|Title||Breaking and re-forming the disulfide bond at the high-potential, respiratory-type Rieske [2Fe-2S] center of thermus thermophilus: characterization of the sulfhydryl state by protein-film voltammetry.|
|Publication Type||Journal Article|
|Year of Publication||2002|
|Authors||Zu, Y, Fee, JA, Hirst, J|
|Date Published||2002 Nov 26|
|Keywords||Bacterial Proteins, Electrochemistry, Electron Transport Complex III, Iron-Sulfur Proteins, Models, Molecular, Oxidation-Reduction, Protein Conformation, Sulfhydryl Compounds, Thermus thermophilus|
A disulfide bond, adjacent to the [2Fe-2S] cluster, is conserved in all high-potential Rieske proteins from the respiratory and photosynthetic cytochrome bc(1) and b(6)f complexes but is absent from the low-potential, bacterial dioxygenase Rieske proteins. The role of the disulfide is unclear, since cysteine mutants have resulted in only apoprotein. The high stability of the soluble Thermus thermophilus Rieske protein permits chemical reduction of the disulfide bond and characterization of the sulfhydryl (dithiol) form by protein-film voltammetry. The effect of disulfide reduction on the cluster potential is small (DeltaE(0)'
|Grant List||GM35342 / GM / NIGMS NIH HHS / United States|