Results 271 to 280 of about 553,570 (305)

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
openaire   +1 more source

Chemical and electrochemical interrelationships of the 1-Fe, 2-Fe, and 4-Fe analogs of the active sites of iron-sulfur proteins

Inorganic Chemistry, 1977
Die ein-, zwei- und vier-kernigen Titelkomplexe (I) bis (IV) sind aus einfachen Eisensalzen zuganglich.
J. Cambray, R. W. Lane, A. G. Wedd, Richard W. Johnson, R. H. Holm   +4 more
openaire   +1 more source

The role of Fe–S proteins in sensing and regulation in bacteria

Current Opinion in Microbiology, 2003
Fe-S clusters are key to the sensing and transcription functions of three transcription factors, FNR, IscR and SoxR. All three proteins were discovered in Escherichia coli but experimental data and bioinformatic predictions suggest that homologs of these proteins exist in other bacterial species, highlighting the widespread nature of Fe-S-dependent ...
Patricia J, Kiley, Helmut, Beinert
openaire   +2 more sources

The Search for A “Prismane” Fe–S Protein

1999
Publisher 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
openaire   +1 more source

Evidence for one-electron transfer by the Fe protein of nitrogenase

Biochemical and Biophysical Research Communications, 1978
Abstract 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
openaire   +2 more sources

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
openaire   +2 more sources

Isolation by crystallization of the MoFe protein of Azotobacter nitrogenase

Biochemical and Biophysical Research Communications, 1970
Abstract Homogeneous MoFe 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 MoFe 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
openaire   +2 more sources

Variations on a theme of Fe-O-Fe proteins

Biochemical Society Transactions, 1994
P C, Wilkins, H, Dalton
openaire   +2 more sources

Fe-S Proteins

2021
openaire   +1 more source

On the path to [Fe-S] protein maturation: A personal perspective

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
Azotobacter 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 ...
openaire   +2 more sources