Results 201 to 210 of about 112,766 (248)
Some of the next articles are maybe not open access.
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 ...
openaire +1 more source
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 ...
openaire +1 more source
Biosynthesis of Iron-Sulfur Structures in Iron-Sulfur Proteins
1979Iron 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
openaire +1 more source
Iron–sulfur proteins in health and disease
Trends in Endocrinology & Metabolism, 2010Iron-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.
openaire +3 more sources
Protein Film Electrochemistry of Iron–Sulfur Enzymes
2018A 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
openaire +3 more sources
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 ...
openaire +1 more source
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 ...
openaire +1 more source
Dithiol-iron-sulfur and selenium complexes: A comparison with iron sulfur proteins
Bioinorganic Chemistry, 19751, 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
openaire +1 more source
Endonuclease III is an iron-sulfur protein
Biochemistry, 1989Elemental 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
openaire +2 more sources
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 ...
openaire +1 more source
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 ...
openaire +1 more source
Electrochemistry of iron-sulfur proteins
1997Iron-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
openaire +1 more source

