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Title: Dioxygen reactivity of a biomimetic [4Fe-4S] compound exhibits [4Fe-4S] to [2Fe-2S] cluster conversion
Award ID(s):
1807845
PAR ID:
10313636
Author(s) / Creator(s):
; ; ;
Date Published:
Journal Name:
Journal of Inorganic Biochemistry
Volume:
228
Issue:
C
ISSN:
0162-0134
Format(s):
Medium: X
Sponsoring Org:
National Science Foundation
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  1. The nucleotide binding protein 35 (Nbp35)/cytosolic Fe‐S cluster deficient 1 (Cfd1)/alternative pyrimidine biosynthetic protein C (ApbC) protein homologs have been identified in all three domains of life. In eukaryotes, the Nbp35/Cfd1 heterocomplex is an essential Fe‐S cluster assembly scaffold required for the maturation of Fe‐S proteins in the cytosol and nucleus, whereas the bacterial ApbC is an Fe‐S cluster transfer protein only involved in the maturation of a specific target protein. Here, we show that the Nbp35/ApbC homolog MMP0704 purified from its native archaeal hostMethanococcus maripaludiscontains a [4Fe‐4S] cluster that can be transferred to a [4Fe‐4S] apoprotein. Deletion ofmmp0704fromM. maripaludisdoes not cause growth deficiency under our tested conditions. Our data indicate that Nbp35/ApbC is a nonessential [4Fe‐4S] cluster transfer protein in methanogenic archaea.

     
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  2. null (Ed.)