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Cells
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Cytochrome C—Alternative Functions, New Interactions and Technological Applications
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Cytochrome C—Alternative Functions, New Interactions and Technological Applications

A special issue of Cells (ISSN 2073-4409).

Deadline for manuscript submissions: closed (30 June 2024) | Viewed by 5113

Special Issue Editors

Dr. Tatiana V. Vygodina

E-Mail Website
Guest Editor
Department of Bioenergetics, A.N. Belozersky Institute of Physico-Chemical Biology, M.V. Lomonosov Moscow State University, 119992 Moscow, Russia
Interests: oxidative phosphorylation; mitochondria; respiratory chain; cytochrome oxidase; cytochrome c; reactive oxygen species
Special Issues, Collections and Topics in MDPI journals
Dr. Rita Chertkova

E-Mail Website
Guest Editor
Department of Bioengineering, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, RAS, 117997 Moscow, Russia
Interests: bioengineering; recombinant proteins; structure and functions of proteins; heme-containing proteins; cytochrome C; globins; neuroglobin; apoptosis; electron transport chain; mitochondria; amyloidogenesis; biodetectors and biosensors; bionanoelectronics

Special Issue Information

Dear Colleagues,

Cytochrome c (Сс) is a single-electron carrier between complex bc1 and cytochrome oxidase in the electron transport chain (ETC), located in the intermembrane space of mitochondria (IMS).

In recent years, this small (only 104 amino acids) alkaline protein has received the intense attention of the scientific community due to many additional functions that it plays in the cell: cardiolipin peroxidation, apoptose signaling, apoptosome formation, radical scavenging, participation via Mia40-ALR(Erv) in folding of dithiol proteins in IMS, etc. This Special Issue welcomes studies shedding light on structural features, post-translational modifications (phosphorylation, methylation) or partial activities of the enzyme, allowing it to perform additional functions. Additionally, we will be glad to consider the papers devoted to the design based on cytochrome c of various biosensors, detectors, as well as constructions potentially applicable in bio-nanoelectronics. At the same time, we will be less interested in the articles dealing with the traditional function of cytochrome c as en electron carrier in ETC.

Dr. Tatiana V. Vygodina
Dr. Rita V. Chertkova
Guest Editors

Manuscript Submission Information

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Keywords

  • cytochrome c
  • proapoptotic activities
  • superoxide scavenging
  • peroxidase-like activity
  • mem-brane-permeabilizing activity
  • Raman spectroscopy
  • circular dichroism
  • aggregation
  • post-translational modifications
  • biosensor
  • bio-nanoelectronics

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Published Papers (2 papers)

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Research

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19 pages, 2940 KiB  
Article
Mutant Cytochrome C as a Potential Detector of Superoxide Generation: Effect of Mutations on the Function and Properties
by Rita V. Chertkova, Ilya P. Oleynikov, Alexey A. Pakhomov, Roman V. Sudakov, Victor N. Orlov, Marina A. Semenova, Alexander M. Arutyunyan, Vasily V. Ptushenko, Mikhail P. Kirpichnikov, Dmitry A. Dolgikh and Tatiana V. Vygodina
Cells 2023, 12(18), 2316; https://doi.org/10.3390/cells12182316 - 19 Sep 2023
Cited by 2 | Viewed by 1649
Abstract
Cytochrome c (CytC) is a single-electron carrier between complex bc1 and cytochrome c-oxidase (CcO) in the electron transport chain (ETC). It is also known as a good radical scavenger but its participation in electron flow through the ETC makes it impossible to use [...] Read more.
Cytochrome c (CytC) is a single-electron carrier between complex bc1 and cytochrome c-oxidase (CcO) in the electron transport chain (ETC). It is also known as a good radical scavenger but its participation in electron flow through the ETC makes it impossible to use CytC as a radical sensor. To solve this problem, a series of mutants were constructed with substitutions of Lys residues in the universal binding site (UBS) which interact electrostatically with negatively charged Asp and Glu residues at the binding sites of CytC partners, bc1 complex and CcO. The aim of this study was to select a mutant that had lost its function as an electron carrier in the ETC, retaining the structure and ability to quench radicals. It was shown that a mutant CytC with substitutions of five (8Mut) and four (5Mut) Lys residues in the UBS was almost inactive toward CcO. However, all mutant proteins kept their antioxidant activity sufficiently with respect to the superoxide radical. Mutations shifted the dipole moment of the CytC molecule due to seriously changed electrostatics on the surface of the protein. In addition, a decrease in the redox potential of the protein as revealed by the redox titrations of 8Mut was detected. Nevertheless, the CD spectrum and dynamic light scattering suggested no significant changes in the secondary structure or aggregation of the molecules of CytC 8Mut. Thus, a variant 8Mut with multiple mutations in the UBS which lost its ability to electron transfer and saved most of its physico-chemical properties can be effectively used as a detector of superoxide generation both in mitochondria and in other systems. Full article
(This article belongs to the Special Issue Cytochrome C—Alternative Functions, New Interactions and Technological Applications)
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Review

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21 pages, 2435 KiB  
Review
Phosphorylations and Acetylations of Cytochrome c Control Mitochondrial Respiration, Mitochondrial Membrane Potential, Energy, ROS, and Apoptosis
by Paul T. Morse, Tasnim Arroum, Junmei Wan, Lucynda Pham, Asmita Vaishnav, Jamie Bell, Lauren Pavelich, Moh H. Malek, Thomas H. Sanderson, Brian F.P. Edwards and Maik Hüttemann
Cells 2024, 13(6), 493; https://doi.org/10.3390/cells13060493 - 12 Mar 2024
Cited by 15 | Viewed by 2934
Abstract
Cytochrome c (Cytc) has both life-sustaining and cellular death-related functions, depending on subcellular localization. Within mitochondria, Cytc acts as a single electron carrier as part of the electron transport chain (ETC). When released into the cytosol after cellular insult, Cyt [...] Read more.
Cytochrome c (Cytc) has both life-sustaining and cellular death-related functions, depending on subcellular localization. Within mitochondria, Cytc acts as a single electron carrier as part of the electron transport chain (ETC). When released into the cytosol after cellular insult, Cytc triggers the assembly of the apoptosome, committing the cell to intrinsic apoptosis. Due to these dual natures, Cytc requires strong regulation by the cell, including post-translational modifications, such as phosphorylation and acetylation. Six phosphorylation sites and three acetylation sites have been detected on Cytc in vivo. Phosphorylations at T28, S47, Y48, T49, T58, and Y97 tend to be present under basal conditions in a tissue-specific manner. In contrast, the acetylations at K8, K39, and K53 tend to be present in specific pathophysiological conditions. All of the phosphorylation sites and two of the three acetylation sites partially inhibit respiration, which we propose serves to maintain an optimal, intermediate mitochondrial membrane potential (ΔΨm) to minimize reactive oxygen species (ROS) production. Cytc phosphorylations are lost during ischemia, which drives ETC hyperactivity and ΔΨm hyperpolarization, resulting in exponential ROS production thus causing reperfusion injury following ischemia. One of the acetylation sites, K39, shows a unique behavior in that it is gained during ischemia, stimulating respiration while blocking apoptosis, demonstrating that skeletal muscle, which is particularly resilient to ischemia-reperfusion injury compared to other organs, possesses a different metabolic strategy to handle ischemic stress. The regulation of Cytc by these post-translational modifications underscores the importance of Cytc for the ETC, ΔΨm, ROS production, apoptosis, and the cell as a whole. Full article
(This article belongs to the Special Issue Cytochrome C—Alternative Functions, New Interactions and Technological Applications)
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