Abstract:
:The aldehyde oxidoreductase from Desulfovibrio gigas belongs to the family of molybdenum hydroxylases. Besides a molybdenum cofactor which constitutes their active site, these enzymes contain two [2Fe-2S](2+,1+) clusters which are believed to transfer the electrons provided by the substrate to an acceptor which is either a FAD group or an electron-transferring protein. When the three metal centers of D. gigas AOR are simultaneously paramagnetic, splittings due to intercenter spin-spin interactions are visible when the EPR spectra are recorded at low temperatures. By studying quantitatively these interactions with a model based on the X-ray crystal structure, which takes into consideration the interactions between the magnetic moments carried by all the metal sites of the system, it is possible to determine the location of the reducible sites of the [2Fe-2S] clusters. When combined with the electron-transfer pathways proposed on the basis of the X-ray crystal structure, the results provide a detailed description of the electron-transfer system of D. gigas AOR.
journal_name
Biochemistryjournal_title
Biochemistryauthors
More C,Asso M,Roger G,Guigliarelli B,Caldeira J,Moura J,Bertrand Pdoi
10.1021/bi0510025subject
Has Abstractpub_date
2005-08-30 00:00:00pages
11628-35issue
34eissn
0006-2960issn
1520-4995journal_volume
44pub_type
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