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Iron–sulfur protein folds, iron–sulfur chemistry, and evolution
JBIC Journal of Biological Inorganic Chemistry, 2007An inventory of unique local protein folds around Fe-S clusters has been derived from the analysis of protein structure databases. Nearly 50 such folds have been identified, and over 90% of them harbor low-potential [2Fe-2S](2+,+) or [4Fe-4S](2+,+) clusters. In contrast, high-potential Fe-S clusters, notwithstanding their structural diversity, occur in
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Chemical & Engineering News Archive, 2000
Adecade ago, bioinorganic chemists thought they had pretty much figured out what the iron-sulfur clusters found in many proteins were there for. The prevailing wisdom was that these proteins had one basic function in biology—to move electrons around, says Michael K. Johnson, chemistry professor at the University of Georgia, Athens. Biological processes
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Adecade ago, bioinorganic chemists thought they had pretty much figured out what the iron-sulfur clusters found in many proteins were there for. The prevailing wisdom was that these proteins had one basic function in biology—to move electrons around, says Michael K. Johnson, chemistry professor at the University of Georgia, Athens. Biological processes
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2007
The sections in this article are 1 Introduction 2 NMR and Hyperfine Coupling in Various FeS Proteins 3 Structural Information on the Diamagnetic Part 4 Biographical Sketches Related ...
BERTINI, IVANO, LUCHINAT, CLAUDIO
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The sections in this article are 1 Introduction 2 NMR and Hyperfine Coupling in Various FeS Proteins 3 Structural Information on the Diamagnetic Part 4 Biographical Sketches Related ...
BERTINI, IVANO, LUCHINAT, CLAUDIO
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Folding properties of iron—sulfur proteins
Inorganica Chimica Acta, 1998Abstract The 1 H NMR spectra in water of HiPIP I from Ectothiorhodospira halophila , the Cys77Ser mutant of the HiPIP from Chromatium vinosum , the 7Fe8S ferredoxin from Bacillus schlegelii , the 8Fe8S ferredoxin from Clostridium pasteurianum and the 2Fe2S ferredoxin from P.
BERTINI, IVANO +3 more
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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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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
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
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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.
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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
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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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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, 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
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