[NMR paper] Tangled web of interactions among proteins involved in iron-sulfur cluster assembly as unraveled by NMR, SAXS, chemical crosslinking, and functional studies.
Tangled web of interactions among proteins involved in iron-sulfur cluster assembly as unraveled by NMR, SAXS, chemical crosslinking, and functional studies.
Tangled web of interactions among proteins involved in iron-sulfur cluster assembly as unraveled by NMR, SAXS, chemical crosslinking, and functional studies.
Biochim Biophys Acta. 2014 Nov 22;
Authors: Kim JH, Bothe JR, Reid Alderson T, Markley JL
Abstract
Proteins containing iron-sulfur (Fe-S) clusters arose early in evolution and are essential to life. Organisms have...
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12-03-2014 04:05 PM
Tangled web of interactions among proteins involved in iron-sulfur cluster assembly as unraveled by NMR, SAXS, chemical crosslinking, and functional studies
Tangled web of interactions among proteins involved in iron-sulfur cluster assembly as unraveled by NMR, SAXS, chemical crosslinking, and functional studies
Publication date: Available online 22 November 2014
Source:Biochimica et Biophysica Acta (BBA) - Molecular Cell Research</br>
Author(s): Jin Hae Kim , Jameson R. Bothe , T. Reid Alderson , John L. Markley</br>
Proteins containing iron-sulfur (Fe-S) clusters arose early in evolution and are essential to life. Organisms have evolved machinery consisting of specialized proteins that operate together to assemble...
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11-22-2014 01:48 PM
Solid-State NMR Study of the Charge-Transfer Complex between Ubiquinone-8 and Disulfide Bond Generating Membrane Protein DsbB.
Solid-State NMR Study of the Charge-Transfer Complex between Ubiquinone-8 and Disulfide Bond Generating Membrane Protein DsbB.
Solid-State NMR Study of the Charge-Transfer Complex between Ubiquinone-8 and Disulfide Bond Generating Membrane Protein DsbB.
J Am Chem Soc. 2011 Mar 4;
Authors: Tang M, Sperling LJ, Berthold DA, Nesbitt AE, Gennis RB, Rienstra CM
Ubiquinone (Coenzyme Q) plays an important role in the mitochondrial respiratory chain and also acts as an antioxidant in its reduced form, protecting cellular membranes from peroxidation....
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03-08-2011 01:40 PM
Solid-State NMR Study of the Charge-Transfer Complex between Ubiquinone-8 and Disulfide Bond Generating Membrane Protein DsbB
Solid-State NMR Study of the Charge-Transfer Complex between Ubiquinone-8 and Disulfide Bond Generating Membrane Protein DsbB
Ming Tang, Lindsay J. Sperling, Deborah A. Berthold, Anna E. Nesbitt, Robert B. Gennis and Chad M. Rienstra
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja107775w/aop/images/medium/ja-2010-07775w_0004.gif
Journal of the American Chemical Society
DOI: 10.1021/ja107775w
http://feeds.feedburner.com/~ff/acs/jacsat?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/jacsat/~4/WdFsSgH1V7w
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03-05-2011 02:44 AM
[NMR paper] Solution NMR structure of the iron-sulfur cluster assembly protein U (IscU) with zinc
Solution NMR structure of the iron-sulfur cluster assembly protein U (IscU) with zinc bound at the active site.
Related Articles Solution NMR structure of the iron-sulfur cluster assembly protein U (IscU) with zinc bound at the active site.
J Mol Biol. 2004 Nov 19;344(2):567-83
Authors: Ramelot TA, Cort JR, Goldsmith-Fischman S, Kornhaber GJ, Xiao R, Shastry R, Acton TB, Honig B, Montelione GT, Kennedy MA
IscU is a highly conserved protein that serves as the scaffold for IscS-mediated assembly of iron-sulfur () clusters. We report the NMR...
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11-24-2010 10:03 PM
[NMR paper] Exploration of the structural environment of the iron-sulfur cluster in putidaredoxin
Exploration of the structural environment of the iron-sulfur cluster in putidaredoxin by nitrogen-15 NMR spectroscopy of selectively labeled cysteine residues.
Related Articles Exploration of the structural environment of the iron-sulfur cluster in putidaredoxin by nitrogen-15 NMR spectroscopy of selectively labeled cysteine residues.
Biochem Biophys Res Commun. 1998 Aug 28;249(3):773-80
Authors: Sari N, Holden MJ, Mayhew MP, Vilker VL, Coxon B
Putidaredoxin is a di-iron protein whose paramagnetic region is not well characterized by 1H...
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11-17-2010 11:15 PM
[NMR paper] Proton NMR investigation of the [4Fe--4S]1+ cluster environment of nitrogenase iron p
Proton NMR investigation of the 1+ cluster environment of nitrogenase iron protein from Azotobacter vinelandii: defining nucleotide-induced conformational changes.
Related Articles Proton NMR investigation of the 1+ cluster environment of nitrogenase iron protein from Azotobacter vinelandii: defining nucleotide-induced conformational changes.
Biochemistry. 1995 Dec 5;34(48):15646-53
Authors: Lanzilotta WN, Holz RC, Seefeldt LC
This work presents the complete assignment of the isotropically shifted 1H NMR resonances of Azotobacter vinelandii...
Cluster-Dependent Charge-Transfer Dynamics in Iron–SulfurProteins
Linear Mode
