Publication date: July 2017 Source:Journal of Magnetic Resonance, Volume 280
Author(s): Sabine Van Doorslaer
Heme proteins are versatile proteins that are involved in a large number of biological processes. Many spectroscopic methods are used to gain insight into the different mechanistic processes governing heme-protein functions. Since many (intermediate) states of heme proteins are paramagnetic, electron paramagnetic resonance (EPR) methods, such as hyperfine spectroscopy, offer unique tools for these investigations. This perspective gives an overview of the use of state-of-the-art hyperfine spectroscopy in heme research, focusing on the advantages, limits and challenges of the different techniques. Graphical abstract
14 Spectroscopic NMR Characterizations of HNO Adducts of Ferrous Heme Proteins
14 Spectroscopic NMR Characterizations of HNO Adducts of Ferrous Heme Proteins
Publication date: 2017
Source:The Chemistry and Biology of Nitroxyl (HNO)</br>
Author(s): M.R. Kumar, P.J. Farmer</br>
HNO reacts with the ferrous states of many heme proteins such as myoglobin and hemoglobin to form stable HNO-Fe(II) adducts. Like the analogous O2 adducts, the HNO adducts are diamagnetic, but with a characteristic HNO resonance in 1H NMR c.15ppm that splits into doublets for H15NO adducts. As an illustration, we discuss HNO adducts of several heme-pocket mutants of...
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05-10-2017 06:52 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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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
Understanding NMR Spectroscopy
Understanding NMR Spectroscopy
http://www.spectroscopynow.com/common/images/thumbnails/sepspec10366education.jpgJames Keeler, Editor-in-Chief of Magnetic Resonance in Chemistry, discusses the high-resolution NMR of liquid samples, concentratring exclusively on spin-half nuclei (mainly 1H and 13C). It is aimed at people who are familiar with the use of routine NMR for structure determination and who wish to deepen their understanding of just exactly how NMR experiments work.
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02-03-2013 09:28 AM
Understanding NMR Spectroscopy
Understanding NMR Spectroscopy
http://www.spectroscopynow.com/common/images/thumbnails/no_img.gifFeatured here are the lecture notes given by Professor James Keeler of the University of Cambridge during his visit to the University of California, Irvine, in 2002.
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02-03-2013 09:28 AM
[NMR paper] 1H-NMR study of reduced heme proteins myoglobin and cytochrome P450.
1H-NMR study of reduced heme proteins myoglobin and cytochrome P450.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif Related Articles 1H-NMR study of reduced heme proteins myoglobin and cytochrome P450.
Eur J Biochem. 1993 Jul 15;215(2):431-7
Authors: Banci L, Bertini I, Marconi S, Pierattelli R
The 1H-NMR spectra of deoxymyoglobin and reduced cytochrome P450 are analyzed by NOE spectroscopy. Progress has been made in the assignment of the...
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08-22-2010 03:01 AM
[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...