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L'vov, N. P.; Nosikov, A N; Антипов, А. Н.

doi:10.1023/a:1014461913945

Cited by 49 publications

(21 citation statements)

References 39 publications

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“…In MoCo, the pterin platform has two sulfur atoms that bind the Mo atom and, in aldehyde oxidase, there is a third sulfane sulfur atom terminally bonded to the Mo atom; all three sulfur atoms originate as S 0 extracted from cysteine by pyridoxal 5′-phosphate (PLP)-containing cysteine desulfurases [9]. In the tungsten-containing enzymes of hyperthermophilic archaea, the Mo is replaced by its congener, W, on the two sulfur atoms of the same pterin platform [10]. …”

Section: Sulfur In Biologymentioning

confidence: 99%

Thiosulfoxide (Sulfane) Sulfur: New Chemistry and New Regulatory Roles in Biology

Toohey¹,

2014

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The understanding of sulfur bonding is undergoing change. Old theories on hypervalency of sulfur and the nature of the chalcogen-chalcogen bond are now questioned. At the same time, there is a rapidly expanding literature on the effects of sulfur in regulating biological systems. The two fields are inter-related because the new understanding of the thiosulfoxide bond helps to explain the newfound roles of sulfur in biology. This review examines the nature of thiosulfoxide (sulfane, S0) sulfur, the history of its regulatory role, its generation in biological systems, and its functions in cells. The functions include synthesis of cofactors (molybdenum cofactor, iron-sulfur clusters), sulfuration of tRNA, modulation of enzyme activities, and regulating the redox environment by several mechanisms (including the enhancement of the reductive capacity of glutathione). A brief review of the analogous form of selenium suggests that the toxicity of selenium may be due to over-reduction caused by the powerful reductive activity of glutathione perselenide.

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Section: Sulfur In Biologymentioning

confidence: 99%

Thiosulfoxide (Sulfane) Sulfur: New Chemistry and New Regulatory Roles in Biology

Toohey¹,

2014

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“…It has been reported that W is needed for enzymes within the aldehyde:ferredoxin oxidoreductase (AOR) family and some other enzymes belonging to molybdoprotein families in certain prokaryotes [ 7 – 10 ]. Although molybdoproteins and tungstoproteins appeared to have a preference for either of the two metals in many cases [ 8 – 10 ], the presence or exchange of both metals in certain enzymes has also been reported [ 11 ]. So far it is very difficult to distinguish the utilization of Mo and W in the majority of molybdoproteins due to similar physical-chemical and functional properties between them.…”

Section: Introductionmentioning

confidence: 99%

Comparative genomics of molybdenum utilization in prokaryotes and eukaryotes

Peng

Zhang

2018

BMC Genomics

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BackgroundMolybdenum (Mo) is an essential micronutrient for almost all biological systems, which holds key positions in several enzymes involved in carbon, nitrogen and sulfur metabolism. In general, this transition metal needs to be coordinated to a unique pterin, thus forming a prosthetic group named molybdenum cofactor (Moco) at the catalytic sites of molybdoenzymes. The biochemical functions of many molybdoenzymes have been characterized; however, comprehensive analyses of the evolution of Mo metabolism and molybdoproteomes are quite limited.ResultsIn this study, we analyzed almost 5900 sequenced organisms to examine the occurrence of the Mo utilization trait at the levels of Mo transport system, Moco biosynthetic pathway and molybdoproteins in all three domains of life. A global map of Moco biosynthesis and molybdoproteins has been generated, which shows the most detailed understanding of Mo utilization in prokaryotes and eukaryotes so far. Our results revealed that most prokaryotes and all higher eukaryotes utilize Mo whereas many unicellular eukaryotes such as parasites and most yeasts lost the ability to use this metal. By characterizing the molybdoproteomes of all organisms, we found many new molybdoprotein-rich species, especially in bacteria. A variety of new domain fusions were detected for different molybdoprotein families, suggesting the presence of novel proteins that are functionally linked to molybdoproteins or Moco biosynthesis. Moreover, horizontal gene transfer event involving both the Moco biosynthetic pathway and molybdoproteins was identified. Finally, analysis of the relationship between environmental factors and Mo utilization showed new evolutionary trends of the Mo utilization trait.ConclusionsOur data provide new insights into the evolutionary history of Mo utilization in nature.Electronic supplementary materialThe online version of this article (10.1186/s12864-018-5068-0) contains supplementary material, which is available to authorized users.

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“…Tungsten is the heaviest chemical element in biology, and plays essential roles in biological carbon, nitrogen, and sulfur metabolisms [1][2][3][4][5][6][7][8]. In tungsten-dependent enzymes, the tungsten ion has an oxidation number varying from +4 to +6 and is seen to be bound to pterin cofactors.…”

Section: Introductionmentioning

confidence: 99%