Primary structure of desulfoferrodoxin from Desulfovibrio desulfuricans ATCC 27774, a new class of non-heme iron proteins.
The primary structure of desulfoferrodoxin from Desulfovibrio desulfuricans ATCC 27774, a redox protein with two mononuclear iron sites, was determined by automatic Edman degradation and mass spectrometry of the composing peptides. It contains 125 amino acid residues of which five are cysteines. The first four, Cys-9, Cys-12, Cys-28 and Cys-29, are responsible for the binding of Center I which has a distorted tetrahedral sulfur coordination similar to that found in desulforedoxin from D. gigas. The remaining Cys-115 is proposed to be involved in the coordination of Center II, which is probably octahedrally coordinated with predominantly nitrogen/oxygen containing ligands as previously suggested by Mössbauer and Raman spectroscopy.
Devreese
B
B
Vakgroep Biochemie Fysiologie en Microbiologie, Universiteit Gent, Belguim.
Tavares
P
P
Lampreia
J
J
Van Damme
N
N
Le Gall
J
J
Moura
J J
JJ
Van Beeumen
J
J
Moura
I
I
D000595:Amino Acid Sequence; D001665:Binding Sites; D017124:Conserved Sequence; D003901:Desulfovibrio / Q000737:chemistry*; D019143:Evolution, Molecular; D005288:Ferredoxins / Q000737:chemistry*; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry; D016415:Sequence Alignment; D017421:Sequence Analysis; D012697:Serine Endopeptidases / Q000378:metabolism; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
D005288:Ferredoxins; D010455:Peptides; C066602:desulfoferrodoxin; D012697:Serine Endopeptidases; C028344:glutamyl endopeptidase