Related ArticlesThe 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 extent of heme ruffling and to provide insights into the effect of ruffling on the electronic structure. Through the use of mutants of each of these cytochromes that differ in the amount of heme ruffling, NMR characterization of the low-spin (S = (1)/2) ferric proteins has confirmed and refined the developing understanding of how ruffling influences the spin distribution on heme. The chemical shifts of the core heme carbons were obtained through site-specific labeling of the heme via biosynthetic incorporation of (13)C-labeled 5-aminolevulinic acid derivatives. Analysis of the contact shifts of these core heme carbons allowed Fermi contact spin densities to be estimated and changes upon ruffling to be evaluated. The results allow a deconvolution of the contributions to heme hyperfine shifts and a test of the influence of heme ruffling on the electronic structure and hyperfine shifts. The data indicate that as heme ruffling increases, the spin densities on the ?-pyrrole carbons decrease while the spin densities on the ?-pyrrole carbons and meso carbons increase. Furthermore, increased ruffling is associated with stronger bonding to the heme axial His ligand.
PMID: 24187968 [PubMed - as supplied by publisher]
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] Electron Spin Density on the Axial His Ligand of High-Spin and Low-Spin Nitrophorin 2 Probed by Heteronuclear NMR Spectroscopy.
Electron Spin Density on the Axial His Ligand of High-Spin and Low-Spin Nitrophorin 2 Probed by Heteronuclear NMR Spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Electron Spin Density on the Axial His Ligand of High-Spin and Low-Spin Nitrophorin 2 Probed by Heteronuclear NMR Spectroscopy.
Inorg Chem. 2013 Jan 17;
Authors: Abriata LA, Zaballa ME, Berry RE, Yang F, Zhang H, Walker FA, Vila AJ
Abstract
The electronic structure of heme proteins is exquisitely tuned...
[CNS Yahoo group] HEME topology file
HEME topology file
Hi I am refining structure that needs HEME toplogy files. I am using the CNS programme. Please let me know if anybody having the HEME topology file in their
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09-16-2011 10:02 PM
Influence of substrate modification and C-terminal truncation on the active site structure of substrate-bound heme oxygenase from Neisseriae meningitidis; A 1H NMR study.
Influence of substrate modification and C-terminal truncation on the active site structure of substrate-bound heme oxygenase from Neisseriae meningitidis; A 1H NMR study.
Influence of substrate modification and C-terminal truncation on the active site structure of substrate-bound heme oxygenase from Neisseriae meningitidis; A 1H NMR study.
Biochemistry. 2011 Aug 27;
Authors: Peng D, Satterlee JD, Ma LH, Dallas JL, Smith KM, Zhang X, Sato M, La Mar GN
Abstract
Heme oxygenase, HO, from the pathogenic bacterium N. meningitidis, NmHO, which...
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08-30-2011 04:52 PM
[NMR paper] 1H NMR structure of the heme pocket of HNO-myoglobin.
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J Biol Inorg Chem. 2003 Feb;8(3):348-52
Authors: Sulc F, Fleischer E, Farmer PJ, Ma D, La Mar GN
The unique (1)H NMR signal of nitrosyl hydride at 14.8 ppm is used to obtain a solution structure of the distal pocket of Mb-HNO, a rare nitroxyl adduct with a half-life of several months at room temperature. (1)H NMR, NOESY and TOCSY data were obtained under identical experimental conditions on solutions of the diamagnetic...
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11-24-2010 08:58 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.
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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...
The Influence of Heme Ruffling on Spin Densities in Ferricytochromes c Probed by Heme Core (13)C NMR.
Linear Mode
