The cytochrome c oxidase binding site on cytochrome c. Differential chemical modification of lysine residues in free and oxidase-bound cytochrome c.

Rieder, Rainer; Bosshard, Hans Rudolf

doi:10.1016/s0021-9258(17)34577-5

Cited by 105 publications

(15 citation statements)

References 33 publications

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“…Site-directed mutagenesis studies have also been utilized for elucidating the cyt c −CcP binding interaction, , and it has recently been shown that this interaction can be modulated by groups which do not interact directly and may lie outside the interface defined by crystallographic studies . The CcO recognition site of cyt c is also suggested to be mostly the exposed heme edge by chemical modification − and comparative kinetic studies of various cyt c …”

Section: Introductionmentioning

confidence: 99%

“…12 Site-directed mutagenesis studies have also been utilized for elucidating the cyt c-CcP binding interaction, 13,14 and it has recently been shown that this interaction can be modulated by groups which do not interact directly and may lie outside the interface defined by crystallographic studies. 15 The CcO recognition site of cyt c is also suggested to be mostly the exposed heme edge by chemical modification [16][17][18] and comparative kinetic studies of various cyt c. 19 The cytochrome b 6 f complex is an integral oligomeric membrane protein complex existing in the photosynthetic organism. Cyt f receives electrons from the Rieske iron-sulfur protein of the cytochrome b 6 f complex and donates electrons to the soluble blue copper protein, plastocyanin (PC).…”

Section: Introductionmentioning

confidence: 99%

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Interactions of Cytochrome c and Cytochrome f with Aspartic Acid Peptides

et al. 1999

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Cytochrome c (cyt c) and cytochrome f (cyt f) molecular recognition characters and their structural changes due to complex formation with negatively charged aspartic acid peptides (Aspptd's) have been studied. Changes in the absorption spectrum of cyt c in the Soret region were detected when Aspptd's, up to penta-Asp, were added to the cyt c solution. These changes were the same as those observed when cyt c interacted with plastocyanin (PC), indicating that Aspptd's interacted with cyt c in the same way as PC. Conformational changes of cyt c due to interaction with Aspptd's observed by resonance Raman spectroscopy were similar to those reported for cyt c when bound with its native partner, cytochrome c oxidase. Electrochemical measurements showed that the redox potential of cyt c and cyt f shifted to lower potentials by 7−20 mV upon Aspptd binding, showing the enhancement in the electron donor ability of both cyt c and cyt f upon complex formation with Aspptd. The changes in the absorption spectrum and redox potential increased with the length and concentration of Aspptd. The observed structural and redox changes of cyt c and cyt f are attributed to adduct formations with Aspptd's by electrostatic interactions and suggest that similar changes would occur for cyt c and cyt f when interacting with proteins. Aspptd's, tetra- and penta-aspartic acid, served as competitive inhibitors of the electron transfer from cyt c or cyt f to PC, which was ascribable to the same adduct formation.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Interactions of Cytochrome c and Cytochrome f with Aspartic Acid Peptides

et al. 1999

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“…Several attempts have been made to deter- mine the number and location of the cytochrome c binding sites on the enzyme. Analytical gel filtration experiments have typically given a stoichiometry of two binding sites per oxidase monomer (Rieder & Bosshard, 1978;Taha & Ferguson-Miller, 1992). Direct binding studies have demonstrated interaction between cytochrome c and the highaffinity binding site with a Ko less than 100 nM (Ferguson-Miller et al, 1976).…”

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confidence: 99%

Electron Transfer between Cytochrome c and the Isolated CuA Domain: Identification of Substrate-Binding Residues in Cytochrome c Oxidase

Lappalainen

Watmough²,

Greenwood³

et al. 1995

Biochemistry

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Subunit II of cytochrome c oxidase has a C-terminal domain that is exposed to aqueous solution on membrane surface and contains a copper center called CuA. The central part of the cytochrome c binding site is thought to reside in this domain. We have expressed the subunit II fragment of the Paracoccus denitrificans cytochrome c oxidase in a soluble form and studied its interaction with cytochrome c by stopped-flow spectroscopy. The oxidation of cytochrome c by the CuA domain follows monophasic kinetics, indicating the presence of a single kinetically competent binding site. In low ionic strength medium, the domain oxidizes Paracoccus cytochrome c-550 and horse mitochondrial cytochrome c at the rates of 1.5 x 10(6) and 3 x 10(5) M-1 s-1, respectively. The reaction rates are strongly dependent on ionic strength, which must reflect electrostatic interactions within the complex. The KD for the complex between the bacterial cytochrome c and the domain is 1.6 microM; i.e., it is similar to that between the mitochondrial cytochrome c and the intact oxidase, suggesting that both contain the same catalytically competent binding site. Using site-directed mutagenesis, we have identified five conserved residues of the CuA domain that are involved in the cytochrome c binding. Mutations of glutamine 148, glutamate 154, aspartate 206, aspartate 221, or glutamate 246 lead to a 35-85% decrease in the rate of cytochrome c oxidation. The simultaneous substitution of three invariant carboxylic acids (aspartate 206, aspartate 221, and glutamate 246) leads to a 95% decrease in the reaction rate. Conversely, the reaction can be enhanced by removing a positive charge (lysine 219) from the CuA domain.

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“…One of these acidic residues, Glu-198, lies between two cysteine residues which probably serve as ligands of CuA (Ferguson-Miller et al, 1978;Millett et al, 1983;Rieder & Bosshard, 1978;Smith et al, 1977) placing the heme of cytochrome c in proximity to CuA, the first acceptor of electrons from cytochrome c (Hill, 1991). Isoform-1 of yeast cytochrome c contains a cysteine at residue 107 which is exposed on the surface of the molecule opposite the side which binds to cytochrome oxidase subunit II, and Cys-115 of subunit III can be cross-linked to Cys-107 of yeast cytochrome c via a disulfide bond when it is bound at the high affinity site (Birchmeier et al, 1976;Fuller et al, 1981; Darley-Usmar et al, 1984).…”

Section: Discussionmentioning

confidence: 99%

Electron Microscopy of Cytochrome c Oxidase Crystals: Labeling of Subunit III with a Monomaleimide Undecagold Cluster Compound

Crum

Gruys²,

Frey³

1994

Biochemistry

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Two-dimensional crystals of beef heart mitochondrial cytochrome c oxidase dimers were labeled at Cys-115 of subunit III with a monomaleimide derivative of an undecagold cluster compound. The binding site of the gold cluster compound and hence the site of subunit III were identified by image processing of cryoelectron micrographs of the crystals preserved in a mixture of glucose and uranyl acetate. The shape of the cytochrome oxidase dimer can be approximated as a parallelogram which is 44 by 82 A with an included angle of 80 degrees oriented with its long dimension along the a axis of the crystal. Labeling of subunit III was confirmed by a shift in the mobility of approximately 50% of subunit III molecules upon electrophoresis in polyacrylamide gels in the presence of sodium dodecyl sulfate. Averaged images of undecagold cluster labeled crystals and of unlabeled crystals were calculated; each image represents an average of approximately 17,000 molecules of either labeled or unlabeled cytochrome oxidase. On the basis of a statistical analysis of the differences between the two images, the gold cluster binds along a line 30 degrees from the a axis and 29 A from the center of the dimer. This result is interpreted in the context of other structural studies including the site of cytochrome c binding which Frey and Murray found to be near the a axis and 18 A from the center of the dimer [Frey, T. G., & Murray, J. M. (1994) J. Mol. Biol. 237, 275-297].(ABSTRACT TRUNCATED AT 250 WORDS)

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The cytochrome c oxidase binding site on cytochrome c. Differential chemical modification of lysine residues in free and oxidase-bound cytochrome c.

Cited by 105 publications

References 33 publications

Interactions of Cytochrome c and Cytochrome f with Aspartic Acid Peptides

Interactions of Cytochrome c and Cytochrome f with Aspartic Acid Peptides

Electron Transfer between Cytochrome c and the Isolated CuA Domain: Identification of Substrate-Binding Residues in Cytochrome c Oxidase

Electron Microscopy of Cytochrome c Oxidase Crystals: Labeling of Subunit III with a Monomaleimide Undecagold Cluster Compound

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