Universität zu Köln

Bender, Daniel ORCID: 0000-0002-2975-4186 and Schwarz, Guenter ORCID: 0000-0002-2118-9338 (2018). Nitrite-dependent nitric oxide synthesis by molybdenum enzymes. FEBS Lett., 592 (12). S. 2126 - 2140. HOBOKEN: WILEY. ISSN 1873-3468

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Abstract

Nitric oxide (NO) is an important gasotransmitter involved in numerous intra- and intercellular signaling events. In addition to the oxidative pathway of NO generation, which includes three NO synthase (NOS) isoforms in mammals, a reductive pathway contributes to NO generation. In this pathway, nitrite is reduced to NO by various metal-containing proteins. Among these, all members of the eukaryotic molybdenum (Mo)-dependent enzyme family were found to be able to reduce nitrite to NO. This Review focuses on the current state of research in the field of Mo-dependent nitrite reduction in eukaryotes. An overview on the five eukaryotic Mo-enzymes is given, and similarities as well as differences in their nitrite reduction mechanisms are presented and discussed in the context of physiological relevance.

Item Type:	Journal Article
Creators:	Creators Email ORCID ORCID Put Code Bender, Daniel UNSPECIFIED orcid.org/0000-0002-2975-4186 UNSPECIFIED Schwarz, Guenter UNSPECIFIED orcid.org/0000-0002-2118-9338 UNSPECIFIED
URN:	urn:nbn:de:hbz:38-183349
DOI:	10.1002/1873-3468.13089
Journal or Publication Title:	FEBS Lett.
Volume:	592
Number:	12
Page Range:	S. 2126 - 2140
Date:	2018
Publisher:	WILEY
Place of Publication:	HOBOKEN
ISSN:	1873-3468
Language:	English
Faculty:	Faculty of Mathematics and Natural Sciences
Divisions:	Faculty of Mathematics and Natural Sciences > Department of Chemistry > Institute of Biochemistry
Subjects:	no entry
Uncontrolled Keywords:	Keywords Language ISCHEMIA-REPERFUSION INJURY; REDUCING COMPONENT MARC; PLANT NITRATE REDUCTASE; LIVER ALDEHYDE OXIDASE; SMOOTH-MUSCLE-CELLS; SULFITE OXIDASE; XANTHINE-OXIDASE; S-NITROSYLATION; IN-VIVO; SYNTHASE ACTIVITY Multiple languages Biochemistry & Molecular Biology; Biophysics; Cell Biology Multiple languages
Refereed:	Yes
URI:	http://kups.ub.uni-koeln.de/id/eprint/18334