Abstract:
:Iron-sulfur flavoproteins (ISF) constitute a widespread family of redox-active proteins in anaerobic prokaryotes. Based on sequence homologies, their overall structure is expected to be similar to that of flavodoxins, but in addition to a flavin mononucleotide cofactor they also contain a cubane-type [4Fe:4S] cluster. In order to gain further insight into the function and properties of ISF, the three-dimensional structures of two ISF homologs, one from the thermophilic methanogen Methanosarcina thermophila and one from the hyperthermophilic sulfate-reducing archaeon Archaeoglobus fulgidus, were determined. The structures indicate that ISF assembles to form a tetramer and that electron transfer between the two types of redox cofactors requires oligomerization to juxtapose the flavin mononucleotide and [4Fe:4S] cluster bound to different subunits. This is only possible between different monomers upon oligomerization. Fundamental differences in the surface properties of the two ISF homologs underscore the diversity encountered within this protein family.
journal_name
J Bacterioljournal_title
Journal of bacteriologyauthors
Andrade SL,Cruz F,Drennan CL,Ramakrishnan V,Rees DC,Ferry JG,Einsle Odoi
10.1128/JB.187.11.3848-3854.2005keywords:
subject
Has Abstractpub_date
2005-06-01 00:00:00pages
3848-54issue
11eissn
0021-9193issn
1098-5530pii
187/11/3848journal_volume
187pub_type
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