Cytochrome bc1 and cytochrome oxidase can bind to the same surface domain of the cytochrome c molecule

Rieder, Rainer; Bosshard, Hans Rudolf

doi:10.1016/0014-5793(78)80759-5

Cited by 52 publications

(14 citation statements)

References 17 publications

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“…Indeed, one may ask what features of this mechanism are common to the smaller and larger cytochromes c of classes S and L. It may be, in light of the fact that no conformational change has been observed in molecules of these classes, that they function by a different mechanism (10). SUMMARY By using a three-point superposition of the oxidized and reduced forms of cytochrome c, motivated by chemical evidence (5)(6)(7) and by the observed (9) fit between the cytochrome c and cytochrome c peroxidase crystal structures, we have shown that the observed structure changes in cytochrome c upon oxidation correspond in detail to the binding mode for redox suggested by both chemical modification studies and the graphical docking experiments. We suggest that the observed large motion of lysine-27 upon oxidation leads to a change in binding affinity, which provides a dissociation signal to the cytochrome c-redox partner complex.…”

Section: Resultsmentioning

confidence: 99%

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On the redox conformational change in cytochrome c.

Rackovsky¹,

Goldstein²

1984

Proc. Natl. Acad. Sci. U.S.A.

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The relationship between the crystal structures of oxidized and reduced tuna cytochrome c has been reexamiined by a superposition method motivated by recent studies of the cytochrome c-cytochrome c peroxidase complex. It is shown that the observed structural changes precisely reflect the binding face suggested by chemical modification studies. It is further suggested that the large observed motion of Iysine-27 and a smaller overall motion of the two binding edges constitute a redox binding-affinity switch and that the driving force for the conformational change of the protein is provided by the internal conformational change and charge redistribution of the heme, which cause it to tilt, under the influence of covalent and nonbonded interactions, within its protein envelope. A picture is presented of the molecule as an electron storage/ transfer machine with three elements-a binding module, an electron storage module, and a conformational energy-storage module.The architecture of cytochrome c and the relationship of that structure to the molecule's role as an electron-transfer pro' tein have been a concern of molecular biologists for some time. The occurrence of variants of the molecule in the most diverse species has made it the classic subject for studies of molecular evolution. The fact that many of the cytochromes c can be crystallized has made it possible to consider this problem not only from the viewpoint of sequence homology but also to relate the observed features of sequence variation to the structure of the molecule.A problem of central interest is the comparison of the structures of the oxidized and reduced forms of the molecule and the unraveling of the relationship between any observed changes and the function of the molecule. In a classic series of papers (1-3), Dickerson and collaborators have elucidated the structures of the oxidized and reduced forms of tuna cytochrome c, and have compared the two forms by a superposition method. In these studies, in which superposition of all corresponding atoms of the protein (excluding the heme) was optimized, significant conformational changes were observed in the "bottom half' of the molecule, particularly in the region of residues 47-57. It was suggested that these changes, together with motions of the heme, constitute a mechanism for regulating the redox potential of the molecule. Recent calculations (4) also indicate that the protein environment lowers the apparent activation energy for electron transfer by the heme.Still another question which has been investigated extensively is the mode of binding of cytochrome c to its redox partners. Modification studies (5-7) have strongly supported the suggestion that a ring of lysine residues is responsible for proper binding of cytochrome c and that this binding occurs by an electrostatic mechanism. The lysines believed to be responsible are at positions 8, 13, 27, 72, 79, 86, and 87. Until recently, however, no crystallographic evidence was available for this hypothesis. Now, however, the structure of c...

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Section: Resultsmentioning

confidence: 99%

“…[4] Since the position of T is fixed, we can determine that of t by determining the vector r1 and the angle 4 between R12 and the x-axis. It is readily found that r2 = X12 + A2, r2 = (x+1 + COS -x2)2 + (9 + 12 sin )2, [5] r2= [ …”

Section: Appendix: Three-point Superpositionmentioning

confidence: 99%

On the redox conformational change in cytochrome c.

Rackovsky¹,

Goldstein²

1984

Proc. Natl. Acad. Sci. U.S.A.

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“…They form reversible associations with their reductases and oxidases, that are mediated by complementary charge interactions [2,3]. Separation of cytochrome c oxidase by affinity chromatography on a cytochrome c column has been attempted [4] although the technique proved to be effective only with the Neurospora enzyme [5].…”

Section: Introductionmentioning

confidence: 99%

“…The inability of a Sepharose 4B-cytochrome c column to easily and reproducibly separate cytochrome c oxidase may be due to the fact that the lysine residues, through which cytochrome c crosslinks to CNBractivated Sepharose 4B, are most probably the residues which are necessary for the cytochrome c oxidase and reductase binding [2,3,6].…”

Section: Introductionmentioning

confidence: 99%

Affinity chromatography purification of cytochrome c oxidase

et al. 1980

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“…It is not required for electron transfer [3], but it was reported to be indispensable for the formation of a complex between cytochrome c1 and cytochrome c [4,5]. In an active complex between these two cytochromes some amino acid sequences will realise a preferential contact.…”

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confidence: 99%

Interaction Between Isolated Cytochrome c1 and Cytochrome c

1983

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Cytochrome c1 from bovine heart mitochondria was isolated by a modification of the technique of König et al. [(1980) Biochim. Biophys. Acta 621, 283–295] which involved an affinity chromatography step on a gel with yeast cytochrome c as a ligand. Its spectra, electrophoretic pattern in presence of sodium dodecylsulfate, its reducibilty by ascorbate and cytochrome c were characteristic of a native cytochrome, with a single polypeptide having an apparent molecular weight of 30000. By using an arylazido derivative of cytochrome c, having the photoactive group bound to lysine 13, upon illumination a cross‐link with the described preparation of cytochrome c1 was obtained. By pepsin degestion of the cross‐linked complex a limiting fragment was obtained and partially sequenced. It allowed to identify the site of binding of cytochrome c near the sequence 167–174 of cytochrome c1.

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Cytochrome bc₁ and cytochrome oxidase can bind to the same surface domain of the cytochrome c molecule

Cited by 52 publications

References 17 publications

On the redox conformational change in cytochrome c.

On the redox conformational change in cytochrome c.

Affinity chromatography purification of cytochrome c oxidase

Interaction Between Isolated Cytochrome c1 and Cytochrome c

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