Spectroscopic Studies of Mononuclear Molybdenum Enzyme Centers
Molecules, 2022 A concise review is provided of the contributions that various spectroscopic methods have made to our understanding of the physical and electronic structures of mononuclear molybdenum enzymes.
Martin L. Kirk, Russ Hille
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The genetic basis of energy conservation in the sulfate-reducing bacterium Desulfovibrio alaskensis G20. [PDF]
, 2014 Sulfate-reducing bacteria play major roles in the global carbon and sulfur cycles, but it remains unclear how reducing sulfate yields energy. To determine the genetic basis of energy conservation, we measured the fitness of thousands of pooled mutants of
Arkin, Adam P +6 more
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Frontiers in Microbiology, 2011 Sulfite dehydrogenases are enzymes that catalyze the oxidation of the toxic and mutagenic compound sulfite to sulfate, thereby protecting cells from adverse effects associated with sulfite exposure.
Louie eLow +3 more
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Cytosolic Fe-S cluster protein maturation and iron regulation are independent of the mitochondrial Erv1/Mia40 import system [PDF]
, 2015 The sulfhydryl oxidase Erv1 partners with the oxidoreductase Mia40 to import cysteine-rich proteins in the mitochondrial intermembrane space. In Saccharomyces cerevisiae, Erv1 has also been implicated in cytosolic Fe-S protein maturation and iron ...
Adrienne C. Dlouhy +65 more
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Fabrication of a Sulfite Biosensor by the Use of Conducting Polymer [PDF]
Iranian Journal of Chemistry & Chemical Engineering, 2008 In this research, an enzyme modified electrode has been produced during the electropolymerization of aniline through incorporation of sulfite oxidase into a conducting polymer.
Mohammad Hosseini +3 more
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Molybdenum‐Based Nanomaterials for Photothermal Cancer Therapy
Advanced NanoBiomed Research, 2022 Molybdenum (Mo) is a trace dietary element that is essential for human survival. Several molybdenum‐containing enzymes (e.g., aldehyde oxidase, xanthine oxidase and sulfite oxidase) are associated with key metabolic activities in the body.
Zhan Zhou +7 more
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Molecules, 2023 The mitochondrial amidoxime-reducing component (mARC) is the most recently discovered molybdoenzyme in humans after sulfite oxidase, xanthine oxidase and aldehyde oxidase. Here, the timeline of mARC’s discovery is briefly described. The story begins with
Bernd Clement, Michel A. Struwe
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Physiological function and catalytic versatility of bacterial multihaem cytochromescinvolved in nitrogen and sulfur cycling [PDF]
, 2011 Bacterial MCCs (multihaem cytochromes c) represent widespread respiratory electron-transfer proteins. In addition, some of them convert substrates such as nitrite, hydroxylamine, nitric oxide, hydrazine, sulfite, thiosulfate or hydrogen peroxide. In many
Arslan +54 more
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CoQ deficiency causes disruption of mitochondrial sulfide oxidation, a new pathomechanism associated with this syndrome [PDF]
, 2017 Coenzyme Q (CoQ) is a key component of the mitochondrial respiratory chain, but it also has several other functions in the cellular metabolism. One of them is to function as an electron carrier in the reaction catalyzed by sulfide:quinone oxidoreductase (
Barriocanal-Casado, Eliana +5 more
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Bringing Nitric Oxide to the Molybdenum World—A Personal Perspective
Molecules, 2023 Molybdenum-containing enzymes of the xanthine oxidase (XO) family are well known to catalyse oxygen atom transfer reactions, with the great majority of the characterised enzymes catalysing the insertion of an oxygen atom into the substrate. Although some
Luisa B. Maia
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