Modifications of Protein Environment of the [2Fe-2S] Cluster of the bc(1) Complex: EFFECTS ON THE BIOPHYSICAL PROPERTIES OF THE RIESKE IRON-SULFUR PROTEIN AND ON THE KINETICS OF THE COMPLEX

The rate-determining step in the overall turnover of the bc(1) complex is electron transfer from ubiquinol to the Rieske iron-sulfur protein (ISP) at the Q(o)-site. Structures of the ISP from Rhodobacter sphaeroides show that serine 154 and tyrosine 156 form H-bonds to S-1 of the [2Fe-2S] cluster an...

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Hlavní autoři: Lhee, Sangmoon, Kolling, Derrick R. J., Nair, Satish K., Dikanov, Sergei A., Crofts, Antony R.
Médium: Artigo
Jazyk:Inglês
Vydáno: American Society for Biochemistry and Molecular Biology 2010
Témata:
Bioenergetics
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC2838342/
https://ncbi.nlm.nih.gov/pubmed/20023300
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1074/jbc.M109.043505
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