English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  NADH Oxidation by the Na+-translocating NADH:Quinone Oxidoreductase from Vibrio cholerae: FUNCTIONAL ROLE OF THE NqrF SUBUNIT

Türk, K., Puhar, A., Neese, F., Bill, E., Fritz, G., & Steuber, J. (2004). NADH Oxidation by the Na+-translocating NADH:Quinone Oxidoreductase from Vibrio cholerae: FUNCTIONAL ROLE OF THE NqrF SUBUNIT. The Journal of Biological Chemistry, 279(20), 21349-21355. doi:10.1074/jbc.M311692200.

Item is

Basic

show hide
Genre: Journal Article

Files

show Files

Locators

show

Creators

show
hide
 Creators:
Türk, Karin1, Author
Puhar, Andrea1, Author
Neese, Frank2, Author           
Bill, Eckhard2, Author           
Fritz, Günter3, Author
Steuber, Julia1, Author
Affiliations:
1Mikrobiologisches Institut der Eidgenössischen Technischen Hochschule, ETH-Zentrum, CH-8092 Zürich, Switzerland, ou_persistent22              
2Research Department Wieghardt, Max Planck Institute for Bioinorganic Chemistry, Max Planck Society, ou_3023881              
3Fachbereich Biologie, Universität Konstanz, D-78457 Konstanz, Germany, ou_persistent22              

Content

show
hide
Free keywords: -
 Abstract: The Na+-translocating NADH:quinone oxidoreductase from Vibrio cholerae is a six subunit enzyme containing four flavins and a single motif for the binding of a Fe-S cluster on its NqrF subunit. This study reports the production of a soluble variant of NqrF (NqrF′) and its individual flavin and Fe-S-carrying domains using V. cholerae or Escherichia coli as expression hosts. NqrF′ and the flavin domain each contain 1 mol of FAD/mol of enzyme and exhibit high NADH oxidation activity (20,000 μmol min-1 mg-1). EPR, visible absorption, and circular dichroism spectroscopy indicate that the Fe-S cluster in NqrF′ and its Fe-S domain is related to 2Fe ferredoxins of the vertebrate-type. The addition of NADH to NqrF′ results in the formation of a neutral flavosemiquinone and a partial reduction of the Fe-S cluster. The NqrF subunit harbors the active site of NADH oxidation and acts as a converter between the hydride donor NADH and subsequent one-electron reaction steps in the Na+-translocating NADH:quinone oxidoreductase complex. The observed electron transfer NADH → FAD → [2Fe-2S] in NqrF requires positioning of the FAD and the Fe-S cluster in close proximity in accordance with a structural model of the subunit.

Details

show
hide
Language(s): eng - English
 Dates: 2003-10-242004-05-14
 Publication Status: Published in print
 Pages: 7
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1074/jbc.M311692200
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: The Journal of Biological Chemistry
  Other : JBC
  Abbreviation : J. Biol. Chem.
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: Baltimore, etc. : American Society for Biochemistry and Molecular Biology [etc.]
Pages: - Volume / Issue: 279 (20) Sequence Number: - Start / End Page: 21349 - 21355 Identifier: ISSN: 0021-9258
CoNE: https://pure.mpg.de/cone/journals/resource/954925410826_1