A further investigation of the cytochrome b
5–cytochrome c complex

Banci, Lucia; Bertini, Ivano; Felli, Isabella C.; Krippahl, Ludwig; Kubíček, Karel; Moura, José J. G.; Rosato, Antonio

doi:10.1007/s00775-003-0479-y

Cited by 17 publications

(26 citation statements)

References 69 publications

(143 reference statements)

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“…Somewhat different results were obtained for the complex of reduced rabbit Cb 5 with reduced yeast Cc (Banci et al, 2003). The chemical-shift perturbations are of similar size and also rather extensive, but cover a somewhat different surface area.…”

Section: Complexes Of Cytochrome B 5 With Cytochrome C and Myoglobinmentioning

confidence: 74%

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Transient complexes of redox proteins: structural and dynamic details from NMR studies

Prudêncio

Ubbink

2004

J of Molecular Recognition

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Redox proteins participate in many metabolic routes, in particular those related to energy conversion. Protein-protein complexes of redox proteins are characterized by a weak affinity and a short lifetime. Two-dimensional NMR spectroscopy has been applied to many redox protein complexes, providing a wealth of information about the process of complex formation, the nature of the interface and the dynamic properties of the complex. These studies have shown that some complexes are non-specific and exist as a dynamic ensemble of orientations while in other complexes the proteins assume a single orientation. The binding interface in these complexes consists of a small hydrophobic patch for specificity, surrounded by polar, uncharged residues that may enhance dissociation, and, in most complexes, a ring or patch of charged residues that enhances the association by electrostatic interactions. The entry and exit port of the electrons is located within the hydrophobic interaction site, ensuring rapid electron transfer from one redox centre to the next.

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Section: Complexes Of Cytochrome B 5 With Cytochrome C and Myoglobinmentioning

confidence: 74%

“…It is outside the scope of this review to discuss all the earlier work (see Banci et al, 2003;Shao et al, 2003 for an overview). We will focus on the recent two-dimensional NMR spectroscopy studies that have enabled a detailed mapping of the binding sites on both Cb 5 and Cc.…”

Section: Complexes Of Cytochrome B 5 With Cytochrome C and Myoglobinmentioning

confidence: 98%

Transient complexes of redox proteins: structural and dynamic details from NMR studies

Prudêncio

Ubbink

2004

J of Molecular Recognition

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“…It is to be noted that the interprotein interfaces of cyt b 5 in the Northrup and Salemme model are very similar. A chemical shift mapping study is also available on the interaction between 15 N-enriched reduced yeast iso-1-cyt c and ferrous rabbit cyt b 5 (52). The interprotein interface is close to, but different from, those experiencing the largest shifts in this work, presumably indicating a slightly different interface.…”

Section: Confirmation Of the Resonance Assignments For Horse Cyt Cmentioning

confidence: 82%

Characterization and Calculation of a Cytochrome c−Cytochrome b₅ Complex Using NMR Data

Deep

Zuiderweg

et al. 2005

Biochemistry

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To identify the binding site for bovine cytochrome b(5) (cyt b(5)) on horse cytochrome c (cyt c), cross-saturation transfer NMR experiments were performed with (2)H- and (15)N-enriched cyt c and unlabeled cyt b(5). In addition, chemical shift changes of the cyt c backbone amide and side chain methyl resonances were monitored as a function of cyt b(5) concentration. The chemical shift changes indicate that the complex is in fast exchange, and are consistent with a 1:1 stoichiometry. A K(a) of (4 +/- 3) x 10(5) M(-)(1) was obtained with a lower limit of 855 s(-)(1) for the dissociation rate of the complex. Mapping of the chemical shift variations and intensity changes upon cross-saturation NMR experiments in the complex reveals a single, contiguous interaction interface on cyt c. Using NMR data as constraints, a protein docking program was used to calculate two low-energy model complex clusters. Independent calculations of the effect of the cyt b(5) heme ring current-induced magnetic dipole on cyt c were used to discriminate between the different models. The interaction surface of horse cyt c in the current experimentally constrained model of the cyt c-cyt b(5) complex is similar but not identical to the interface predicted in yeast cyt c by Brownian dynamics and docking calculations. The occurrence of different amino acids at the protein-protein interface and the dissimilar assumptions employed in the calculations can largely account for the nonidentical interfaces.

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“…However, recent NMR studies revealed pronounced dynamics within the complex, suggesting the presence of multiple binding geometries [17], [56]. Depending on the source of Cb 5 and the experimental conditions, formation of binary Cb 5 -Cc and ternary Cb 5 -(Cc) 2 complexes has been reported [54]–[58].…”

Section: Resultsmentioning

confidence: 99%

Electron Transfer Interactome of Cytochrome c

Volkov

Nuland

2012

PLoS Comput Biol

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Lying at the heart of many vital cellular processes such as photosynthesis and respiration, biological electron transfer (ET) is mediated by transient interactions among proteins that recognize multiple binding partners. Accurate description of the ET complexes – necessary for a comprehensive understanding of the cellular signaling and metabolism – is compounded by their short lifetimes and pronounced binding promiscuity. Here, we used a computational approach relying solely on the steric properties of the individual proteins to predict the ET properties of protein complexes constituting the functional interactome of the eukaryotic cytochrome c (Cc). Cc is a small, soluble, highly-conserved electron carrier protein that coordinates the electron flow among different redox partners. In eukaryotes, Cc is a key component of the mitochondrial respiratory chain, where it shuttles electrons between its reductase and oxidase, and an essential electron donor or acceptor in a number of other redox systems. Starting from the structures of individual proteins, we performed extensive conformational sampling of the ET-competent binding geometries, which allowed mapping out functional epitopes in the Cc complexes, estimating the upper limit of the ET rate in a given system, assessing ET properties of different binding stoichiometries, and gauging the effect of domain mobility on the intermolecular ET. The resulting picture of the Cc interactome 1) reveals that most ET-competent binding geometries are located in electrostatically favorable regions, 2) indicates that the ET can take place from more than one protein-protein orientation, and 3) suggests that protein dynamics within redox complexes, and not the electron tunneling event itself, is the rate-limiting step in the intermolecular ET. Further, we show that the functional epitope size correlates with the extent of dynamics in the Cc complexes and thus can be used as a diagnostic tool for protein mobility.

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A further investigation of the cytochrome b 5–cytochrome c complex

Cited by 17 publications

References 69 publications

Transient complexes of redox proteins: structural and dynamic details from NMR studies

Transient complexes of redox proteins: structural and dynamic details from NMR studies

Characterization and Calculation of a Cytochrome c−Cytochrome b₅ Complex Using NMR Data

Electron Transfer Interactome of Cytochrome c

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A further investigation of the cytochrome b 5–cytochrome c complex

Cited by 17 publications

References 69 publications

Transient complexes of redox proteins: structural and dynamic details from NMR studies

Transient complexes of redox proteins: structural and dynamic details from NMR studies

Characterization and Calculation of a Cytochrome c−Cytochrome b5 Complex Using NMR Data

Electron Transfer Interactome of Cytochrome c

Contact Info

Product

Resources

About

Characterization and Calculation of a Cytochrome c−Cytochrome b₅ Complex Using NMR Data