The search of a putative physiological electron acceptor for thiocyanate dehydrogenase (TcDH) newly discovered in the thiocyanate-oxidizing bacteria Thioalkalivibrio paradoxus revealed an unusually large, single-heme cytochrome c (CytC552), which was co-purified with TcDH from the periplasm. Recombinant CytC552, produced in Escherichia coli as a mature protein without a signal peptide, has spectral properties similar to the endogenous protein and serves as an in vitro electron acceptor in the...
[NMR paper] (113) Cd NMR Experiments Reveal an Unusual Metal Cluster in the Solution Structure of the Yeast Splicing Protein Bud31p.
(113) Cd NMR Experiments Reveal an Unusual Metal Cluster in the Solution Structure of the Yeast Splicing Protein Bud31p.
(113) Cd NMR Experiments Reveal an Unusual Metal Cluster in the Solution Structure of the Yeast Splicing Protein Bud31p.
Angew Chem Int Ed Engl. 2015 Feb 20;
Authors: van Roon AM, Yang JC, Mathieu D, Bermel W, Nagai K, Neuhaus D
Abstract
Establishing the binding topology of structural zinc ions in proteins is an essential part of their structure determination by NMR spectroscopy. Using (113) Cd NMR experiments...
[NMR paper] Unusual structural features revealed by the solution NMR structure of the NLRC5 caspase recruitment domain.
Unusual structural features revealed by the solution NMR structure of the NLRC5 caspase recruitment domain.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Unusual structural features revealed by the solution NMR structure of the NLRC5 caspase recruitment domain.
Biochemistry. 2014 May 20;53(19):3106-17
Authors: Gutte PG, Jurt S, Grütter MG, Zerbe O
Abstract
The cytosolic nucleotide-binding domain and leucine-rich repeat-containing receptors (NLRs)...
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[NMR paper] Solution NMR study of the yeast cytochrome c peroxidase: cytochrome c interaction.
Solution NMR study of the yeast cytochrome c peroxidase: cytochrome c interaction.
Solution NMR study of the yeast cytochrome c peroxidase: cytochrome c interaction.
J Biomol NMR. 2013 May 25;
Authors: Volkov AN, van Nuland NA
Abstract
Here we present a solution NMR study of the complex between yeast cytochrome c (Cc) and cytochrome c peroxidase (CcP), a paradigm for understanding the biological electron transfer. Performed for the first time, the CcP-observed heteronuclear NMR experiments were used to probe the Cc binding in solution....
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[NMR paper] Interaction of the E2 and E3 components of the pyruvate dehydrogenase multienzyme com
Interaction of the E2 and E3 components of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus. Use of a truncated protein domain in NMR spectroscopy.
Related Articles Interaction of the E2 and E3 components of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus. Use of a truncated protein domain in NMR spectroscopy.
FEBS J. 2005 Jan;272(1):259-68
Authors: Allen MD, Broadhurst RW, Solomon RG, Perham RN
A (15)N-labelled peripheral-subunit binding domain (PSBD) of the dihydrolipoyl...
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[NMR paper] An NMR and circular dichroism study of the interaction of thiocyanate with human and
An NMR and circular dichroism study of the interaction of thiocyanate with human and cross-linked hemoglobin: identification of Lys-alpha-99 as a possible dissociation linked binding site.
Related Articles An NMR and circular dichroism study of the interaction of thiocyanate with human and cross-linked hemoglobin: identification of Lys-alpha-99 as a possible dissociation linked binding site.
Biophys Chem. 2003 Dec 1;106(3):233-40
Authors: Sau AK, Currell D, Mazumdar S, Mitra S
The interaction of thiocyanate with human native and cross-linked...
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[NMR paper] NMR solution structure of AlcR (1-60) provides insight in the unusual DNA binding pro
NMR solution structure of AlcR (1-60) provides insight in the unusual DNA binding properties of this zinc binuclear cluster protein.
Related Articles NMR solution structure of AlcR (1-60) provides insight in the unusual DNA binding properties of this zinc binuclear cluster protein.
J Mol Biol. 2000 Jan 28;295(4):729-36
Authors: Cerdan R, Cahuzac B, Félenbok B, Guittet E
The three-dimensional structure of the DNA-binding domain (residues 1-60) of the ethanol regulon transcription factor AlcR from Aspergillus nidulans has been solved by NMR....
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11-18-2010 09:15 PM
[NMR paper] C-NMR study on the interaction of medium-chain acyl-CoA dehydrogenase with acetoacety
C-NMR study on the interaction of medium-chain acyl-CoA dehydrogenase with acetoacetyl-CoA.
Related Articles C-NMR study on the interaction of medium-chain acyl-CoA dehydrogenase with acetoacetyl-CoA.
J Biochem. 1996 Mar;119(3):512-9
Authors: Miura R, Nishina Y, Fuji S, Shiga K
The change-transfer interaction in the complex of pig kidney medium-chain acyl-CoA dehydrogenase (MCAD) with acetoacetyl-CoA was investigated by 13C-NMR spectroscopy and molecular orbital treatment. The acyl carbons of acetoacetyl-CoA were separately 13C-labeled and...
Unusual Cytochrome c552 from Thioalkalivibrio paradoxus: Solution NMR Structure and Interaction with Thiocyanate Dehydrogenase
Linear Mode
