Electric field-induced functional changes in electrode-immobilized mutant species of human cytochrome c

Olloqui‐Sariego, José Luis; Pérez‐Mejías, Gonzalo; Márquez, Inmaculada; Guerra‐Castellano, Alejandra; Calvente, Juan José; Rosa, Miguel A. De la; Andreu, Rafael; Dı́az-Moreno, Irene

doi:10.1016/j.bbabio.2022.148570

Cited by 4 publications

(2 citation statements)

References 80 publications

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“…Cc Y97 is phosphorylated in heart, and the K m for the reaction with CcO is increased 2-fold [ 74 ]. Tyr 97 phosphorylation was also characterized with the replacement of tyrosine with a phosphomimetic, p-carboxymethyl-L-phenylalanine (pCMF), which actually increased the CcO activity [ 75 , 76 ]. Cc is phosphorylated at T58 in rat kidney, which controls mitochondrial respiration and apoptosis [ 77 ].…”

Section: Discussionmentioning

confidence: 99%

Accelerated Evolution of Cytochrome c in Higher Primates, and Regulation of the Reaction between Cytochrome c and Cytochrome Oxidase by Phosphorylation

Brand¹,

Scharlau

Geren

et al. 2022

Cells

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Cytochrome c (Cc) underwent accelerated evolution from the stem of the anthropoid primates to humans. Of the 11 amino acid changes that occurred from horse Cc to human Cc, five were at Cc residues near the binding site of the Cc:CcO complex. Single-point mutants of horse and human Cc were made at each of these positions. The Cc:CcO dissociation constant KD of the horse mutants decreased in the order: T89E > native horse Cc > V11I Cc > Q12M > D50A > A83V > native human. The largest effect was observed for the mutants at residue 50, where the horse Cc D50A mutant decreased KD from 28.4 to 11.8 μM, and the human Cc A50D increased KD from 4.7 to 15.7 μM. To investigate the role of Cc phosphorylation in regulating the reaction with CcO, phosphomimetic human Cc mutants were prepared. The Cc T28E, S47E, and Y48E mutants increased the dissociation rate constant kd, decreased the formation rate constant kf, and increased the equilibrium dissociation constant KD of the Cc:CcO complex. These studies indicate that phosphorylation of these residues plays an important role in regulating mitochondrial electron transport and membrane potential ΔΨ.

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Section: Discussionmentioning

confidence: 99%

Accelerated Evolution of Cytochrome c in Higher Primates, and Regulation of the Reaction between Cytochrome c and Cytochrome Oxidase by Phosphorylation

Brand¹,

Scharlau

Geren

et al. 2022

Cells

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“…It has already been shown that different electric field modalities, such as oscillating [ 30 , 31 ] and static fields [ 32 , 33 ] can induce significant structural changes in amylogenic proteins [ 34 , 35 ] and disrupt aggregations and fibrils [ 36 ]. Studies also report electric field-induced changes in activity [ 37 , 38 ], hydration [ 39 ], and adsorption [ 40 ] of proteins. Molecular dynamics (MD) simulation is one of the leading tools to study biomolecular phenomena due to the valuable molecular information that can be obtained.…”

Section: Introductionmentioning

confidence: 99%

Effect of Electric Field on α-Synuclein Fibrils: Revealed by Molecular Dynamics Simulations

Razzokov

Fazliev

Makhkamov³

et al. 2023

IJMS

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The self-association of amylogenic proteins to the fibril form is considered a pivotal factor in the pathogenesis of neurodegenerative diseases, including Parkinson’s disease (PD). PD causes unintended or uncontrollable movements in its common symptoms. α-synuclein is the major cause of PD development and thus has been the main target of numerous studies to suppress and sequester its expression or effectively degrade it. Nonetheless, to date, there are no efficient and proven ways to prevent pathological protein aggregation. Recent investigations proposed applying an external electric field to interrupt the fibrils. This method is a non-invasive approach that has a certain benefit over others. We performed molecular dynamics (MD) simulations by applying an electric field on highly toxic fibrils of α-synuclein to gain a molecular-level insight into fibril disruption mechanisms. The results revealed that the applied external electric field induces substantial changes in the conformation of the α-synuclein fibrils. Furthermore, we show the threshold value for electric field strength required to completely disrupt the α-synuclein fibrils by opening the hydrophobic core of the fibril. Thus, our findings might serve as a valuable foundation to better understand molecular-level mechanisms of the α-synuclein fibrils disaggregation process under an applied external electric field.

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SERS uncovers the link between conformation of cytochrome c heme and mitochondrial membrane potential

Brazhe

Nikelshparg

Baizhumanov

et al. 2023

Free Radical Biology and Medicine

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Electric field-induced functional changes in electrode-immobilized mutant species of human cytochrome c

Cited by 4 publications

References 80 publications

Accelerated Evolution of Cytochrome c in Higher Primates, and Regulation of the Reaction between Cytochrome c and Cytochrome Oxidase by Phosphorylation

Accelerated Evolution of Cytochrome c in Higher Primates, and Regulation of the Reaction between Cytochrome c and Cytochrome Oxidase by Phosphorylation

Effect of Electric Field on α-Synuclein Fibrils: Revealed by Molecular Dynamics Simulations

SERS uncovers the link between conformation of cytochrome c heme and mitochondrial membrane potential

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