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Hydroxylamine oxidoreductase from Nitrosomonas: absorption spectra and content of heme and metal.

作者信息

Hooper A B, Maxwell P C, Terry K R

出版信息

Biochemistry. 1978 Jul 25;17(15):2984-9. doi: 10.1021/bi00608a007.

DOI:10.1021/bi00608a007
PMID:698180
Abstract
摘要

相似文献

1
Hydroxylamine oxidoreductase from Nitrosomonas: absorption spectra and content of heme and metal.
Biochemistry. 1978 Jul 25;17(15):2984-9. doi: 10.1021/bi00608a007.
2
Highly purified hydroxylamine oxidoreductase derived from Nitrosomonas europaea. Some physicochemical and enzymatic properties.源自欧洲亚硝化单胞菌的高度纯化的羟胺氧化还原酶。一些物理化学和酶学性质。
J Biochem. 1979 Oct;86(4):1101-8. doi: 10.1093/oxfordjournals.jbchem.a132604.
3
Spectroscopic and rapid kinetic studies of reduction of cytochrome c554 by hydroxylamine oxidoreductase from Nitrosomonas europaea.欧洲亚硝化单胞菌中羟胺氧化还原酶还原细胞色素c554的光谱及快速动力学研究
Biochemistry. 1991 Dec 3;30(48):11466-72. doi: 10.1021/bi00112a014.
4
Studies on the hydroxylamine metabolism of Nitrosomonas europaea. II. Molecular properties of the electron-transport particle, hydroxylamine oxidase.欧洲亚硝化单胞菌羟胺代谢的研究。II. 电子传递颗粒——羟胺氧化酶的分子特性
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5
Resolution of multiple heme centers of hydroxylamine oxidoreductase from Nitrosomonas. 2. Mössbauer spectroscopy.
Biochemistry. 1982 Aug 17;21(17):3973-6. doi: 10.1021/bi00260a011.
6
The partial characterization of purified nitrite reductase and hydroxylamine oxidase from Nitrosomonas europaea.欧洲亚硝化单胞菌纯化的亚硝酸还原酶和羟胺氧化酶的部分特性
Biochem J. 1974 Mar;138(3):471-80. doi: 10.1042/bj1380471.
7
Suicide inactivation of hydroxylamine oxidoreductase of Nitrosomonas europaea by organohydrazines.欧洲亚硝化单胞菌的羟胺氧化还原酶被有机肼自杀失活。
Biochemistry. 1995 Jul 18;34(28):9257-64. doi: 10.1021/bi00028a039.
8
Heme P460 of hydroxylamine oxidoreductase of Nitrosomonas. Reaction with CO and H2O2.亚硝化单胞菌羟胺氧化还原酶的血红素P460。与一氧化碳和过氧化氢的反应。
Eur J Biochem. 1983 Jul 15;134(1):83-7. doi: 10.1111/j.1432-1033.1983.tb07534.x.
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Resolution of the hemes of hydroxylamine oxidoreductase by redox potentiometry and optical spectroscopy.通过氧化还原电位滴定法和光谱法解析羟胺氧化还原酶的血红素
FEBS Lett. 1983 Oct 31;163(1):25-7. doi: 10.1016/0014-5793(83)81154-5.
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Studies of the hydroxylamine metabolism of Nitrosomonas europaea. I. Purification of hydroxylamine oxidase.欧洲亚硝化单胞菌羟胺代谢的研究。I. 羟胺氧化酶的纯化。
Biochemistry. 1968 Jan;7(1):353-66. doi: 10.1021/bi00841a045.

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Role of Nitric Oxide in Hydroxylamine Oxidation by Ammonia-Oxidizing Bacteria.一氧化氮在硝化细菌羟胺氧化中的作用。
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Revision of N2O-producing pathways in the ammonia-oxidizing bacterium Nitrosomonas europaea ATCC 19718.欧洲亚硝化单胞菌ATCC 19718中一氧化二氮产生途径的修订
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多血红素蛋白:自然界的电子多功能工具。
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Comparison among amoA primers suited for quantification and diversity analyses of ammonia-oxidizing bacteria in soil.比较适用于土壤氨氧化细菌定量和多样性分析的 amoA 引物。
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Kinetic and product distribution analysis of NO* reductase activity in Nitrosomonas europaea hydroxylamine oxidoreductase.欧洲亚硝化单胞菌羟胺氧化还原酶中NO*还原酶活性的动力学及产物分布分析
J Biol Inorg Chem. 2008 Sep;13(7):1073-83. doi: 10.1007/s00775-008-0393-4. Epub 2008 Jun 14.
6
The crystal structure of cytochrome P460 of Nitrosomonas europaea reveals a novel cytochrome fold and heme-protein cross-link.欧洲亚硝化单胞菌细胞色素P460的晶体结构揭示了一种新型的细胞色素折叠和血红素-蛋白质交联。
Biochemistry. 2007 Jul 17;46(28):8340-9. doi: 10.1021/bi700086r. Epub 2007 Jun 21.
7
Isolation of a multiheme protein with features of a hydrazine-oxidizing enzyme from an anaerobic ammonium-oxidizing enrichment culture.从厌氧氨氧化富集培养物中分离出一种具有肼氧化酶特征的多血红素蛋白。
Appl Environ Microbiol. 2007 Feb;73(4):1065-72. doi: 10.1128/AEM.01978-06. Epub 2006 Dec 15.
8
O isotope shift in N NMR analysis of biological N-oxidations: H(2)O-NO(2) exchange in the ammonia-oxidizing bacterium Nitrosomonas.N 核磁共振分析中 N 同位素位移:氨氧化细菌硝化单胞菌中 H(2)O-NO(2) 交换。
Proc Natl Acad Sci U S A. 1982 Oct;79(19):5871-5. doi: 10.1073/pnas.79.19.5871.
9
Expression, purification, crystallization and preliminary X-ray diffraction of a novel Nitrosomonas europaea cytochrome, cytochrome P460.新型欧洲亚硝化单胞菌细胞色素——细胞色素P460的表达、纯化、结晶及初步X射线衍射分析
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Apr 1;62(Pt 4):395-8. doi: 10.1107/S1744309106008785. Epub 2006 Mar 25.
10
The evolution of nitrogen cycling.氮循环的演变
Orig Life Evol Biosph. 1988;18:311-25. doi: 10.1007/BF01808213.