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Why is manganese so valuable to bacterial pathogens?
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SYSNO ASEP 0570247 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Why is manganese so valuable to bacterial pathogens? Tvůrce(i) Čapek, Jan (MBU-M) ORCID
Večerek, Branislav (MBU-M) RID, ORCIDČíslo článku 943390 Zdroj.dok. Frontiers in Cellular and Infection Microbiology. - : Frontiers Media - ISSN 2235-2988
Roč. 13, 3 February (2023)Poč.str. 29 s. Jazyk dok. eng - angličtina Země vyd. CH - Švýcarsko Klíč. slova manganese ; metallostasis ; pathogenesis ; mismetallation ; iron ; oxidative stress Obor OECD Microbiology CEP GA23-05634S GA ČR - Grantová agentura ČR Způsob publikování Open access Institucionální podpora MBU-M - RVO:61388971 UT WOS 000939239600001 EID SCOPUS 85148421126 DOI 10.3389/fcimb.2023.943390 Anotace Apart from oxygenic photosynthesis, the extent of manganese utilization in bacteria varies from species to species and also appears to depend on external conditions. This observation is in striking contrast to iron, which is similar to manganese but essential for the vast majority of bacteria. To adequately explain the role of manganese in pathogens, we first present in this review that the accumulation of molecular oxygen in the Earth's atmosphere was a key event that linked manganese utilization to iron utilization and put pressure on the use of manganese in general. We devote a large part of our contribution to explanation of how molecular oxygen interferes with iron so that it enhances oxidative stress in cells, and how bacteria have learned to control the concentration of free iron in the cytosol. The functioning of iron in the presence of molecular oxygen serves as a springboard for a fundamental understanding of why manganese is so valued by bacterial pathogens. The bulk of this review addresses how manganese can replace iron in enzymes. Redox-active enzymes must cope with the higher redox potential of manganese compared to iron. Therefore, specific manganese-dependent isoenzymes have evolved that either lower the redox potential of the bound metal or use a stronger oxidant. In contrast, redox-inactive enzymes can exchange the metal directly within the individual active site, so no isoenzymes are required. It appears that in the physiological context, only redox-inactive mononuclear or dinuclear enzymes are capable of replacing iron with manganese within the same active site. In both cases, cytosolic conditions play an important role in the selection of the metal used. In conclusion, we summarize both well-characterized and less-studied mechanisms of the tug-of-war for manganese between host and pathogen. Pracoviště Mikrobiologický ústav Kontakt Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Rok sběru 2024 Elektronická adresa https://www.frontiersin.org/articles/10.3389/fcimb.2023.943390/full
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