English
 
User Manual Privacy Policy Disclaimer Contact us
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Structural basis of biological NO generation by octaheme oxidoreductases

Maalcke, W. J., Dietl, A., Marritt, S. J., Butt, J. N., Jetten, M. S., T.Keltjens, J., et al. (2013). Structural basis of biological NO generation by octaheme oxidoreductases. The Journal of Biological Chemistry, 289(3), 1228-1242. doi:10.1074/jbc.M113.525147.

Item is

Basic

show hide
Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-8FA6-4 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-8FA7-2
Genre: Journal Article

Files

show Files
hide Files
:
JBiolChem_289_2014_1228.pdf (Any fulltext), 2MB
 
File Permalink:
-
Name:
JBiolChem_289_2014_1228.pdf
Description:
-
Visibility:
Restricted (Max Planck Institute for Medical Research, MHMF; )
MIME-Type / Checksum:
application/pdf
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show

Creators

show
hide
 Creators:
Maalcke, Wouter J., Author
Dietl, Andreas1, Author              
Marritt, Sophie J., Author
Butt, Julea N., Author
Jetten, Mike S.M., Author
T.Keltjens, Jan, Author
Barends, Thomas1, Author              
Kartal, Boran, Author
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

Content

show
hide
Free keywords: Anaerobic Ammonium Oxidation, Enzyme Kinetics, Enzyme Purification, Hydroxylamine, Nitric Oxide, Nitrogen Metabolism, Octaheme Proteins, Protein Structure, Reactive Nitrogen Species, X-ray Crystallography
 Abstract: Nitric oxide is an important molecule in all domains of life with significant biological functions in both pro- and eukaryotes. Anaerobic ammonium-oxidizing (anammox) bacteria that contribute substantially to the release of fixed nitrogen into the atmosphere use the oxidizing power of NO to activate inert ammonium into hydrazine (N2H4). Here, we describe an enzyme from the anammox bacterium Kuenenia stuttgartiensis that uses a novel pathway to make NO from hydroxylamine. This new enzyme is related to octaheme hydroxylamine oxidoreductase, a key protein in aerobic ammonium-oxidizing bacteria. By a multiphasic approach including the determination of the crystal structure of the K. stuttgartiensis enzyme at 1.8 Å resolution and refinement and reassessment of the hydroxylamine oxidoreductase structure from Nitrosomonas europaea, both in the presence and absence of their substrates, we propose a model for NO formation by the K. stuttgartiensis enzyme. Our results expand the understanding of the functions that the widespread family of octaheme proteins have

Details

show
hide
Language(s): eng - English
 Dates: 2013-10-112013-12-032013-12-032013-01-17
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1074/jbc.M113.525147
Other: 7941
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: The Journal of Biological Chemistry
  Other : JBC
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 289 (3) Sequence Number: - Start / End Page: 1228 - 1242 Identifier: ISSN: 0021-9258
CoNE: https://pure.mpg.de/cone/journals/resource/954925410826_1