Universität zu Köln

Versantvoort, Wouter ORCID: 0000-0001-5418-2741, Guerrero-Castillo, Sergio ORCID: 0000-0002-6630-0562, Wessels, Hans J. C. T., van Niftrik, Laura ORCID: 0000-0002-7011-7234, Jetten, Mike S. M., Brandt, Ulrich ORCID: 0000-0003-1869-6811, Reimann, Joachim and Kartal, Boran ORCID: 0000-0003-4199-952X (2019). Complexome analysis of the nitrite-dependent methanotroph Methylomirabilis lanthanidiphila. Biochim. Biophys. Acta-Bioenerg., 1860 (9). S. 734 - 745. AMSTERDAM: ELSEVIER. ISSN 1879-2650

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Abstract

The atmospheric concentration of the potent greenhouse gases methane and nitrous oxide (N2O) has increased drastically during the last century. Methylomirabilis bacteria can play an important role in controlling the emission of these two gases from natural ecosystems, by oxidizing methane to CO2 and reducing nitrite to N-2 without producing N2O. These bacteria have an anaerobic metabolism, but are proposed to possess an oxygen-dependent pathway for methane activation. Methylomirabilis bacteria reduce nitrite to NO, and are proposed to dismutate NO into O-2 and N-2 by a putative NO dismutase (NO-D). The O-2 produced in the cell can then be used to activate methane by a particulate methane monooxygenase. So far, the metabolic model of Methylomirabilis bacteria was based mainly on (meta)genomics and physiological experiments. Here we applied a complexome profiling approach to determine which of the proposed enzymes are actually expressed in Methylomirabilis lanthanidiphila. To validate the proposed metabolic model, we focused on enzymes involved in respiration, as well as nitrogen and carbon transformation. All complexes suggested to be involved in nitrite-dependent methane oxidation, were identified in M. lanthanidiphila, including the putative NO-D. Furthermore, several complexes involved in nitrate reduction/nitrite oxidation and NO reduction were detected, which likely play a role in detoxification and redox homeostasis. In conclusion, complexome profiling validated the expression and composition of enzymes hypothesized to be involved in the energy, methane and nitrogen metabolism of M. lanthanidiphila, thereby further corroborating their unique metabolism involved in the environmentally relevant process of nitrite-dependent methane oxidation.

Item Type:	Journal Article
Creators:	Creators Email ORCID ORCID Put Code Versantvoort, Wouter UNSPECIFIED orcid.org/0000-0001-5418-2741 UNSPECIFIED Guerrero-Castillo, Sergio UNSPECIFIED orcid.org/0000-0002-6630-0562 UNSPECIFIED Wessels, Hans J. C. T. UNSPECIFIED UNSPECIFIED UNSPECIFIED van Niftrik, Laura UNSPECIFIED orcid.org/0000-0002-7011-7234 UNSPECIFIED Jetten, Mike S. M. UNSPECIFIED UNSPECIFIED UNSPECIFIED Brandt, Ulrich UNSPECIFIED orcid.org/0000-0003-1869-6811 UNSPECIFIED Reimann, Joachim UNSPECIFIED UNSPECIFIED UNSPECIFIED Kartal, Boran UNSPECIFIED orcid.org/0000-0003-4199-952X UNSPECIFIED
URN:	urn:nbn:de:hbz:38-142040
DOI:	10.1016/j.bbabio.2019.07.011
Journal or Publication Title:	Biochim. Biophys. Acta-Bioenerg.
Volume:	1860
Number:	9
Page Range:	S. 734 - 745
Date:	2019
Publisher:	ELSEVIER
Place of Publication:	AMSTERDAM
ISSN:	1879-2650
Language:	English
Faculty:	Unspecified
Divisions:	Unspecified
Subjects:	no entry
Uncontrolled Keywords:	Keywords Language METHYLENE-TETRAHYDROMETHANOPTERIN DEHYDROGENASE; ANAEROBIC METHANE OXIDATION; CRYSTAL-STRUCTURE; METHENYLTETRAHYDROMETHANOPTERIN CYCLOHYDROLASE; SUPRAMOLECULAR ORGANIZATION; RESPIRATORY CHAINS; NITRATE REDUCTION; BACTERIA; EVOLUTION; PROTEINS Multiple languages Biochemistry & Molecular Biology; Biophysics Multiple languages
Refereed:	Yes
URI:	http://kups.ub.uni-koeln.de/id/eprint/14204