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.

TitleBreaking 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 TypeJournal Article
Year of Publication2002
AuthorsZu, Y, Fee, JA, Hirst, J
JournalBiochemistry
Volume41
Issue47
Pagination14054-65
Date Published2002 Nov 26
ISSN0006-2960
KeywordsBacterial Proteins, Electrochemistry, Electron Transport Complex III, Iron-Sulfur Proteins, Models, Molecular, Oxidation-Reduction, Protein Conformation, Sulfhydryl Compounds, Thermus thermophilus
Abstract

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)'

DOI10.1021/bi026589r
Alternate JournalBiochemistry
Citation Key10.1021/bi026589r
PubMed ID12437363
Grant ListGM35342 / GM / NIGMS NIH HHS / United States