Characterization of the recombinant Clostridium pasteurianum ferredoxin and comparison of its properties with those of the native protein.
Ferredoxins (Fds) constitute an important class of nonheme iron-sulfur proteins. One of the most studied Fds is the [8Fe-8S] Fd from Clostridium pasteurianum. The gene for this Fd has previously been cloned and sequenced. We report the expression of this Fd in Escherichia coli, and the characterization and comparison of this recombinant protein to the native Fd. We have found that the purified recombinant protein has the same enzymatic, redox, magnetic and electronic properties as the native Fd isolated from C. pasteurianum, which indicates that the two [4Fe-4S] clusters present in the Fd were correctly formed in E. coli.
Department of Chemistry, University of Wisconsin-Milwaukee.
J R
JR
Baur
M C
MC
Graves
B A
BA
Feinberg
S W
SW
Ragsdale
D001426:Bacterial Proteins / Q000235:genetics / Q000378:metabolism*; D001483:Base Sequence; D003013:Clostridium / Q000032:analysis* / Q000235:genetics; D004579:Electron Transport; D004926:Escherichia coli / Q000235:genetics; D005288:Ferredoxins / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D010084:Oxidation-Reduction; D011994:Recombinant Proteins / Q000378:metabolism*
D001426:Bacterial Proteins; D005288:Ferredoxins; D011994:Recombinant Proteins