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Redox Enzymes: Molecular Mechanisms, Structural Features, Physiological Roles

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Biophysics".

Deadline for manuscript submissions: closed (31 December 2023) | Viewed by 1359

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Guest Editor
Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Leninskie Gory, Moscow 119991, Russia
Interests: biochemistry; molecular mechanisms of enzyme action; molecular bioenergetics; membrane proteins; respiratory chains; terminal oxidases; cytochromes
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Special Issue Information

Dear Colleagues,

Redox enzymes are enzymes that catalyze biological electron transfer reactions and carry redox-active cofactors for this purpose. Among the redox enzymes are protein complexes of the respiratory chains of mitochondria and bacteria, enzymes involved in photosynthetic metabolism, ROS scavenging enzymes including superoxide dismutases, peroxidases, and catalases, and many others. Redox proteins are the core of the enzymatic antioxidant machinery which helps organisms to prevent or reduce ROS-induced oxidative stress. The investigation of the molecular mechanisms of the energy-transducing redox enzymes allows us to clarify the features of the device and the design of artificial membranes and nanosystems that are able to efficiently convert different forms of energy. The study of respiratory chain enzymes is extremely important and promising from a biomedical point of view. In particular, a comparative study of the heme-copper oxidases and the cytochrome bd oxidases may contribute to the development of new-generation antibiotics.

This Special Issue aims to collect the results of new insights into the molecular mechanisms and structure of the respiratory chain, light-transducing and ROS scavenging enzymes, their physiological roles, assembly pathways, biotechnological applications, and utility as drug targets. Original research articles and up-to-date reviews on these and related topics are welcome in this Special Issue.

Prof. Dr. Vitaliy Borisov
Guest Editor

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Keywords

  • metalloenzyme
  • terminal oxidase
  • cytochrome
  • heme
  • respiratory chain
  • photosynthesis
  • enzyme activation and inhibition
  • ROS scavenging enzyme
  • reactive oxygen species
  • ROS defense mechanism
  • molecular bioenergetics
  • drug target

Published Papers (1 paper)

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20 pages, 3984 KiB  
Article
Membrane-Bound Redox Enzyme Cytochrome bd-I Promotes Carbon Monoxide-Resistant Escherichia coli Growth and Respiration
by Martina R. Nastasi, Vitaliy B. Borisov and Elena Forte
Int. J. Mol. Sci. 2024, 25(2), 1277; https://doi.org/10.3390/ijms25021277 - 20 Jan 2024
Viewed by 757
Abstract
The terminal oxidases of bacterial aerobic respiratory chains are redox-active electrogenic enzymes that catalyze the four-electron reduction of O2 to 2H2O taking out electrons from quinol or cytochrome c. Living bacteria often deal with carbon monoxide (CO) which can [...] Read more.
The terminal oxidases of bacterial aerobic respiratory chains are redox-active electrogenic enzymes that catalyze the four-electron reduction of O2 to 2H2O taking out electrons from quinol or cytochrome c. Living bacteria often deal with carbon monoxide (CO) which can act as both a signaling molecule and a poison. Bacterial terminal oxidases contain hemes; therefore, they are potential targets for CO. However, our knowledge of this issue is limited and contradictory. Here, we investigated the effect of CO on the cell growth and aerobic respiration of three different Escherichia coli mutants, each expressing only one terminal quinol oxidase: cytochrome bd-I, cytochrome bd-II, or cytochrome bo3. We found that following the addition of CO to bd-I-only cells, a minimal effect on growth was observed, whereas the growth of both bd-II-only and bo3-only strains was severely impaired. Consistently, the degree of resistance of aerobic respiration of bd-I-only cells to CO is high, as opposed to high CO sensitivity displayed by bd-II-only and bo3-only cells consuming O2. Such a difference between the oxidases in sensitivity to CO was also observed with isolated membranes of the mutants. Accordingly, O2 consumption of wild-type cells showed relatively low CO sensitivity under conditions favoring the expression of a bd-type oxidase. Full article
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