganisms	amoA	AMO	NH2OH	hao	HAO	Reference
Alcaligenes faecalis strain NR	-		+		+	[33]
Arthrobacter arilaitensis			+		+	[34]
Arthrobacter sp. HHEP5	+			+		[35]
Acinetobacter sp. ND7			-	+		[36]
Acinetobacter junii YB			+	+		[37]
Pseudomonas aeruginosa P-1	+	+			+	[38]
Sphingomonas sp. YY2	+			+		[39]
Klebsiella sp. KSND	-			-		[40-41]
Bacillus sp. K5					+	[42]
Thauera sp. SND5	-		-	-		[43]
Sporidiobolus pararoseus Y1	+					[44]
Streptomyces mediolani EM-B2		+	-		+	[45]
Pseudomonas sp. JQ-H3	+	+	+		+	[46]

), ArticleFig(id=1227681723115303913, tenantId=1146029695717560320, journalId=1192105938417971205, articleId=1226554097130717322, language=CN, label=表1, caption=

HAOB中的羟胺及其生成和转化有关的基因和酶

, figureFileSmall=null, figureFileBig=null, tableContent=

Microorganisms	amoA	AMO	NH2OH	hao	HAO	Reference
Alcaligenes faecalis strain NR	-		+		+	[33]
Arthrobacter arilaitensis			+		+	[34]
Arthrobacter sp. HHEP5	+			+		[35]
Acinetobacter sp. ND7			-	+		[36]
Acinetobacter junii YB			+	+		[37]
Pseudomonas aeruginosa P-1	+	+			+	[38]
Sphingomonas sp. YY2	+			+		[39]
Klebsiella sp. KSND	-			-		[40-41]
Bacillus sp. K5					+	[42]
Thauera sp. SND5	-		-	-		[43]
Sporidiobolus pararoseus Y1	+					[44]
Streptomyces mediolani EM-B2		+	-		+	[45]
Pseudomonas sp. JQ-H3	+	+	+		+	[46]

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