Assembly pathway of a bacterial complex iron sulfur molybdoenzyme

Cherak, Stephana J.; Turner, Raymond J.

doi:10.1515/bmc-2017-0011

Cited by 7 publications

(6 citation statements)

References 133 publications

(199 reference statements)

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“…Formation of these Mo-PPT derivatives is catalyzed by the MocA and MobA proteins, with MobB likely to contribute to the process (Palmer et al, 1994(Palmer et al, , 1996Guse et al, 2003;Neumann et al, 2009b;Leimkühler, 2014) (Figure 2). Pathways for the incorporation of the cofactors into individual molybdoenzymes follow enzyme-specific pathways that often require maturation chaperones (Leimkühler and Klipp, 1999;Oresnik et al, 2001;Turner et al, 2004;Iobbi-Nivol and Leimkühler, 2013;Cherak and Turner, 2017). Further information about Mo-PPT biosynthesis can be found in several excellent review papers (Leimkühler et al, 2011;Magalon et al, 2011;Iobbi-Nivol and Leimkühler, 2013;Mendel, 2013;Hille et al, 2014;Leimkühler and Iobbi-Nivol, 2016;Leimkühler, 2020;Mayr et al, 2020).…”

Section: The Molybdenum-pyranopterin Cofactor and Its Biosynthesismentioning

confidence: 99%

Molybdenum Enzymes and How They Support Virulence in Pathogenic Bacteria

2020

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Mononuclear molybdoenzymes are highly versatile catalysts that occur in organisms in all domains of life, where they mediate essential cellular functions such as energy generation and detoxification reactions. Molybdoenzymes are particularly abundant in bacteria, where over 50 distinct types of enzymes have been identified to date. In bacterial pathogens, all aspects of molybdoenzyme biology such as molybdate uptake, cofactor biosynthesis, and function of the enzymes themselves, have been shown to affect fitness in the host as well as virulence. Although current studies are mostly focused on a few key pathogens such as Escherichia coli, Salmonella enterica, Campylobacter jejuni, and Mycobacterium tuberculosis, some common themes for the function and adaptation of the molybdoenzymes to pathogen environmental niches are emerging. Firstly, for many of these enzymes, their role is in supporting bacterial energy generation; and the corresponding pathogen fitness and virulence defects appear to arise from a suboptimally poised metabolic network. Secondly, all substrates converted by virulence-relevant bacterial Mo enzymes belong to classes known to be generated in the host either during inflammation or as part of the host signaling network, with some enzyme groups showing adaptation to the increased conversion of such substrates. Lastly, a specific adaptation to bacterial in-host survival is an emerging link between the regulation of molybdoenzyme expression in bacterial pathogens and the presence of immune system-generated reactive oxygen species. The prevalence of molybdoenzymes in key bacterial pathogens including ESKAPE pathogens, paired with the mounting evidence of their central roles in bacterial fitness during infection, suggest that they could be important future drug targets.

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Section: The Molybdenum-pyranopterin Cofactor and Its Biosynthesismentioning

confidence: 99%

Molybdenum Enzymes and How They Support Virulence in Pathogenic Bacteria

2020

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“…Some species, such as Haloferax mediterranei have developed strategies to enable survival and growth in the absence of oxygen (Matarredona et al ., 2020). Other halophile species can also use alternative electron acceptors for anaerobic respiration, these include nitrate, (NO 3 − ), nitrite (NO 2 − ), fumarate (C 4 H 4 O 4 ), dimethyl sulfoxide (DMSO), and/or trimethylamine N‐oxide (TMAO) (Hartmann et al ., 1980; Oren, 2013; Cherak and Turner, 2017). In the current study, functional analyses of salticle‐, brine‐pool, and soil metagenomes were used to determine the abundance of genes related to anaerobic respiration, many of which belong within the iron–sulfur molybdoenzyme (CISM) family (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…Haloarchaea generally grow as aerobic chemoheterotrophs, but there is limited solubility of oxygen in brines. Some species, such as Haloferax mediterranei have developed strategies to enable survival and growth in the absence of oxygen (Matarredona et al, 2020 (Hartmann et al, 1980;Oren, 2013;Cherak and Turner, 2017). In the current study, functional analyses of salticle-, brine-pool, and soil metagenomes were used to determine the abundance of genes related to anaerobic respiration, many of which belong within the iron-sulfur molybdoenzyme (CISM) family (Fig.…”

Section: Capacity For Osmoregulation In Nacl-saturated Solutionsmentioning

confidence: 99%

Microbiology of a NaCl stalactite ‘salticle’ in Triassic halite

Thompson

Kelly

Skvortsov

et al. 2021

Environmental Microbiology

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Large regions of Earth's surface are underlain by salt deposits that evaporated from ancient oceans and are populated by extreme halophilic microbes. Some of these halophiles may have been preserved over geological timescales within hypersaline fluid inclusions, but ingresses of water and/or anthropogenic activities can lead to the formation of alternative habitats, including NaCl stalactites or other speleothems. While the microbiology of ancient evaporites has been well studied, the ecology of these recently formed structures is less-well understood. Here, the microbiology of a NaCl stalactite ('salticle') in a Triassic halite mine is characterized. The specific aims were to determine the presence of fluid inclusions, determine the microbial structure of the salticle compared with a nearby brine-pool and surficial soil, and characterize the ecophysiological capabilities of this unique ecosystem. The salticle contained fluid inclusions, and their microbiome was composed of Euryarchaetota, Proteobacteria, and Actinobacteria, with Haloarchaea in greater abundance than brinepool or soil microbiomes. The salticle metagenome exhibited a greater abundance of genes involved in osmoregulation, anaerobic respiration, UV resistance, oxidative stress, and stress-protein synthesis relative to the soil microbiome. We discuss the potential astrobiological implications of salticles as enclosed salt-saturated habitats that are protected from ionizing radiation and have a stable water activity.

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“…The molybdenum is found in a variety of enzymes that catalyze hydride transfers that are coupled with redox reactions. Examples of these enzymes are present in the xanthine oxidase (EC 1.17.3.2, XO) [118], DMSO reductase (EC 1.8.5.3) [119], and sulfite oxidase (EC 1.8.3.1, SO) [120] families [121]. In these enzymes, the Mo ion is coordinated to one or two pyranopterin dithiolene ligands (PDT), forming what is known as a molybdenopterin cofactor.…”

Section: Enzymes That Catalyze the Hydride Transfer Reactionsmentioning

confidence: 99%

Formation of Unstable and very Reactive Chemical Species Catalyzed by Metalloenzymes: A Mechanistic Overview

et al. 2019

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Nature has tailored a wide range of metalloenzymes that play a vast array of functions in all living organisms and from which their survival and evolution depends on. These enzymes catalyze some of the most important biological processes in nature, such as photosynthesis, respiration, water oxidation, molecular oxygen reduction, and nitrogen fixation. They are also among the most proficient catalysts in terms of their activity, selectivity, and ability to operate at mild conditions of temperature, pH, and pressure. In the absence of these enzymes, these reactions would proceed very slowly, if at all, suggesting that these enzymes made the way for the emergence of life as we know today. In this review, the structure and catalytic mechanism of a selection of diverse metalloenzymes that are involved in the production of highly reactive and unstable species, such as hydroxide anions, hydrides, radical species, and superoxide molecules are analyzed. The formation of such reaction intermediates is very difficult to occur under biological conditions and only a rationalized selection of a particular metal ion, coordinated to a very specific group of ligands, and immersed in specific proteins allows these reactions to proceed. Interestingly, different metal coordination spheres can be used to produce the same reactive and unstable species, although through a different chemistry. A selection of hand-picked examples of different metalloenzymes illustrating this diversity is provided and the participation of different metal ions in similar reactions (but involving different mechanism) is discussed.

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Assembly pathway of a bacterial complex iron sulfur molybdoenzyme

Cited by 7 publications

References 133 publications

Molybdenum Enzymes and How They Support Virulence in Pathogenic Bacteria

Molybdenum Enzymes and How They Support Virulence in Pathogenic Bacteria

Microbiology of a NaCl stalactite ‘salticle’ in Triassic halite

Formation of Unstable and very Reactive Chemical Species Catalyzed by Metalloenzymes: A Mechanistic Overview

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