The Interactions of Cyanobacterial Cytochromec6 and Cytochrome f, Characterized by NMR

Crowley, Peter B.; Díaz‐Quintana, Antonio; Molina-Heredia, Fernando P.; Nieto, Pedro M.; Sutter, M.; Haehnel, Wolfgang; Rosa, Miguel Á. De la; Ubbink, Marcellus

doi:10.1074/jbc.m203983200

Cited by 33 publications

(64 citation statements)

References 40 publications

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“…These residues are surrounding the heme crevice and constitute the interaction surface (Fig. 2c), which is very well-conserved among complexes involving c-type cytochromes [14,29,[46][47][48][49][50][51][52][53][54][55]. In addition, significant CSP are detected (Dd avg -P 0.05 ppm) for Lys7, Lys13, Val20, Ser47, Lys73, Val83, Lys88 and Ala92.…”

Section: The Heterologous Hcc-pcc 1 Complexmentioning

confidence: 99%

Respiratory complexes III and IV can each bind two molecules of cytochrome c at low ionic strength

et al. 2015

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a b s t r a c tThe transient interactions of respiratory cytochrome c with complexes III and IV is herein investigated by using heterologous proteins, namely human cytochrome c, the soluble domain of plant cytochrome c 1 and bovine cytochrome c oxidase. The binding molecular mechanisms of the resulting cross-complexes have been analyzed by Nuclear Magnetic Resonance and Isothermal Titration Calorimetry. Our data reveal that the two cytochrome c-involving adducts possess a 2:1 stoichiometry -that is, two cytochrome c molecules per adduct -at low ionic strength. We conclude that such extra binding sites at the surfaces of complexes III and IV can facilitate the turnover and sliding of cytochrome c molecules and, therefore, the electron transfer within respiratory supercomplexes.

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Section: The Heterologous Hcc-pcc 1 Complexmentioning

confidence: 99%

Respiratory complexes III and IV can each bind two molecules of cytochrome c at low ionic strength

et al. 2015

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“…) [12]. The chemical-shift perturbation map indicates that Nostoc Cc 6 binds to Nostoc and Phormidium Cf in a similar way.…”

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“…A fast-kinetics study using a Zn-Cc 6 derivative has been recently reported [11]. The only structural data correspond to cross-complexes between proteins from different sources [12,13]. Here, we report a study of the interaction between both cytochromes, isolated from the same organism, by chemical-shift perturbation mapping and docking approaches based on ambiguous interface restraints [14].…”

Section: Introductionmentioning

confidence: 99%

An NMR‐based docking model for the physiological transient complex between cytochrome f and cytochrome c₆

et al. 2005

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The physiological transient complex between cytochrome f (Cf) and cytochrome c 6 (Cc 6 ) from the cyanobacterium Nostoc sp. PCC 7119 has been analysed by NMR spectroscopy. The binding constant at low ionic strength is 8 ± 2 mM À1, and the binding site of Cc 6 for Cf is localized around its exposed haem edge. On the basis of the experimental data, the resulting docking simulations suggest that Cc 6 binds to Cf in a fashion that is analogous to that of plastocyanin but differs between prokaryotes and eukaryotes.

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“…Two-dimensional NMR is a useful technique to study such transient protein-protein interactions of complexes between electron carrier proteins and their partner enzymes (11,12,13). This technique was successfully applied to the study of the electron transfer complex between Fd and FNR (9).…”

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“…A series of site-directed mutagenesis experiments on maize Fd demonstrated that certain acidic residues were crucial for interaction and electron transfer with SiR, as is the case for interaction with FNR (7). A recent study on chemical modifications of lysine and arginine residues of maize SiR showed that some basic residues are also involved in SiR binding to Fd (10).Two-dimensional NMR is a useful technique to study such transient protein-protein interactions of complexes between electron carrier proteins and their partner enzymes (11,12,13). This technique was successfully applied to the study of the electron transfer complex between Fd and FNR (9).…”

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NMR Study of the Electron Transfer Complex of Plant Ferredoxin and Sulfite Reductase

Saitoh

Ikegami

Nakayama

et al. 2006

Journal of Biological Chemistry

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Plant ferredoxin serves as the physiological electron donor for sulfite reductase, which catalyzes the reduction of sulfite to sulfide. Ferredoxin and sulfite reductase form an electrostatically stabilized 1:1 complex for the intermolecular electron transfer. The proteinprotein interaction between these proteins from maize leaves was analyzed by nuclear magnetic resonance spectroscopy. Chemical shift perturbation and cross-saturation experiments successfully mapped the location of two major interaction sites of ferredoxin: region 1 including Glu-29, Glu-30, and Asp-34 and region 2 including Glu-92, Glu-93, and Glu-94. The importance of these two acidic patches for interaction with sulfite reductase was confirmed by sitespecific mutation of acidic ferredoxin residues in regions 1 and 2, separately and in combination, by which the ability of mutant ferredoxins to transfer electrons and bind to sulfite reductase was additively lowered. Taken together, this study gives a clear illustration of the molecular interaction between ferredoxin and sulfite reductase. We also present data showing that this interaction surface of ferredoxin significantly differs from that when ferredoxin-NADP ؉ reductase is the interaction partner Plant sulfite reductase (SiR) 2 (EC 1.8.7.1) plays an essential role in the reductive assimilation of sulfate by plants, algae, and cyanobacteria by catalyzing the six-electron reduction of sulfite to sulfide (1). The enzyme is a soluble, monomeric protein with a molecular mass of ϳ65 kDa and contains a single siroheme and a single [4Fe-4S] cluster as prosthetic groups (2, 3). Plant-type ferredoxin (Fd) is a small (11 kDa), one-electron carrier protein with a single [2Fe-2S] cluster and serves as the physiological electron donor for SiR (4). The midpoint redox potential (E m ) values for the [4Fe-4S] cluster and siroheme in maize SiR are Ϫ400 and Ϫ285 mV, respectively (5). Therefore, electron flow to the enzyme from the reduced Fd, which has an Em value ϳ Ϫ400 mV, is thermodynamically favorable A transient electron transfer complex is formed between Fd and SiR with 1:1 stoichiometry to facilitate efficient intermolecular electron transfer (6, 7). Other Fd-dependent enzymes of varying molecular size, primary structure, and prosthetic group composition, such as Fd-NADP ϩ reductase (FNR), nitrite reductase, glutamate synthase, andFd-thioredoxin reductase, also form productive electron transfer complexes with Fd. Several lines of evidence obtained from chemical modification experiments, cross-linking experiments, and mutagenesis experiments have indicated that the complexes between Fd and these Fd-dependent enzymes are mainly stabilized by electrostatic forces through the negative charges of Fd and positive charges of each enzyme (8). An example can be seen in the recently determined crystal structure of the complex between maize leaf Fd and FNR (9). The redox centers of Fd and FNR are in close proximity in the complex to allow fast electron transfer between them. The intermolecular contact site near th...

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The Interactions of Cyanobacterial Cytochromec6 and Cytochrome f, Characterized by NMR

Cited by 33 publications

References 40 publications

Respiratory complexes III and IV can each bind two molecules of cytochrome c at low ionic strength

Respiratory complexes III and IV can each bind two molecules of cytochrome c at low ionic strength

An NMR‐based docking model for the physiological transient complex between cytochrome f and cytochrome c₆

NMR Study of the Electron Transfer Complex of Plant Ferredoxin and Sulfite Reductase

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The Interactions of Cyanobacterial Cytochromec6 and Cytochrome f, Characterized by NMR

Cited by 33 publications

References 40 publications

Respiratory complexes III and IV can each bind two molecules of cytochrome c at low ionic strength

Respiratory complexes III and IV can each bind two molecules of cytochrome c at low ionic strength

An NMR‐based docking model for the physiological transient complex between cytochrome f and cytochrome c6

NMR Study of the Electron Transfer Complex of Plant Ferredoxin and Sulfite Reductase

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An NMR‐based docking model for the physiological transient complex between cytochrome f and cytochrome c₆