1993
DOI: 10.1021/bi00091a047
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Abstract: The structural changes in oxidized yeast iso-1-cytochrome c and fully oxidized bovine cytochrome c oxidase that are induced upon complex formation have been analyzed by resonance Raman spectroscopy. The main spectral changes could be ascribed to cytochrome c, which in the case of the wild-type protein are essentially the same as previously observed in the complex of horse heart cytochrome c and bovine cytochrome c oxidase [Hildebrandt et al. (1990) Biochemistry 29, 1661-1668]. These spectral changes are attrib… Show more

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Cited by 48 publications
(58 citation statements)
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References 63 publications
(106 reference statements)
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“…These surface features are likely to play a role in molecular recognition for specific protein-protein interactions in the course of copper exchange. An example for such recognition sites is a clustering of basic residues on cytochrome c that interacts electrostatically with negatively charged residues on cytochrome c oxidase or peroxidase (44,45). It is tempting to speculate that one of the charged faces of CopZ is required to interact with a copper donor, and the other one supports recognition of a copper acceptor, such as CopY.…”
Section: Discussionmentioning
confidence: 99%
“…Details of the experimental setup are described elsewhere. 11,15 The S/N ratio was improved by repetitive scanning so that the total accumulation time was between 30 and 70 s per data point. The single scan spectra of each experiment were carefully compared and only combined if no spectral differences were noted.…”
Section: Rr Measurementsmentioning
confidence: 99%
“…For beef heart aa 3 oxidase such a complex with its natural redox partner cytochrome c is readily formed in solutions of low ionic strength because the nature of the principal intermolecular interactions is electrostatic. 15,19 If such interactions also prevail for the redox couple from T. thermophilus, a solution of equimolar concentrations of Cyt-c 552 and ba 3 in 10 mM Tris-HCl should contain the 1 : 1 protein complex as well. Indeed, prior research showed that Cyt-c 552 is capable of binding to negatively charged surfaces similar to Cyt-c, despite the lack of a positively charged lysine-rich domain around the heme crevice that is a characteristic struc- Figure 8.…”
Section: Complex Between Ba 3 Oxidase and Cyt-c 552mentioning
confidence: 99%
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“…For example, structural variations were also observed during the complex formation of cyt c and its natural electron-transfer partner, cyt c oxidase. 23,24 A lowered environmental dielectric constant through the combination of peptide backbones has been suggested to modulate the electron-transfer rate between the two proteins. As is well known, organic solvents commonly have low dielectric constant (ε), for instance, εDMSO = 46.7, εDMF = 37.8, while εwater = 78.5.…”
Section: Resultsmentioning
confidence: 99%