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Primary structure of desulfoferrodoxin from Desulfovibrio desulfuricans ATCC 27774, a new class of non‐heme iron proteins
Author(s) -
Devreese Bart,
Tavares Pedro,
Lampreia Jorge,
Van Damme Nancy,
Le Gall Jean,
Moura JoséJ.G.,
Van Beeumen Jozef,
Moura Isabel
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00364-x
Subject(s) - chemistry , heme , edman degradation , protein primary structure , desulfovibrio , primary (astronomy) , raman spectroscopy , myoglobin , redox , metalloprotein , biochemistry , amino acid , stereochemistry , crystallography , peptide sequence , inorganic chemistry , enzyme , organic chemistry , physics , astronomy , sulfate , optics , gene
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.