Tungsten in biological systems

Kletzin, Arnulf; Adams, Michael W. W.

doi:10.1111/j.1574-6976.1996.tb00226.x

Cited by 302 publications

(164 citation statements)

References 284 publications

(318 reference statements)

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“…However, the capability of E. coli ModA to interact with W has no physiological basis, as E. coli does not utilize W-cofactor-containing enzymes and, in many instances, W substitution for Mo results in enzyme inactivation (38). Only a single exception has been reported, with the in vivo substitution of W in the molybdoenzyme trimethylamine N-oxide (TMAO) reductase (39).…”

Section: Moda Is Required For Mo Acquisitionmentioning

confidence: 99%

Acquisition and Role of Molybdate in Pseudomonas aeruginosa

Pederick

Eijkelkamp

Ween

et al. 2014

Appl Environ Microbiol

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In microaerophilic or anaerobic environments, Pseudomonas aeruginosa utilizes nitrate reduction for energy production, a process dependent on the availability of the oxyanionic form of molybdenum, molybdate (MoO 4 2؊ ). Here, we show that molybdate acquisition in P. aeruginosa occurs via a high-affinity ATP-binding cassette permease (ModABC). ModA is a cluster D-III solute binding protein capable of interacting with molybdate or tungstate oxyanions. Deletion of the modA gene reduces cellular molybdate concentrations and results in inhibition of anaerobic growth and nitrate reduction. Further, we show that conditions that permit nitrate reduction also cause inhibition of biofilm formation and an alteration in fatty acid composition of P. aeruginosa. Collectively, these data highlight the importance of molybdate for anaerobic growth of P. aeruginosa and reveal novel consequences of nitrate reduction on biofilm formation and cell membrane composition.

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Section: Moda Is Required For Mo Acquisitionmentioning

confidence: 99%

Acquisition and Role of Molybdate in Pseudomonas aeruginosa

Pederick

Eijkelkamp

Ween

et al. 2014

Appl Environ Microbiol

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“…Although molybdenum-containing enzymes are ubiquitous in biology, microorganisms that require tungsten are extremely limited (10). Indeed, tungsten and molybdenum have such similar chemical and physical properties that almost all microorganisms cannot distinguish between them and often times incorporate tungsten into their molybdoenzymes.…”

mentioning

confidence: 99%

“…P. furious grows by fermenting sugars (but not cellulose) and peptides and contains five members of the AOR family (abbreviated AOR [17], GAPOR [18], FOR [19], WOR4 [20], and WOR5 [21]), all of which oxidize aldehydes of various types. The prototypical AOR has a broad substrate specificity and is thought to be involved in peptide catabolism wherein it oxidizes amino acid-derived aldehydes (10).…”

mentioning

confidence: 99%

A New Class of Tungsten-Containing Oxidoreductase in Caldicellulosiruptor, a Genus of Plant Biomass-Degrading Thermophilic Bacteria

Scott

Rubinstein

Lipscomb

et al. 2015

Appl Environ Microbiol

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bCaldicellulosiruptor bescii grows optimally at 78°C and is able to decompose high concentrations of lignocellulosic plant biomass without the need for thermochemical pretreatment. C. bescii ferments both C 5 and C 6 sugars primarily to hydrogen gas, lactate, acetate, and CO 2 and is of particular interest for metabolic engineering applications given the recent availability of a genetic system. Developing optimal strains for technological use requires a detailed understanding of primary metabolism, particularly when the goal is to divert all available reductant (electrons) toward highly reduced products such as biofuels. During an analysis of the C. bescii genome sequence for oxidoreductase-type enzymes, evidence was uncovered to suggest that the primary redox metabolism of C. bescii has a completely uncharacterized aspect involving tungsten, a rarely used element in biology. An active tungsten utilization pathway in C. bescii was demonstrated by the heterologous production of a tungsten-requiring, aldehyde-oxidizing enzyme (AOR) from the hyperthermophilic archaeon Pyrococcus furiosus. Furthermore, C. bescii also contains a tungsten-based AOR-type enzyme, here termed XOR, which is phylogenetically unique, representing a completely new member of the AOR tungstoenzyme family. Moreover, in C. bescii, XOR represents ca. 2% of the cytoplasmic protein. XOR is proposed to play a key, but as yet undetermined, role in the primary redox metabolism of this cellulolytic microorganism.T hermophilic bacteria of the genus Caldicellulosiruptor are currently under intense investigation due to their ability to decompose lignocellulosic plant biomass anaerobically at high temperature, thereby potentially mitigating costly thermochemical pretreatment steps (1, 2). One of these species, Caldicellulosiruptor bescii, has an optimal growth temperature of 78°C and is the most thermophilic cellulose degrader known to date. It is able to ferment high concentrations of cellulosic feedstock primarily to hydrogen gas, lactate, acetate, and CO 2 (3, 4). Species from this genus can degrade cellulose (and also xylan), using novel multidomain glycosyl hydrolases, representing a new paradigm in cellulose conversion by anaerobic thermophiles (2). Moreover, the recent development of a genetic system for C. bescii creates potential for using this and related species for consolidated biomass processing in the production of liquid fuels (5).Developing metabolic engineering strategies for any microorganism obviously requires an in-depth understanding of their primary metabolism. Evidence that C. bescii may have a completely uncharacterized aspect to its primary redox metabolism came from an analysis of its genome sequence for molybdoenzymes (6). These are present in virtually all forms of life, serving diverse roles in primary metabolism of carbon, nitrogen and sulfur (7). As expected, we found that the C. bescii genome contains genes necessary for the synthesis of the pyranopterin cofactor that coordinates molybdenum (Mo) in such enzymes (7). Accordin...

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“…3,4), tungsten has joined its congener molybdenum as a component of redox enzymes (ref. 5,6). The molybdenum and tungsten enzymes have been extensively reviewed in recent years (ref.…”

Section: Molybdenum and Tungsten Enzymesmentioning

confidence: 99%

“…The molybdenum and tungsten enzymes have been extensively reviewed in recent years (ref. [5][6][7][8][9][10][11][12][13][14][15][16][17][18].…”

Section: Molybdenum and Tungsten Enzymesmentioning

confidence: 99%

Transition metal sulfur chemistry and its relevance to molybdenum and tungsten enzymes

Stiefel¹

1998

Pure and Applied Chemistry

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Molybdenum or tungsten is present at the active sites of over 30 distinct enzymes. The Mo enzyme nitrogenase, with its unique polynuclear metal sulfide clusters, falls in a class by itself All other Mo and W enzymes are mononuclear, with pterin-ene-dithiolate coordination. Recent x-ray crystallographic results on several of these enzymes confirm the potential additional presence of 0x0 (one or two), sulfido, cysteine, selenocysteine, serine, aquohydroxo, and/or a second dithiolene in the various metal coordination spheres. The rich chemistry of multisulhr transition metal systems admits ligand redox, internal electron transfer, and 'intermediate' redox states. This redox flexibility may facilitate coupled protodelectron transfer and/or 0x0 transfer mechanisms, which are effectively exploited by Mo and W enzymes. In the case of nitrogenase, a hypothesis is put forward that the relatively isolated heavy atom grouping at the FeMoco active site allows that site to become locally 'hot' during turnover, thereby facilitating activation of the recalcitrant dinitrogen molecule. MOLYBDENUM AND TUNGSTEN ENZYMESMolybdenum has been recognized as a requirement for bacterial nitrogen fixation for over 60 years (ref. 1) and as an essential element for animals for over 40 years (ref. 2). In the last 20 years (ref. 3,4), tungsten has joined its congener molybdenum as a component of redox enzymes (ref. 5,6). The molybdenum and tungsten enzymes have been extensively reviewed in recent years (ref. 5-18).Nitrogenase, the enzyme responsible for nitrogen fixation, falls in a class by itself. Its metalloclusters, the P cluster and iron molybdenum cofactor, FeMoco, are polynuclear metal sulfide groupings arrayed to catalyze the multielectron reduction of the dinitrogen molecule (ref.

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Tungsten in biological systems

Cited by 302 publications

References 284 publications

Acquisition and Role of Molybdate in Pseudomonas aeruginosa

Acquisition and Role of Molybdate in Pseudomonas aeruginosa

A New Class of Tungsten-Containing Oxidoreductase in Caldicellulosiruptor, a Genus of Plant Biomass-Degrading Thermophilic Bacteria

Transition metal sulfur chemistry and its relevance to molybdenum and tungsten enzymes

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