English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/190812
Share/Impact:
Statistics
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE
Exportar a otros formatos:

Title

Structural differences of oxidized iron-sulfur and nickel-iron cofactors in O2-tolerant and O2-sensitive hydrogenases studied by X-ray absorption spectroscopy

AuthorsSigfridsson, Kajsa G.V.; Leidel, Nils; Sanganas, Oliver; Chernev, Petko; Lenz, Oliver; Yoon, Ki-Seok; Nishihara, H.; Parkin, Alison; Armstrong, Fraser A.; Dementin, Sébastien; Rousset, Marc; López de Lacey, Antonio ; Haumann, Michael
KeywordsX-ray absorption spectroscopy
O2-tolerance
[NiFe]-hydrogenase
[NiFe] active site
FeS cluster
Issue DateFeb-2015
PublisherElsevier
CitationBiochimica et Biophysica Acta (BBA) - Bioenergetics 1847(2): 162-170 (2015)
AbstractThe class of [NiFe]-hydrogenases comprises oxygen-sensitive periplasmic (PH) and oxygen-tolerant membrane-bound (MBH) enzymes. For three PHs and four MBHs from six bacterial species, structural features of the nickel–iron active site of hydrogen turnover and of the iron–sulfur clusters functioning in electron transfer were determined using X-ray absorption spectroscopy (XAS). Fe-XAS indicated surplus oxidized iron and a lower number of ~ 2.7 Å Fe–Fe distances plus additional shorter and longer distances in the oxidized MBHs compared to the oxidized PHs. This supported a double-oxidized and modified proximal FeS cluster in all MBHs with an apparent trimer-plus-monomer arrangement of its four iron atoms, in agreement with crystal data showing a [4Fe3S] cluster instead of a [4Fe4S] cubane as in the PHs. Ni-XAS indicated coordination of the nickel by the thiol group sulfurs of four conserved cysteines and at least one iron–oxygen bond in both MBH and PH proteins. Structural differences of the oxidized inactive [NiFe] cofactor of MBHs in the Ni-B state compared to PHs in the Ni–A state included a ~ 0.05 Å longer Ni-O bond, a two times larger spread of the Ni–S bond lengths, and a ~ 0.1 Å shorter Ni–Fe distance. The modified proximal [4Fe3S] cluster, weaker binding of the Ni–Fe bridging oxygen species, and an altered localization of reduced oxygen species at the active site may each contribute to O2 tolerance.
Publisher version (URL)https://doi.org/10.1016/j.bbabio.2014.06.011
URIhttp://hdl.handle.net/10261/190812
DOIhttp://dx.doi.org/10.1016/j.bbabio.2014.06.011
ISSN0005-2728
Appears in Collections:(ICP) Artículos
Files in This Item:
File Description SizeFormat 
accesoRestringido.pdf15,38 kBAdobe PDFThumbnail
View/Open
Show full item record
Review this work
 


WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.