DSpace UNL

RUN >
Instituto de Tecnologia Química e Biológica (ITQB) >
ITQB R&D Units >
ITQB: Biological Chemistry >
ITQB: Metalloenzymes and Molecular Bioenergetics >
ITQB: MMB - Artigos em revista internacional com arbitragem científica >

Please use this identifier to cite or link to this item: http://hdl.handle.net/10362/3584

Title: Spectroscopic Studies and Characterization of a Novel Electron-Transfer Chain
Authors: Gomes, Claudio
Vicente, João
Wasserfallen, Alain
Teixeira, Miguel
Issue Date: 1999
Publisher: American Chemical Society
Abstract: A novel two-component enzyme system from Escherichia coli involving a flavorubredoxin (FlRd) and its reductase was studied in terms of spectroscopic, redox, and biochemical properties of its constituents. FlRd contains one FMN and one rubredoxin (Rd) center per monomer. To assess the role of the Rd domain, FlRd and a truncated form lacking the Rd domain (FlRd¢Rd), were characterized. FlRd contains 2.9 ( 0.5 iron atoms/subunit, whereas FlRd¢Rd contains 2.1 ( 0.6 iron atoms/subunit. While for FlRd one iron atom corresponds to the Rd center, the other two irons, also present in FlRd¢Rd, are most probably due to a di-iron site. Redox titrations of FlRd using EPR and visible spectroscopies allowed us to determine that the Rd site has a reduction potential of -140 ( 15 mV, whereas the FMN undergoes reduction via a red-semiquinone, at -140 ( 15 mV (Flox/Flsq) and -180 ( 15 mV (Flsq/Flred), at pH 7.6. The Rd site has the lowest potential ever reported for a Rd center, which may be correlated with specific amino acid substitutions close to both cysteine clusters. The gene adjacent to that encoding FlRd was found to code for an FAD-containing protein, (flavo)rubredoxin reductase (FlRd-reductase), which is capable of mediating electron transfer from NADH to DesulfoVibrio gigas Rd as well as to E. coli FlRd. Furthermore, electron donation was found to proceed through the Rd domain of FlRd as the Rd-truncated protein does not react with FlRd-reductase. In vitro, this pathway links NADH oxidation with dioxygen reduction. The possible function of this chain is discussed considering the presence of FlRd homologues in all known genomes of anaerobes and facultative aerobes.
URI: http://hdl.handle.net/10362/3584
Appears in Collections:ITQB: MMB - Artigos em revista internacional com arbitragem científica

Files in This Item:

File Description SizeFormat
Spectroscopic Studies and Characterization of a Novel.pdf182.9 kBAdobe PDFView/Open
Statistics
View Statistics
FacebookTwitterDeliciousLinkedInDiggGoogle BookmarksMySpaceOrkut
Formato BibTex mendeley Endnote Logotipo do DeGóis 

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

 

Universidade Nova de Lisboa  - Statistics  - Feedback
Estamos no RCAAP Governo Português separator Ministério da Educação e Ciência   Fundação para a Ciência e a Tecnologia

Financiado por:

POS_C UE