Results 21 to 30 of about 1,904,807 (242)

Mechanism of Iron–Sulfur Cluster Assembly: In the Intimacy of Iron and Sulfur Encounter

Inorganics, 2020
Iron–sulfur (Fe–S) clusters are protein cofactors of a multitude of enzymes performing essential biological functions. Specialized multi-protein machineries present in all types of organisms support their biosynthesis.
Batoul Srour, Sylvain Gervason, Beata Monfort, Benoit D’Autréaux   +3 more
doaj   +1 more source

Structural Basis of RICs Iron Donation for Iron-Sulfur Cluster Biogenesis

Frontiers in Microbiology, 2021
Escherichia coli YtfE is a di-iron protein of the widespread Repair of Iron Centers proteins (RIC) family that has the capacity to donate iron, which is a crucial component of the biogenesis of the ubiquitous family of iron-sulfur proteins.
Liliana S. O. Silva, Pedro M. Matias, Pedro M. Matias, Célia V. Romão, Lígia M. Saraiva   +4 more
doaj   +1 more source

Structural organization of essential iron-sulfur clusters in the evolutionarily highly conserved ATP-binding cassette protein ABCE1 [PDF]

, 2007
The ABC protein ABCE1, formerly named RNase L inhibitor RLI1, is one of the most conserved proteins in evolution and is expressed in all organisms except eubacteria.
Dinkelaker, Stephanie, Meyer-Klaucke, Wolfram, Dinkelaker, Stephanie,, Janoschka, Adam,, Albers, Sonja-Verena,, Tampe, Robert, Bill, Eckhard, MacMillan, Fraser,, Scheele, U., Meyer-Klaucke, Wolfram,, Driessen, A.rnold J. M., Verena Albers, S., Albers, Sonja-Verena, Stagni, Marco Salamone, Schunemann, Volker, Bill, Eckhard,, Barthelme, Dominik, Schunemann, V., Tampe, R., Scheele, Urte, Macmillan, Fraser, Barthelme, D., Driessen, Arnold J.M.,, Albers, Sonja-Vernea, Scheele, Urte,, Schünemann, Volker,, Tampé, Robert,, Driessen, Arnold J. M., Bill, E., Salamone-Stagni, Marco, MacMillan, F., Driessen, A. J. M., Albers, Sonja Verena, Janoschka, Adam, Meyer-Klaucke, W., Salamone Stagni, Marco,, Salomone Stagni, M., Dinkeleker, S., Barthelme, Dominik,, Schuenemann, Volker, Janoschka, A.   +40 more
core   +2 more sources

The Iron Maiden. Cytosolic Aconitase/IRP1 Conformational Transition in the Regulation of Ferritin Translation and Iron Hemostasis

Biomolecules, 2021
Maintaining iron homeostasis is fundamental for almost all living beings, and its deregulation correlates with severe and debilitating pathologies.
Cécilia Hognon, Emmanuelle Bignon, Guillaume Harle, Nadège Touche, Stéphanie Grandemange, Antonio Monari   +5 more
doaj   +1 more source

Iron-induced changes in the proteome of Trichomonas vaginalis hydrogenosomes. [PDF]

PLoS ONE, 2013
Iron plays a crucial role in metabolism as a key component of catalytic and redox cofactors, such as heme or iron-sulfur clusters in enzymes and electron-transporting or regulatory proteins.
Neritza Campo Beltrán, Lenka Horváthová, Petr L Jedelský, Miroslava Sedinová, Petr Rada, Michaela Marcinčiková, Ivan Hrdý, Jan Tachezy   +7 more
doaj   +1 more source

Erythropoiesis and Iron Sulfur Cluster Biogenesis

Advances in Hematology, 2010
Erythropoiesis in animals is a synchronized process of erythroid cell differentiation that depends on successful acquisition of iron. Heme synthesis depends on iron through its dependence on iron sulfur (Fe-S) cluster biogenesis.
Hong Ye, Tracey A. Rouault
doaj   +1 more source

The Molecular Bases of the Dual Regulation of Bacterial Iron Sulfur Cluster Biogenesis by CyaY and IscX

Frontiers in Molecular Biosciences, 2018
IscX (or YfhJ) is a protein of unknown function which takes part in the iron-sulfur cluster assembly machinery, a highly specialized and essential metabolic pathway. IscX binds to iron with low affinity and interacts with IscS, the desulfurase central to
Salvatore Adinolfi, Rita Puglisi, Jason C. Crack, Clara Iannuzzi, Clara Iannuzzi, Fabrizio Dal Piaz, Petr V. Konarev, Petr V. Konarev, Dmitri I. Svergun, Stephen Martin, Nick E. Le Brun, Annalisa Pastore, Annalisa Pastore   +12 more
doaj   +1 more source

Escherichia coli RIC is able to donate iron to iron-sulfur clusters. [PDF]

PLoS ONE, 2014
Escherichia coli RIC (Repair of Iron Centers) is a diiron protein previously reported to be involved in the repair of iron-sulfur proteins damaged by oxidative or nitrosative stresses, and proposed to act as an iron donor.
Lígia S Nobre, Ricardo Garcia-Serres, Smilja Todorovic, Peter Hildebrandt, Miguel Teixeira, Jean-Marc Latour, Lígia M Saraiva   +6 more
doaj   +1 more source

The respiratory arsenite oxidase: structure and the role of residues surrounding the Rieske cluster [PDF]

, 2013
The arsenite oxidase (Aio) from the facultative autotrophic Alphaproteobacterium Rhizobium sp. NT-26 is a bioenergetic enzyme involved in the oxidation of arsenite to arsenate.
Muse Oke (452182), Nicole Bruselat (452184), Oke Muse, Konstantinos Thalassinos (452186), Joanne M Santini, Warelow, TP, Santini, JM, Leimkühler, Silke (Prof. Dr.), Thalassinos Konstantinos, Dahl Jan U., James H. Naismith (198956), Bruselat, Nicole, Kappler, U, Sivalingam Ganesh N., Kappler, Ulrike, Dahl, JU, Muse Oke, Barbara Schoepp-Cothenet (95047), Santini, Joanne M., Barbara Schoepp-Cothenet, Ganesh N Sivalingam, Thomas P. Warelow (452181), Ganesh N. Sivalingam (452185), Bruselat Nicole, Oke, M, James H Naismith, Leimkuehler, Silke, Thalassinos, K, Jan U Dahl, Oke, Muse, Schoepp-Cothenet, B, Thomas P Warelow, Silke Leimkühler (126058), Naismith James H., Dahl, Jan U., Konstantinos Thalassinos, Sivalingam, Ganesh N., Jan U. Dahl (452183), Kappler Ulrike, Leimkühler, S, Ulrike Kappler, Naismith, JH, Santini Joanne M., Nicole Bruselat, Silke Leimkühler, Warelow, Thomas P., Ulrike Kappler (129280), Warelow Thomas P., Sivalingam, GN, Schoepp-Cothenet, Barbara, Naismith, James H., Joanne M. Santini (452187), Thalassinos, Konstantinos, Bruselat, N, Leimkühler, Silke, Schoepp-Cothenet Barbara, Leimkühler Silke   +56 more
core   +1 more source

The effect of orientated electric fields on biologically relevant iron-sulfur clusters: Tuning redox reactivity for catalysis [PDF]

, 2021
Enzyme-based iron-sulfur clusters, exemplified in families such as hydrogenases, nitrogenases and radical S-adenosylmethionine enzymes, feature in many essential biological processes.
Anna, Croft, Jonathan, Hirst, Christof, Jaeger, Samuel, Gaughan   +3 more
core   +2 more sources