Comparison of the binding sites on cytochrome c for cytochrome c oxidase, cytochrome bc1, and cytochrome c1. Differential acetylation of lysyl residues in free and complexed cytochrome c.

Rieder, Rainer; Bosshard, Hans Rudolf

doi:10.1016/s0021-9258(19)85557-6

Cited by 181 publications

(59 citation statements)

References 23 publications

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“…Mitochondrial CcO activity assays revealed that electron flow was significantly lower with the two acetyl-mimetics than with the WT Cc species (Figure 7). These data are consistent with the in vitro electron transfer rate of K53Q to CIV recorded by Bazylianska and colleagues [32] and the involvement of Lys8 at the interface of the Cc-CIV complex reported previously [36,74,84,87]. It has actually been published that there are two binding sites for Cc-the so-called proximal and distal sites-on the surface of CIV, where the surface residues exposed to the binding interface differ [15].…”

Section: Thermodynamics and Kinetics Of Interfacial Electron Transfer In Cytochrome Csupporting

confidence: 90%

“…However, the K D value for the Cc 1 -K8Q Cc complex was slightly lower than for the WT complex. This could be explained by the fact that Lys8 is directly involved in the interaction with Cc 1 [16,74].…”

Section: Arabidopsis Thaliana CC 1 Shows Almost Identical Affinity Towards Human and Arabidopsis Thalianamentioning

confidence: 99%

“…It has been shown that PTMs of Cc are able to regulate its electron-donor function [14,32,39,54,[75][76][77][78][79][80]. Since the patch of positively charged lysine residues of Cc contributes to electrostatic interactions with redox partners in mammals, plants, and yeasts [15,16,34,35,37,74,[81][82][83][84], the redox functionality of Cc may be influenced by lysine mutation.…”

Section: Thermodynamics and Kinetics Of Interfacial Electron Transfer In Cytochrome Cmentioning

confidence: 99%

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Structural and functional insights into lysine acetylation of cytochrome c using mimetic point mutants

et al. 2021

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Post-translational modifications frequently modulate protein functions. Lysine acetylation in particular plays a key role in interactions between respiratory cytochrome c and its metabolic partners. To date, in vivo acetylation of lysines at positions 8 and 53 has specifically been identified in mammalian cytochrome c, but little is known about the structural basis of acetylationinduced functional changes. Here, we independently replaced these two residues in recombinant human cytochrome c with glutamine to mimic lysine acetylation, and then characterized the structure and function of the resulting K8Q and K53Q mutants. We found that the physicochemical features were mostly unchanged in the two acetyl-mimetic mutants, but their thermal stability was significantly altered. Nuclear magnetic resonance chemical shift perturbations of the backbone amide resonances revealed local structural changes, and the thermodynamics and kinetics of electron transfer in mutants immobilized on gold electrodes showed an increase in both protein dynamics and solvent involvement in the redox process. We also observed that the K8Q (but not the K53Q) mutation slightly increased the binding affinity of cytochrome c to its physiological electron donor, cytochrome c 1 -which is a component of mitochondrial complex III, or cytochrome bc 1 -thus suggesting that Lys8 (but not Lys53) is located in the interaction area. Finally, the K8Q and K53Q mutants exhibited reduced efficiency as electron donors to complex IV, or cytochrome c oxidase.

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Section: Thermodynamics and Kinetics Of Interfacial Electron Transfer In Cytochrome Csupporting

confidence: 90%

Section: Arabidopsis Thaliana CC 1 Shows Almost Identical Affinity Towards Human and Arabidopsis Thalianamentioning

confidence: 99%

Section: Thermodynamics and Kinetics Of Interfacial Electron Transfer In Cytochrome Cmentioning

confidence: 99%

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Structural and functional insights into lysine acetylation of cytochrome c using mimetic point mutants

et al. 2021

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“…The electron transfer reactions between cytochrome c and CcO and within CcO have been investigated by several methods (14)(15)(16)(17)(18)(19)(20)(21)(22). Alternative approaches include flow-flash experiments of the reaction of the electrostatic CcO/cytochrome c complex with O 2 (23,24), time-resolved measurements of the reverse electron transfer from the binuclear center to the oxidized heme a and Cu A upon photolysis of the three-electron reduced CO-inhibited enzyme (25) and lightinduced electron injection into the oxidase (8,(26)(27)(28)(29) or the electrostatic cytochrome c/cytochrome oxidase complex (30)(31)(32).…”

Section: Introductionmentioning

confidence: 99%

Rates and Equilibrium of CuA to Heme a Electron Transfer in Paracoccus denitrificans Cytochrome c Oxidase

Farver

Grell

Ludwig

et al. 2006

Biophysical Journal

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Intramolecular electron transfer between CuA and heme a in solubilized bacterial (Paracoccus denitrificans) cytochrome c oxidase was investigated by pulse radiolysis. CuA, the initial electron acceptor, was reduced by 1-methylnicotinamide radicals in a diffusion-controlled reaction, as monitored by absorption changes at 825 nm, followed by partial restoration of the absorption and paralleled by an increase in the heme a absorption at 605 nm. The latter observations indicate partial reoxidation of the CuA center and the concomitant reduction of heme a. The rate constants for heme a reduction and CuA reoxidation were identical within experimental error and independent of the enzyme concentration and its degree of reduction, demonstrating that a fast intramolecular electron equilibration is taking place between CuA and heme a. The rate constants for CuA --> heme a ET and the reverse heme a --> CuA process were found to be 20,400 s(-1) and 10,030 s(-1), respectively, at 25 degrees C and pH 7.5, which corresponds to an equilibrium constant of 2.0. Thermodynamic and activation parameters of these intramolecular ET reactions were determined. The significance of the results, particularly the low activation barriers, is discussed within the framework of the enzyme's known three-dimensional structure, potential ET pathways, and the calculated reorganization energies.

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“…Subunit II contains the dinuclear Cu A center, which has been shown to be the entry site of electrons from cytochrome c. − Electron transfer occurs from Cu A to heme a, heme a 3 and Cu B in subunit I where oxygen is reduced to water. Steady-state kinetic studies have revealed that electrostatic interactions are important for complex formation between Cc and CcO. − Extensive chemical modification studies have identified seven highly conserved lysines surrounding the Cc heme crevice that are involved in electrostatic interactions with cytochrome c oxidase. − The X-ray crystal structures of bovine, Paracoccus denitrificans , and R. sphaeroides CcO , have revealed a hydrophobic patch surrounded by a prominent cluster of acidic residues on subunit II, which have been shown by mutagenesis studies to be involved in the binding of Cc . − An unusual sequence of acidic and aromatic residues terminates with Trp 104 (Figures and ), which is in van der Waals contact with the Cu A electron entry site, and could form an electron transfer pathway from the surface of subunit II to Cu A (Table ). Roberts and Pique have used the computational docking program DOT to characterize the interaction between horse Cc and bovine CcO involving a central hydrophobic domain surrounded by complementary electrostatic and hydrogen bonding interactions at the periphery (Figures and ).…”

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confidence: 99%

Definition of the Interaction Domain and Electron Transfer Route between Cytochrome c and Cytochrome Oxidase

et al. 2019

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The reaction between cytochrome c (Cc) and cytochrome c oxidase (CcO) was studied using horse cytochrome c derivatives labeled with ruthenium trisbipyridine at Cys 39 (Ru-39-Cc). Flash photolysis of a 1:1 complex between Ru-39-Cc and bovine CcO at a low ionic strength resulted in the electron transfer from photoreduced heme c to Cu A with an intracomplex rate constant of k 3 = 6 × 10 4 s −1 . The K13A, K72A, K86A, and K87A Ru-39-Cc mutants had nearly the same k 3 value but bound much more weakly to bovine CcO than wild-type Ru-39-Cc, indicating that lysines 13, 72, 86, and 87 were involved in electrostatic binding to CcO, but were not involved in the electron transfer pathway. The Rhodobacter sphaeroides (Rs) W143F mutant (bovine W104) caused a 450-fold decrease in k 3 but did not affect the binding strength with CcO or the redox potential of Cu A . These results are consistent with a computational model for Cc−CcO (Roberts and Pique (1999) J. Biol. Chem. 274, 38051−38060) with the following electron transfer pathway: heme c → CcO-W104 → CcO-M207 → Cu A . A crystal structure for the Cc−CcO complex with the proposed electron transfer pathway heme c → Cc-C14 → Cc-K13 → CcO-Y105 → CcO-M207 → Cu A (S. Shimada et al. (2017) EMBO J. 36, 291−300) is not consistent with the kinetic results because the K13A mutation had no effect on k 3 . Addition of 40% ethylene glycol (as present during the crystal preparation) decreased k 3 significantly, indicating that it affected the conformation of the complex. This may explain the discrepancy between the current results and the crystallographic structure.

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Comparison of the binding sites on cytochrome c for cytochrome c oxidase, cytochrome bc1, and cytochrome c1. Differential acetylation of lysyl residues in free and complexed cytochrome c.

Cited by 181 publications

References 23 publications

Structural and functional insights into lysine acetylation of cytochrome c using mimetic point mutants

Structural and functional insights into lysine acetylation of cytochrome c using mimetic point mutants

Rates and Equilibrium of CuA to Heme a Electron Transfer in Paracoccus denitrificans Cytochrome c Oxidase

Definition of the Interaction Domain and Electron Transfer Route between Cytochrome c and Cytochrome Oxidase

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