Results 221 to 230 of about 179,106 (262)

Methods for Heterologous Overproduction of Fe-S Proteins

2021
Proteins carrying iron-sulfur ([Fe-S]) clusters are critical to the basic metabolism of all organisms. Structural and biochemical investigations of many such [Fe-S] cluster proteins depend on recombinant overproduction using heterologous bacterial hosts such as Escherichia coli .
Elliot I, Corless, Edwin, Antony
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Functional Models of [Fe—S] Nitrosyl Proteins.

ChemInform, 2004
AbstractFor Abstract see ChemInform Abstract in Full Text.
N. A. Sanina, S. M. Aldoshin
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Fe-Fe separation may explain iron protein behavior

Chemical & Engineering News Archive, 2000
The unusually short distance between iron atoms recently discovered in a ferritin intermediate may explain why diiron centers behave so differently in various iron proteins [Science, 287, 122 (2000) ]. Such centers act as catalytic cofactors in oxygen-activating enzymes, for example, but as substrate intermediates in ferritin, the protein that stores ...
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Exchange-coupled Fe-X-Fe model compounds for certain iron proteins

Hyperfine Interactions, 1988
X-ray structure studies, Mossbauer experiments and magnetic susceptibility measurements were used in connection with molecular orbital calculations to monitor structurally induced changes of electronic and magnetic properties in exchangecoupled [Fe2S2 (SR)4]2- and [Fe2OCl6]2- anions.
J. Adler, J. Ensling, P. Gütlich, E. L. Bominaar, J. Guillin, A. X. Trautwein   +5 more
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Fe-Protein Fe:S Ligands

1984
We report functional roles for some Av2 (Azotobacter vinelandii Fe-protein) cysteinyl (Cys) residues using the chemical reactivity of the Cys with iodoacetic acid (IAA) as a probe, Cysteinyl residues were modified with [14C]-IAA under a variety of conditions. The percent carboxymethylation for each of the 7 residues (Cys-5, 38, 85, 97, 132, 151 and 184)
Robert P. Hausinger, James Bryant Howard
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X-ray absorption spectroscopy of 3-Fe clusters in FeS proteins

Inorganica Chimica Acta, 1983
Abstract Fe EXAFS and edge spectroscopy have been used to characterize the 3-Fe clusters in aconitase and Azotobacter vinelandii ferredoxin I (Av Fd I). Fe EXAFS of a frozen solution of oxidized (unactivated) beef heart aconitase indicates a ‘compact’ cluster structure with FeFe distances of ca.
R.A. Scott, S.A. Kazmi, H. Beinert, M.H. Emptage, J.E. Hahn, K.O. Hodgson, C.D. Stout, A.J. Thompson   +7 more
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The c-Fes Family of Protein-Tyrosine Kinases

Critical Reviews™ in Oncogenesis, 1998
The human c-fes protooncogene encodes a protein-tyrosine kinase (c-Fes) distinct from c-Src, c-Abl and other nonreceptor tyrosine kinases. Although originally identified as the cellular homolog of several transforming retroviral oncoproteins, Fes was later found to exhibit strong expression in myeloid hematopoietic cells and to play a direct role in ...
T E, Smithgall, J A, Rogers, K L, Peters, J, Li, S D, Briggs, J M, Lionberger, H, Cheng, A, Shibata, B, Scholtz, S, Schreiner, N, Dunham   +10 more
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Fe-S proteins in sensing and regulatory functions

Current Opinion in Chemical Biology, 1999
In the past five to ten years, it has become increasingly apparent that the function of Fe-S clusters is not limited to electron transfer, a function implicit in their discovery. We now know that the vulnerability of these structures to oxidative destruction is used by nature in sensing O2, iron, and possibly also nitric oxide. Changes in the oxidation
H, Beinert, P J, Kiley
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Directed Cleavage of RNA with Protein-Tethered EDTA–Fe

Methods, 1999
There 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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The Role of Fe Protein in Nitrogenase Catalysis

1985
The role of Fe protein in nitrogenase catalysis seems to be understood (Mortenson, Thorneley, 1979; Hageman, Burris, 1980). Fe protein con­tains a [4Fe-4S] cluster that functions as a one electron donor. Reduced Fe protein, MoFe protein and two MgATP rapidly form a ternary complex.
Haaker, H., Cordewener, J., ten Asbroek, A., Wassink, H., Eady, R.R., Veeger, C.   +5 more
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