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Iron–Sulfur Proteins

2010
Iron–sulfur proteins are proteins in which non-haem iron is coordinated with cysteine sulfur and usually also with inorganic sulfur. They are divided into three major categories: redoxins; “simple iron–sulfur proteins”, containing only iron– sulfur clusters; and “complex iron–sulfur proteins”, containing additional active redox centres such as flavin ...
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Biosynthesis of Iron-Sulfur Structures in Iron-Sulfur Proteins

1979
Iron sulfur proteins are comparatively newcomers on the biochemical scene since active interest in them has developed in the last twenty years and definite information on the structure of representative types has been gained only in this decade. The development of recent research in the field is reflected in the volumes edited by Lovenberg (1).
P. Cerletti, F. Bonomi, S. Pagani
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Iron–sulfur proteins in health and disease

Trends in Endocrinology & Metabolism, 2010
Iron-sulfur (Fe/S) proteins are a class of ubiquitous components that assist in vital and diverse biochemical tasks in virtually every living cell. These tasks include respiration, iron homeostasis and gene expression. The past decade has led to the discovery of novel Fe/S proteins and insights into how their Fe/S cofactors are formed and incorporated ...
Sheftel, A., Stehling, O., Lill, R.
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Protein Film Electrochemistry of Iron–Sulfur Enzymes

2018
A suite of dynamic electrochemical techniques known as protein film electrochemistry (PFE) offers important insight into the roles of active sites in enzymes, including properties of electron-transfer centers (individually or collectively), rates and dependences of catalytic electron transport, and binding and dissociation of inhibitors.
Armstrong, F, Evans, R, Megarity, C
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The Iron-Sulfur Proteins

1980
The field of iron-sulfur proteins, the proteins containing iron complexed with sulfhydryl residues and in most cases with inorganic sulfur, can trace its beginnings to the 1950s. In fact, amazement has been expressed at the lateness of recognition of these ubiquitous components of various electron transport systems with microorganisms, plants, and ...
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Dithiol-iron-sulfur and selenium complexes: A comparison with iron sulfur proteins

Bioinorganic Chemistry, 1975
1, 4-Butanedithiol and dithiothreitol-iron complexes exhibited similar optical absorption spectra to those of rubredoxins. The spectra of butanedithio-iron-sulfur complex showed similarity to those of two iron and two labile sulfur while dithiothreitol-iron-sulfur complex resembled those of eight iron and eight labile sulfur ferredoxins.
Yukio Sugiura   +3 more
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Endonuclease III is an iron-sulfur protein

Biochemistry, 1989
Elemental analyses, Mössbauer, and EPR data are reported to show that endonuclease III of Escherichia coli is an iron-sulfur protein. Mössbauer spectra of protein freshly prepared from E. coli grown on 57Fe-enriched medium demonstrate that the native enzyme contains a single 4Fe-4S cluster in the 2+ oxidation state, with a net spin of zero.
R P, Cunningham   +9 more
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1 Iron—Sulfur Proteins

1975
Publisher Summary This chapter discusses iron-sulfur proteins. Iron proteins are divided into three groups. If the iron atom is coordinated to a porphyrin, the protein is called a “hemoprotein,” irrespective of the chemistry of the axial ligands. If the iron is coordinated to sulfur from either cysteine or from inorganic sulfur, then the protein is ...
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IRON-SULFUR PROTEINS

2001
D. BENTROP   +2 more
  +5 more sources

Electrochemistry of iron-sulfur proteins

1997
Iron-sulfur proteins and enzymes are unique because they possess one or more iron-sulfur clusters. They are ubiquitous in nature, playing key roles in photosynthesis, nitrogen fixation, and terminal respiration, not to mention a host of other biologically important reactions including CO oxidation to CO2, interconversion of H2 and H+, and sulfite ...
Benjamin A. Feinberg, Michael D. Ryan
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