Journal ArticleDOI
Molybdenum cofactors, enzymes and pathways
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TLDR
The biosynthetic pathways leading to both types of cofactor have common mechanistic aspects relating to scaffold formation, metal activation and cofactor insertion into apoenzymes, and have served as an evolutionary 'toolbox' to mediate additional cellular functions in eukaryotic metabolism.Abstract:
The trace element molybdenum is essential for nearly all organisms and forms the catalytic centre of a large variety of enzymes such as nitrogenase, nitrate reductases, sulphite oxidase and xanthine oxidoreductases. Nature has developed two scaffolds holding molybdenum in place, the iron-molybdenum cofactor and pterin-based molybdenum cofactors. Despite the different structures and functions of molybdenum-dependent enzymes, there are important similarities, which we highlight here. The biosynthetic pathways leading to both types of cofactor have common mechanistic aspects relating to scaffold formation, metal activation and cofactor insertion into apoenzymes, and have served as an evolutionary 'toolbox' to mediate additional cellular functions in eukaryotic metabolism.read more
Citations
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Catalytic conversion of nitrogen to ammonia by an iron model complex
TL;DR: Results indicate that a single iron site may be capable of stabilizing the various NxHy intermediates generated during catalytic NH3 formation, and propose that the interstitial carbon atom recently assigned in the nitrogenase cofactor may have a similar role, perhaps by enabling a singleIron site to mediate the enzymatic catalysis through a flexible iron–carbon interaction.
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Radical S-Adenosylmethionine Enzymes
TL;DR: This Review will begin by summarizing unifying features of radical SAM enzymes, and in subsequent sections delve further into the biochemical, spectroscopic, structural, and mechanistic details for those enzymes that catalyze an amazingly diverse set of reactions.
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Photocatalytic fixation of nitrogen to ammonia: state-of-the-art advancements and future prospects
TL;DR: In this paper, the state-of-the-art engineering of efficient photocatalysts for dinitrogen (N2) fixation toward NH3 synthesis is reviewed and the challenges, outlooks and future prospects at the forefront of this research platform are presented.
Journal ArticleDOI
The essential metals for humans: a brief overview
Maria Antonietta Zoroddu,Jan Aaseth,Guido Crisponi,Serenella Medici,Massimiliano Francesco Peana,Valeria Marina Nurchi +5 more
TL;DR: The human body needs about 20 essential elements in order to function properly and among them, for certain, 10 are metal elements, though for every metal we do need, there is another one in our body we could do without it as discussed by the authors.
Journal ArticleDOI
Proterozoic ocean redox and biogeochemical stasis
Christopher T. Reinhard,Noah J. Planavsky,Leslie J. Robbins,Camille A. Partin,Benjamin C. Gill,Stefan V. Lalonde,Andrey Bekker,Kurt O. Konhauser,Timothy W. Lyons +8 more
TL;DR: This model suggests that the oceanic Mo reservoir is extremely sensitive to perturbations in the extent of sulfidic seafloor and that the record of Mo and chromium enrichments through time is consistent with the possibility of a Mo–N colimited marine biosphere during many periods of Earth’s history.
References
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Book
The Metabolic and Molecular Bases of Inherited Disease
TL;DR: In this paper, the authors present a list of disorders of MITOCHONDRIAL FUNCTION, including the following: DISORDERS OF MIOCHONDRIC FERTILITY XIX, XVI, XIX.
Journal ArticleDOI
Structure, function, and formation of biological iron-sulfur clusters
TL;DR: Iron-sulfur [Fe-S] clusters are ubiquitous and evolutionary ancient prosthetic groups that are required to sustain fundamental life processes and important mechanistic questions related to the biosynthetic process involve the molecular details of how these clusters are assembled on scaffold proteins, how they are transferred from scaffolds to target proteins, and how the biosynthesis process is regulated.
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Nitrogenase MoFe-protein at 1.16 A resolution: a central ligand in the FeMo-cofactor.
Oliver Einsle,Oliver Einsle,F. Akif Tezcan,Susana L. A. Andrade,Susana L. A. Andrade,Benedikt Schmid,Mika Yoshida,Mika Yoshida,James B. Howard,Douglas C. Rees,Douglas C. Rees +10 more
TL;DR: A high-resolution crystallographic analysis of the nitrogenase MoFe-protein reveals a previously unrecognized ligand coordinated to six iron atoms in the center of the catalytically essential FeMo-cofactor, consistent with this newly detected component being a light element, most plausibly nitrogen.
Journal ArticleDOI
Structure and function of xanthine oxidoreductase: where are we now?
TL;DR: Of special interest has been the finding that XOR can catalyze the reduction of nitrates and nitrites to nitric oxide (NO), acting as a source of both NO and peroxynitrite.