Journal ArticleDOI
Iron-Sulfur Clusters: Nature's Modular, Multipurpose Structures
TLDR
Iron-sulfur clusters now rank with such biological prosthetic groups as hemes and flavins in pervasive occurrence and multiplicity of function.Abstract:
Iron-sulfur proteins are found in all life forms. Most frequently, they contain Fe2S2, Fe3S4, and Fe4S4 clusters. These modular clusters undergo oxidation-reduction reactions, may be inserted or removed from proteins, can influence protein structure by preferential side chain ligation, and can be interconverted. In addition to their electron transfer function, iron-sulfur clusters act as catalytic centers and sensors of iron and oxygen. Their most common oxidation states are paramagnetic and present significant challenges for understanding the magnetic properties of mixed valence systems. Iron-sulfur clusters now rank with such biological prosthetic groups as hemes and flavins in pervasive occurrence and multiplicity of function.read more
Citations
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Bacterial iron homeostasis
TL;DR: The expression of the iron homeostatic machinery is subject to iron-dependent global control ensuring that iron acquisition, storage and consumption are geared to iron availability and that intracellular levels of free iron do not reach toxic levels.
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Hydrogen Production by Molecular Photocatalysis
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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.
Journal ArticleDOI
Classification and phylogeny of hydrogenases.
TL;DR: Compelling evidence from sequences and structures indicates that the [NiFe]- and [Fe]-H2ases are phylogenetically distinct classes of proteins, which would be consistent with the phylogenetic distinctiveness of the two classes of H2ases.
References
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Interaction between the d -Shells in the Transition Metals. II. Ferromagnetic Compounds of Manganese with Perovskite Structure
TL;DR: In this paper, it was shown that both electrical conduction and ferromagnetic coupling in these compounds arise from a double exchange process, and a quantitative relation was developed between electrical conductivity and the Ferromagnetic Curie temperature.
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Structural and Functional Aspects of Metal Sites in Biology
TL;DR: The authors present here a classification and structure/function analysis of native metal sites based on these functions, and the coordination chemistry of metalloprotein sites and the unique properties of a protein as a ligand are briefly summarized.
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Crystal structure of the nickel–iron hydrogenase from Desulfovibrio gigas
TL;DR: The X-ray structure of the heterodimeric Ni–Fe hydrogenase from Desulfovibrio gigas, the enzyme responsible for the metabolism of molecular hydrogen, has been solved at 2.85 Å resolution and suggests plausible electron and proton transfer pathways.
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Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide, and oxidative stress
Matthias W. Hentze,Lukas C. Kühn +1 more
TL;DR: The discovery of two IRE-regulated mRNAs encoding enzymes of the mitochondrial citric acid cycle may represent the beginnings of elucidating regulatory coupling between iron and energy metabolism, and IRP-1 has highlighted an unexpected role for iron sulfur clusters as post-translational regulatory switches.
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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.