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A more recent version of this article appeared on November 30, 2001
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Papers In Press, published online ahead of print September 18, 2001
J. Biol. Chem, 10.1074/jbc.M107436200
Submitted on August 3, 2001
Revised on September 10, 2001
Accepted on September 17, 2001

Evidence for the intertwined dimer of the cytochrome bc1 complex in solution

Kunhong Xiao, Ananda Chandrasekaran, Linda Yu, and Chang-An Yu

Dept. of Biochemistry and Molecular Biology, Oklahoma State University, Stillwater, OK 74078

Corresponding Author: cayuq{at}okway.okstate.edu

To confirm that the cytochrome bc1 complex exists as a dimer with intertwining Rieske iron sulfur proteins in solution, four Rhodobacter sphaeroides mutants expressing His-tagged cytochrome bc1 complexes containing two pairs of cysteine substitutions, one in the interface between the head domain of iron-sulfur protein (ISP) and cytochrome b and the other between the tail domain of ISP and cytochrome b, were generated and characterized. They are: K70C(ISP)/A185C(cytb)//P33C(ISP)/G89C(cytb), K70C(ISP)/A185C(cytb)//P33C(ISP)/M92C (cytb), K70C(ISP)/A185C(cytb)//L34C(ISP)/V64C(cytb), and K70C(ISP)/A185C(cytb)//N36C(ISP)/G89C(cytb). The K70C(ISP)/A185C(cytb) cysteine pair cross-links the head domain of ISP and cytochrome b; the P33C(ISP)/G89C(cytb), P33C(ISP)/M92C (cytb), L34C(ISP)/V64C(cytb), and N36C(ISP)/ G89C(cytb) cysteine pairs cross-link the tail domain of ISP and cytochrome b. An adduct protein with an apparent molecular mass of 128 kDa containing two cytochrome b and two ISP proteins is detected in the K70C(ISP)/A185C(cytb)//P33C(ISP)/G89C(cytb) and K70C(ISP)/A185C(cytb) //N36C(ISP)/G89C(cytb) mutant complexes, confirming that the bc1 complex exists as a dimer with intertwining ISPs. The loss of activity in these two double-cysteine-pair mutant complexes was attributed to the disulfide bond between the head domain of ISP and cytochrome b, and not the one between the tail domain of ISP and cytochrome b.


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