Posttranslational Modification of Heme b in a Bacterial Peroxidase: The Role of Heme to Protein Ester Bondsin Ligand Binding and Catalysis
Posttranslational Modification of Heme b in a Bacterial Peroxidase: The Role of Heme to Protein Ester Bondsin Ligand Binding and Catalysis
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b00632/20170815/images/medium/bi-2017-00632n_0009.gif
Biochemistry
DOI: 10.1021/acs.biochem.7b00632
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08-17-2017 12:56 AM
The Iron Chaperone Protein CyaY from Vibriocholerae Is a Heme-Binding Protein
The Iron Chaperone Protein CyaY from Vibriocholerae Is a Heme-Binding Protein
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b01304/20170428/images/medium/bi-2016-01304c_0009.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b01304
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04-29-2017 04:33 AM
Heme Trafficking and Modifications during System I Cytochrome c Biogenesis: Insights from Heme Redox Potentials of Ccm Proteins
Heme Trafficking and Modifications during System I Cytochrome c Biogenesis: Insights from Heme Redox Potentials of Ccm Proteins
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.6b00427/20160525/images/medium/bi-2016-00427z_0005.gif
Biochemistry
DOI: 10.1021/acs.biochem.6b00427
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nmrlearner
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05-27-2016 04:11 AM
Cytoplasmic Heme-Binding Protein (HutX) from Vibrio cholerae Is an Intracellular Heme Transport Proteinfor the Heme-Degrading Enzyme, HutZ
Cytoplasmic Heme-Binding Protein (HutX) from Vibrio cholerae Is an Intracellular Heme Transport Proteinfor the Heme-Degrading Enzyme, HutZ
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.5b01273/20160203/images/medium/bi-2015-01273d_0009.gif
Biochemistry
DOI: 10.1021/acs.biochem.5b01273
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02-04-2016 11:46 AM
[NMR paper] The Influence of Heme Ruffling on Spin Densities in Ferricytochromes c Probed by Heme Core (13)C NMR.
The Influence of Heme Ruffling on Spin Densities in Ferricytochromes c Probed by Heme Core (13)C NMR.
Related Articles The Influence of Heme Ruffling on Spin Densities in Ferricytochromes c Probed by Heme Core (13)C NMR.
Inorg Chem. 2013 Nov 4;
Authors: Kleingardner JG, Bowman SE, Bren KL
Abstract
The heme in cytochromes c undergoes a conserved out-of-plane distortion known as ruffling. For cytochromes c from the bacteria Hydrogenobacter thermophilus and Pseudomonas aeruginosa , NMR and EPR spectra have been shown to be sensitive to the...
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11-06-2013 10:20 PM
Expression, Purification, and Solid-State NMR Characterization of the Membrane Binding Heme Protein Nitrophorin 7 in Two Electronic Spin States
Expression, Purification, and Solid-State NMR Characterization of the Membrane Binding Heme Protein Nitrophorin 7 in Two Electronic Spin States
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/bi401020t/aop/images/medium/bi-2013-01020t_0007.gif
Biochemistry
DOI: 10.1021/bi401020t
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09-27-2013 03:28 AM
[NMR paper] Expression, Purification and Solid-state NMR Characterization of the Membrane Binding Heme Protein Nitrophorin 7 in two Electronic Spin States.
Expression, Purification and Solid-state NMR Characterization of the Membrane Binding Heme Protein Nitrophorin 7 in two Electronic Spin States.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Expression, Purification and Solid-state NMR Characterization of the Membrane Binding Heme Protein Nitrophorin 7 in two Electronic Spin States.
Biochemistry. 2013 Sep 13;
Authors: Varghese S, Yang F, Pacheco V, Wrede K, Medvedev A, Ogata H, Knipp M, Heise H
Abstract
The...
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09-17-2013 11:36 PM
[NMR paper] 1H NMR study of the role of heme carboxylate side chains in modulating heme pocket st
1H NMR study of the role of heme carboxylate side chains in modulating heme pocket structure and the mechanism of reconstitution of cytochrome b5.
Related Articles 1H NMR study of the role of heme carboxylate side chains in modulating heme pocket structure and the mechanism of reconstitution of cytochrome b5.
Biochemistry. 1991 Feb 19;30(7):1878-87
Authors: Lee KB, La Mar GN, Pandey RK, Rezzano IN, Mansfield KE, Smith KM
1H nuclear magnetic resonance spectroscopy was used to assign the hyperfine-shifted resonances and determine the position of...