| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1942203 | Biochimica et Biophysica Acta (BBA) - Bioenergetics | 2013 | 17 Pages |
Abstract
⺠Crystal structures of cyt bc1 complexes have been determined from diverse organisms. ⺠ISP-ED, the extrinsic domain of iron-sulfur protein, undergoes binary conformational changes upon binding of different inhibitors. ⺠ISP-ED conformation is controlled through modulating its binding affinity to cyt b subunit. ⺠Bifurcated ET can be explained by the “surface-affinity modulated ISP motion switch hypothesis”. ⺠This mechanism has received substantial experimental support.
Keywords
QH2rms deviationbc1UbiquinolISPNCSISCPDBubiquinoneMPPelectron transferroot-mean-square deviationnon-crystallographic symmetryiron–sulfur clusterCrystal structureCytochrome bc1 complextransmembranephosphatidylinositolphosphatidylcholinephosphatidylethanolamineContact areasurface complementaritymitochondrial processing peptidaseIron–sulfur proteinProtein Data BankCardiolipin
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Authors
Di Xia, Lothar Esser, Wai-Kwan Tang, Fei Zhou, Yihui Zhou, Linda Yu, Chang-An Yu,