Transformations of Aromatic Compounds by Nitrosomonas europaea

Author:

Keener William K.1,Arp Daniel J.1

Affiliation:

1. Laboratory for Nitrogen Fixation Research, Oregon State University, Corvallis, Oregon 97331-2902

Abstract

Benzene and a variety of substituted benzenes inhibited ammonia oxidation by intact cells of Nitrosomonas europaea. In most cases, the inhibition was accompanied by transformation of the aromatic compound to a more oxidized product or products. All products detected were aromatic, and substituents were often oxidized but were not separated from the benzene ring. Most transformations were enhanced by (NH 4 ) 2 SO 4 (12.5 mM) and were prevented by C 2 H 2 , a mechanism-based inactivator of ammonia monooxygenase (AMO). AMO catalyzed alkyl substituent hydroxylations, styrene epoxidation, ethylbenzene desaturation to styrene, and aniline oxidation to nitrobenzene (and unidentified products). Alkyl substituents were preferred oxidation sites, but the ring was also oxidized to produce phenolic compounds from benzene, ethylbenzene, halobenzenes, phenol, and nitrobenzene. No carboxylic acids were identified. Ethylbenzene was oxidized via styrene to two products common also to oxidation of styrene; production of styrene is suggestive of an electron transfer mechanism for AMO. Iodobenzene and 1,2-dichlorobenzene were oxidized slowly to halophenols; 1,4-dichlorobenzene was not transformed. No 2-halophenols were detected as products. Several hydroxymethyl (-CH 2 OH)-substituted aromatics and p -cresol were oxidized by C 2 H 2 -treated cells to the corresponding aldehydes, benzaldehyde was reduced to benzyl alcohol, and o -cresol and 2,5-dimethylphenol were not depleted.

Publisher

American Society for Microbiology

Subject

Ecology,Applied Microbiology and Biotechnology,Food Science,Biotechnology

Reference33 articles.

1. Accessibility to the active site of methane monooxygenase: the first demonstration of exogenous ligand binding to the diiron cluster;Andersson K. K.;J. Am. Chem. Soc.,1992

2. Physiology, biochemistry, and specific inhibitors of CH4, NH4', and CO oxidation by methanotrophs and nitrifiers;Bedard C.;Microbiol. Rev.,1989

3. Bond energies;Benson S. W.;J. Chem. Educ.,1965

4. Mechanisms of hydroxylation by cytochrome P-450: metabolism of monohalobenzenes by phenobarbital-induced microsomes;Burka L. T.;Proc. Natl. Acad. Sci. USA,1983

5. Substrate specificities of the soluble and particulate methane monooxygenases of Methylosinus trichosporium OB3b;Burrows K. J.;J. Gen. Microbiol.,1984

同舟云学术

1.学者识别学者识别

2.学术分析学术分析

3.人才评估人才评估

"同舟云学术"是以全球学者为主线,采集、加工和组织学术论文而形成的新型学术文献查询和分析系统,可以对全球学者进行文献检索和人才价值评估。用户可以通过关注某些学科领域的顶尖人物而持续追踪该领域的学科进展和研究前沿。经过近期的数据扩容,当前同舟云学术共收录了国内外主流学术期刊6万余种,收集的期刊论文及会议论文总量共计约1.5亿篇,并以每天添加12000余篇中外论文的速度递增。我们也可以为用户提供个性化、定制化的学者数据。欢迎来电咨询!咨询电话:010-8811{复制后删除}0370

www.globalauthorid.com

TOP

Copyright © 2019-2024 北京同舟云网络信息技术有限公司
京公网安备11010802033243号  京ICP备18003416号-3