Biosynthesis of Nitrogenase FeMoco
Yilin Hu,Markus W. Ribbe +1 more
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TLDR
A brief account of the recent progress toward understanding the assembly process of FeMoco is given, which has identified some important missing pieces of this biosynthetic puzzle.About:
This article is published in Coordination Chemistry Reviews.The article was published on 2011-05-01 and is currently open access. It has received 71 citations till now. The article focuses on the topics: FeMoco.read more
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Mechanism of Nitrogen Fixation by Nitrogenase: The Next Stage
TL;DR: This paper presents a meta-analyses of the chiral stationary phase replacement of Na6(CO3)(SO4)2, Na2SO4, and Na2CO3 of the H2O/O2 mixture and shows clear patterns in the response of these two types of molecules to each other in a stationary phase.
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Distribution of nitrogen fixation and nitrogenase-like sequences amongst microbial genomes
TL;DR: A new criterion for computational prediction of nitrogen fixation is proposed: the presence of a minimum set of six genes coding for structural and biosynthetic components, namely NifHDK and NifENB.
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Ligand binding to the FeMo-cofactor: Structures of CO-bound and reactivated nitrogenase
Thomas Spatzal,Kathryn A Perez,Oliver Einsle,James B. Howard,James B. Howard,Douglas C. Rees +5 more
TL;DR: A crystal structure of carbon monoxide–inhibited nitrogenase molybdenum-iron (MoFe)–protein at 1.50 angstrom resolution is reported, which reveals a CO molecule bridging Fe2 and Fe6 of the FeMo-cofactor, which provides insights into a catalytically competent state of nitrogenase.
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Developments in the Biomimetic Chemistry of Cubane-Type and Higher Nuclearity Iron–Sulfur Clusters
TL;DR: This article focuses on polynuclear analogues, specifically higher nuclearity, biomimetic metal-sulfur clusters, which contain σ/π-donor ligands that induce smaller d-orbital splittings favoring individual metal sites with high-spin configurations, magnetic interactions among these individual sites, paramagnetic molecular ground states, and labile ligand binding.
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Cell biology of molybdenum in plants and humans.
Ralf R. Mendel,Tobias Kruse +1 more
TL;DR: The transition element molybdenum needs to be complexed by a special cofactor in order to gain catalytic activity, and in different variants is the active compound at the catalytic site of all other Mo-containing enzymes.
References
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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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Structural Basis of Biological Nitrogen Fixation.
James B. Howard,Douglas C. Rees +1 more
TL;DR: An overview of the nitrogenase system is presented in this article that emphasizes the structural organization of the proteins and associated metalloclusters that have the remarkable ability to catalyse nitrogen fixation under ambient conditions.
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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.
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Molybdenum cofactors, enzymes and pathways
TL;DR: 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.