Results 291 to 300 of about 186,109 (312)
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Evidence for one-electron transfer by the Fe protein of nitrogenase
Biochemical and Biophysical Research Communications, 1978Abstract The number of electrons transferred per molecule of the Fe protein of nitrogenase from Clostridium pasteurianum was determined. The Fe protein was enzymically oxidized in the presence of MgATP and a small amount of MoFe protein, and dithionite was introduced to reduce part of the Fe protein.
T, Ljones, R H, Burris
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The Search for A “Prismane” Fe–S Protein
1999Publisher Summary Iron–sulfur (Fe–S) clusters are found throughout nature. They usually function in electron transfer reactions and are found in small molecules, such as the ferredoxins and in redox enzymes, where they shuttle electrons to or from the active site.
Alexander F. Arendsen, Peter F. Lindley
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Directed Cleavage of RNA with Protein-Tethered EDTA–Fe
Methods, 1999There are several methods for locating the RNA site where a protein binds. One of the less common methods is directed cleavage of the RNA by an EDTA-Fe reagent tethered to the protein. The reaction of the EDTA-Fe(III) with ascorbate or hydrogen peroxide produces reactive oxygen species, such as hydroxyl radicals, localized within a 10-A radius of the ...
K B, Hall, R O, Fox
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Isolation by crystallization of the MoFe protein of Azotobacter nitrogenase
Biochemical and Biophysical Research Communications, 1970Abstract Homogeneous MoFe protein of A. vinelandii nitrogenase was isolated in high yields as white needle-like crystals by decreasing the ionic strength of a solution rich in the MoFe protein and free of the Fe protein of nitrogenase. Molecular weight of the di-molybdo crystallized protein is 270,000–300,000; approximate ratios of Mo:Fe:CySH:
R C, Burns, R D, Holsten, R W, Hardy
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Variations on a theme of Fe-O-Fe proteins
Biochemical Society Transactions, 1994P C, Wilkins, H, Dalton
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On the path to [Fe-S] protein maturation: A personal perspective
Biochimica et Biophysica Acta (BBA) - Molecular Cell ResearchAzotobacter vinelandii is a genetically tractable Gram-negative proteobacterium able to fix nitrogen (N2) under aerobic growth conditions. This narrative describes how biochemical-genetic approaches using A. vinelandii to study nitrogen fixation led to the formulation of the "scaffold hypothesis" for the assembly of both simple and complex [Fe-S ...
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Mechanisms, regulation and functions of the unfolded protein response
Nature Reviews Molecular Cell Biology, 2020Claudio Hetz +2 more
exaly
Electrons in Fe-S protein assembly
Nature Chemical Biology, 2010Patricia C Dos Santos, Dennis R Dean
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