Binding site on Rhodospirillum rubrum cytochrome c2 for the Rhodospirillum rubrum cytochrome be bc1 complex

Hans Rudolf Bosshard, R. Max Wynn, David B. Knaff

Research output: Contribution to journalArticle

19 Citations (Scopus)

Abstract

Cytochrome c2 and the detergent-solubilized cytochrome bc1 complex, both from Rhodospirillum rubrum, form a tight complex at a low ionic strength that can be isolated by gel permeation chromatography. The dissociation constant of the complex is estimated to be 10-6 M or less. The binding site for the cytochrome bc1 complex on cytochrome c2 was analyzed by differential acetylation of lysine residues in free and cytochrome bc1 complex bound cytochrome c2. In bound cytochrome c2, three lysine residues at sequence positions 12, 13, and 97 were less reactive toward acetic anhydride. Lys13, which is located above the exposed heme edge, was the least reactive, i.e., the most shielded by the cytochrome bc1 complex. Correlating this information with the crystal structure of cytochrome c2 indicates that the binding site for the cytochrome bc1 complex on cytochrome c2 involves a surface area above, and probably including, the exposed heme edge. This mode of binding is similar to that observed for horse cytochrome c interacting with the mitochondrial cytochrome bc1 complex. A simplified version of the method of differential chemical modification is presented.

Original languageEnglish (US)
Pages (from-to)7688-7693
Number of pages6
JournalBiochemistry
Volume26
Issue number24
StatePublished - 1987

Fingerprint

Cytochromes c2
Rhodospirillum rubrum
Electron Transport Complex III
Cytochromes
Binding Sites
Heme
Lysine
Acetylation
Chemical modification
Gel permeation chromatography
Cytochromes c
Ionic strength
Detergents
Osmolar Concentration
Horses
Gel Chromatography
Crystal structure

ASJC Scopus subject areas

  • Biochemistry

Cite this

Binding site on Rhodospirillum rubrum cytochrome c2 for the Rhodospirillum rubrum cytochrome be bc1 complex. / Bosshard, Hans Rudolf; Wynn, R. Max; Knaff, David B.

In: Biochemistry, Vol. 26, No. 24, 1987, p. 7688-7693.

Research output: Contribution to journalArticle

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N2 - Cytochrome c2 and the detergent-solubilized cytochrome bc1 complex, both from Rhodospirillum rubrum, form a tight complex at a low ionic strength that can be isolated by gel permeation chromatography. The dissociation constant of the complex is estimated to be 10-6 M or less. The binding site for the cytochrome bc1 complex on cytochrome c2 was analyzed by differential acetylation of lysine residues in free and cytochrome bc1 complex bound cytochrome c2. In bound cytochrome c2, three lysine residues at sequence positions 12, 13, and 97 were less reactive toward acetic anhydride. Lys13, which is located above the exposed heme edge, was the least reactive, i.e., the most shielded by the cytochrome bc1 complex. Correlating this information with the crystal structure of cytochrome c2 indicates that the binding site for the cytochrome bc1 complex on cytochrome c2 involves a surface area above, and probably including, the exposed heme edge. This mode of binding is similar to that observed for horse cytochrome c interacting with the mitochondrial cytochrome bc1 complex. A simplified version of the method of differential chemical modification is presented.

AB - Cytochrome c2 and the detergent-solubilized cytochrome bc1 complex, both from Rhodospirillum rubrum, form a tight complex at a low ionic strength that can be isolated by gel permeation chromatography. The dissociation constant of the complex is estimated to be 10-6 M or less. The binding site for the cytochrome bc1 complex on cytochrome c2 was analyzed by differential acetylation of lysine residues in free and cytochrome bc1 complex bound cytochrome c2. In bound cytochrome c2, three lysine residues at sequence positions 12, 13, and 97 were less reactive toward acetic anhydride. Lys13, which is located above the exposed heme edge, was the least reactive, i.e., the most shielded by the cytochrome bc1 complex. Correlating this information with the crystal structure of cytochrome c2 indicates that the binding site for the cytochrome bc1 complex on cytochrome c2 involves a surface area above, and probably including, the exposed heme edge. This mode of binding is similar to that observed for horse cytochrome c interacting with the mitochondrial cytochrome bc1 complex. A simplified version of the method of differential chemical modification is presented.

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