Jump to ContentJump to Main Navigation
Show Summary Details
In This Section

Thomas, Douglas D.

Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Turk, Boris / Wittinghofer, Alfred

12 Issues per year


IMPACT FACTOR 2016: 3.273

CiteScore 2016: 3.01

SCImago Journal Rank (SJR) 2015: 1.607
Source Normalized Impact per Paper (SNIP) 2015: 0.751

Online
ISSN
1437-4315
See all formats and pricing
In This Section
Volume 390, Issue 9 (Sep 2009)

Issues

A soluble form of ammonia monooxygenase in Nitrosomonas europaea

Stefan Gilch
  • Department of Microbiology, University of Bayreuth, D-95447 Bayreuth, Germany
/ Ortwin Meyer
  • Department of Microbiology, University of Bayreuth, D-95447 Bayreuth, Germany
/ Ingo Schmidt
  • Department of Microbiology, University of Bayreuth, D-95447 Bayreuth, Germany
Published Online: 2009-05-20 | DOI: https://doi.org/10.1515/BC.2009.085

Abstract

Ammonia monooxygenase (AMO) of Nitrosomonas europaea is a metalloenzyme that catalyzes the oxidation of ammonia to hydroxylamine. This study shows that AMO resides in the cytoplasm of the bacteria in addition to its location in the membrane and is distributed approximately equally in both subcellular fractions. AMO in both fractions catalyzes the oxidation of ammonia and binds [14C]acetylene, a mechanism-based inhibitor which specifically interacts with catalytically active AMO. Soluble AMO was purified 12-fold to electrophoretic homogeneity with a yield of 8%. AMO has a molecular mass of approximately 283 kDa with subunits of ca. 27 kDa (α-subunit, AmoA), ca. 42 kDa (β-subunit, AmoB), and ca. 24 kDa (γ-subunit, cytochrome c 1) in an α3β3γ3 sub-unit structure. Different from the β-subunit of membrane-bound AMO, AmoB of soluble AMO possesses an N-terminal signal sequence. AMO contains Cu (9.4±0.6 mol per mol AMO), Fe (3.9±0.3 mol per mol AMO), and Zn (0.5 to 2.6 mol per mol AMO). Upon reduction the visible absorption spectrum of AMO reveals absorption bands characteristic of cytochrome c. Electron para-magnetic resonance spectroscopy of air-oxidized AMO at 50 K shows a paramagnetic signal originating from Cu2+ and at 10 K a paramagnetic signal characteristic of heme-Fe.

Keywords: acetylene; ammonia monooxygenase (AMO); AmoA; AmoB; copper and iron enzyme; cytochrome c 1; N-terminal signal sequence; purification

About the article

Corresponding author


Received: 2009-02-17

Accepted: 2009-04-25

Published Online: 2009-05-20

Published in Print: 2009-09-01



Citation Information: Biological Chemistry, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2009.085. Export Citation

Citing Articles

Here you can find all Crossref-listed publications in which this article is cited. If you would like to receive automatic email messages as soon as this article is cited in other publications, simply activate the “Citation Alert” on the top of this page.

[1]
Pierre Offre, Melina Kerou, Anja Spang, and Christa Schleper
Trends in Microbiology, 2014, Volume 22, Number 12, Page 665
[2]
Ke Qin, Garrett C. Struckhoff, Abinash Agrawal, Michael L. Shelley, and Hailiang Dong
Chemosphere, 2015, Volume 119, Page 971
[3]
Achlesh Daverey, Yi-Chian Chen, Shihwu Sung, and Jih-Gaw Lin
Bioresource Technology, 2014, Volume 165, Page 105
[4]
Jianhua Guo, Yongzhen Peng, Shuying Wang, Bin Ma, Shijian Ge, Zhongwei Wang, Huijun Huang, Jingrong Zhang, and Liang Zhang
Critical Reviews in Environmental Science and Technology, 2013, Volume 43, Number 21, Page 2213
[5]

Comments (0)

Please log in or register to comment.
Log in