Results 111 to 120 of about 54,320 (150)
Some of the next articles are maybe not open access.
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
openaire +3 more sources
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
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
openaire +2 more sources
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
openaire +2 more sources
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
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
openaire +1 more source
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
openaire +1 more source
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
openaire +2 more sources
Human ferrochelatase is an iron-sulfur protein
Biochemistry, 1994Recombinant human ferrochelatase has been expressed in Escherichia coli and purified to homogeneity. Metal analyses revealed approximately 2 mol of non-heme Fe per mol of the purified enzyme (M(r) = 40,000). The UV-visible absorption spectrum of the purified enzyme consists of a protein absorption at 278 nm (epsilon approximately 90,000 M-1 cm-1) and ...
H A, Dailey, M G, Finnegan, M K, Johnson
openaire +2 more sources
Biogenesis of iron–sulfur proteins in plants
Trends in Plant Science, 2005Iron-sulfur (Fe-S) clusters are ubiquitous prosthetic groups required to sustain fundamental life processes. The assembly of Fe-S clusters and insertion into polypeptides in vivo has recently become an area of intense research. Many of the genes involved are conserved in bacteria, fungi, animals and plants. Plant cells can carry out both photosynthesis
Balk, Janneke, Lobréaux, Stéphane
openaire +4 more sources
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
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