ATP Synthases from Microbes: The Beauty of a Molecular Nanomotor and Its Importance in Medical Health

Dear Colleagues,

As you know very well, the central energy production of all living beings stems from the transmembranous chemiosmotic process of oxidative phosphorylation or photophosphorylation from Archaea and Bacteria to the actual mitochondria, with the latter in Eukarya. According to the Chemiosmotic Hypothesis of Peter Mitchell—now largely confirmed after its initial postulation in 1961—the proton motive force (pmf) generated by the respiratory or photosynthetic electron transfer chains is consumed by the respective, archeal, bacterial, and mitochondrial F₁F_O-ATP synthases, producing the central energy currency of the cells, i.e., ATP. The bacterial ATP synthases and their structure, function, and regulation are the main subjects of this state-of-the-art Special Issue.

There are several progresses in the understanding of the structure, function, and regulation of mitochondrial ATP synthases, which can form dimers and oligomers, creating mitochondrial cristae. However, bacterial ATP synthases have recently become a focal point of research because of their structural key regulatory elements that show different modes of regulation in bacteria. For a long time, the epsilon subunit of some γ-proteobateria was thought to be a canonical inhibitor of all bacterial ATP synthases. However, recently, it has become evident that ε works as an inhibitor only in some γ-proteobacteria, and it especially does not work in α-proteobacteria, where ε has lost its inhibitory properties. Furthermore, this inhibitory role has been acquired by a novel family of ζ subunits in α-proteobacteria. In addition, another regulatory subunit seems to play this inhibitory role in cyanobacteria. Therefore, an update on this subject is more than needed, and this is the main focus of this Special Issue.

In recent years, bacterial ATP synthases became of particular interest in the latest studies. This occurred due to the urgent need to combat pathogenic bacteria’s resistance to various antibiotics, particularly regarding human and animal pathogens. In addition, the ATP synthases of some unicellular eukaryotes and/or parasites have also began to receive attention. Thus, bacterial and parasitic ATP synthases have become a target for the design and development of new antimicrobial agents, for instance, against Mycobacteruim tuberculosis, where a case of success for bedaquiline has become useful. Moreover, they are being used against some other important bacterial pathogens and eukaryotic parasites. This allows us to describe the actual and putative structural targets for the design of new antimicrobial agents designed to bind the core or regulatory subunits of these ATP synthases of pathogenic bacteria or parasites, ultimately leading to an increase in the interest on this subject in relation to the structure, function, and regulation of bacterial ATP synthases.

Prof. Dr. José J. García-Trejo
Prof. Dr. Gerhard Gruber
Guest Editors

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• bacterial
• ATP synthases
• inhibitory
• subunits
• target
• antimicrobials