Rubredoxin: Difference between revisions

The protein mechanism of rubredoxin is carried out by a reversible Fe3+/Fe2+ redox coupling by the reduction of Fe3+ to Fe2+ and a gating mechanism caused by the conformational changes of Leucine 41. Leucine 41 is a nonpolar side chain that allows transient penetration of water molecules. This increases the polarity of the redox site environment and also provides protons. During this, the four iron-sulfur bond lengths increase while amide NH hydrogen bonding to the S(Cys) shortens in length. The presence of hydrogen bonds between neighboring amino acid backbones and sulfur atoms of the FeS4 unit has given a possible explanation for the low rupture force of the iron-sulfur bonds in rubredoxin by decreasing the covalent character of the iron-sulfur bonds.