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Originally published In Press as doi:10.1074/jbc.M107436200 on September 18, 2001

J. Biol. Chem., Vol. 276, Issue 49, 46125-46131, December 7, 2001
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Evidence for the Intertwined Dimer of the Cytochrome bc1 Complex in Solution*

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

From the Department of Biochemistry and Molecular Biology, Oklahoma State University, Stillwater, Oklahoma 74078

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.

* This work was supported by Grant GM30721 from the National Institutes of Health and by the Agricultural Experiment Station (Project 1819), Oklahoma State University.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed: Dept. of Biochemistry and Molecular Biology, Oklahoma State University, Stillwater, OK 74078. Tel.: 405-744-6198; Fax: 405-744-7799; E-mail: cayuq@okstate.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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Copyright © 2001 by the American Society for Biochemistry and Molecular Biology.