The crystal structure of the three-iron ferredoxin II from Desulfovibrio gigas

AbstractThe crystal structure of oxidized ferredoxin II from the sulfate-reducing bacterium Desulfovibrio gigas has been determined and refined at 1.7 Å resolution. The folding of the polypeptide chain is similar to that of the 2[4Fe-4S] ferredoxin in Peptococcus aerogenes, except for an extended helical segment near the C-terminus. The single [3Fe-4S] cluster in D. gigas is similar to a [4Fe-4S] cluster, but lacks one Fe atom and is coordinated to Cys-8, -14 and -50. The side chain of Cys-11 is not bound to the cluster, but is rotated toward the solvent and modified by some, as yet undetermined, chemical group. Cys-18 and Cys-42 form a disulfide bridge. A previously undetected extra amino acid is found after residue 55

The assignment of the 1H nuclear magnetic resonance spectrum of azurin: an investigation of the 1H NMR spectrum of the blue copper protein, azurin, from Pseudomonas aeruginosa, with reference to the previously determined crystal structure

Macromolecular Biochemistr

The redox properties of azurin from pseudomonas aeruginosa as studied by high frequency proton NMR

Macromolecular Biochemistr

A proton NMR study of the electron exchange between reduced and oxidized azurin from Pseudomonas aeruginosa

Macromolecular Biochemistr