AbstractThe amino acid sequence of a rubredoxin from Desulfovibrio desulfuricans (strain 27774) has been determined. Comparison with rubredoxins from other species reveals pervasive homology, including the regions known to provide the cysteine ligands to the iron atom in several rubredoxins. Neither an extra cysteinyl residue nor a unique histidyl residue in the new sequence is located in the sequence in such a way that, by homology, a functional role in the structure is suggested
The atomic environment around the iron site in the nonheme iron sulfur protein rubredoxin was studie...
The energetic contributions of the protein to the redox potential in an iron-sulfur protein are stud...
Although neglected for a long time, non-heme iron proteins are now acknowledge to participate on imp...
AbstractThe amino acid sequence of a rubredoxin from Desulfovibrio desulfuricans (strain 27774) has ...
AbstractThe X-ray crystallographic structure of rubredoxin from Desulfovibrio desulfuricans strain 2...
AbstractA new rubredoxin from the sulphate-reducing bacterium Desulfovibrio desulfuricans ATCC 27774...
AbstractThe primary structure of desulfoferrodoxin from Desulfovibrio desulfuricans ATCC 27774, a re...
AbstractDesulfoferrodoxin from Desulfovibrio vulgaris, strain Hildenborough, is a homodimer of 28 kD...
A two cluster (4Fe4S) ferredoxin and a rubredoxin have been isolated from the sulfur-reducing bacter...
AbstractA rubredoxin and a flavodoxin have been purified and characterized from soluble extracts of ...
Sequence alignment studies and biochemical investigations have suggested that the two iron rubredoxi...
Abstract: Rubredoxin-oxygen oxidoreductase (ROO) is the final component of a soluble electron transf...
Despite their high sequence homology, rubredoxins from Desulfovibrio gigas and D. desulfuricans are ...
Complete ami no acid sequences of ferredoxin and rubredoxin from Butyribacterium methylotrophicum, a...
Rubredoxin-oxygen oxidoreductase, an 86-kDa homodimeric flavoprotein, is the final component of a so...
The atomic environment around the iron site in the nonheme iron sulfur protein rubredoxin was studie...
The energetic contributions of the protein to the redox potential in an iron-sulfur protein are stud...
Although neglected for a long time, non-heme iron proteins are now acknowledge to participate on imp...
AbstractThe amino acid sequence of a rubredoxin from Desulfovibrio desulfuricans (strain 27774) has ...
AbstractThe X-ray crystallographic structure of rubredoxin from Desulfovibrio desulfuricans strain 2...
AbstractA new rubredoxin from the sulphate-reducing bacterium Desulfovibrio desulfuricans ATCC 27774...
AbstractThe primary structure of desulfoferrodoxin from Desulfovibrio desulfuricans ATCC 27774, a re...
AbstractDesulfoferrodoxin from Desulfovibrio vulgaris, strain Hildenborough, is a homodimer of 28 kD...
A two cluster (4Fe4S) ferredoxin and a rubredoxin have been isolated from the sulfur-reducing bacter...
AbstractA rubredoxin and a flavodoxin have been purified and characterized from soluble extracts of ...
Sequence alignment studies and biochemical investigations have suggested that the two iron rubredoxi...
Abstract: Rubredoxin-oxygen oxidoreductase (ROO) is the final component of a soluble electron transf...
Despite their high sequence homology, rubredoxins from Desulfovibrio gigas and D. desulfuricans are ...
Complete ami no acid sequences of ferredoxin and rubredoxin from Butyribacterium methylotrophicum, a...
Rubredoxin-oxygen oxidoreductase, an 86-kDa homodimeric flavoprotein, is the final component of a so...
The atomic environment around the iron site in the nonheme iron sulfur protein rubredoxin was studie...
The energetic contributions of the protein to the redox potential in an iron-sulfur protein are stud...
Although neglected for a long time, non-heme iron proteins are now acknowledge to participate on imp...