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
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Biochemistry
DOI: 10.1021/acs.biochem.5b01273
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[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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Solution NMR Structure,Backbone Dynamics, and Heme-BindingProperties of a Novel Cytochrome c Maturation ProteinCcmE from Desulfovibrio vulgaris
Solution NMR Structure,Backbone Dynamics, and Heme-BindingProperties of a Novel Cytochrome c Maturation ProteinCcmE from Desulfovibrio vulgaris
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Biochemistry
DOI: 10.1021/bi300457b
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04-25-2012 05:25 AM
[NMR paper] Bis-methionine ligation to heme iron in mutants of cytochrome b562. 2. Characterizati
Bis-methionine ligation to heme iron in mutants of cytochrome b562. 2. Characterization by NMR of heme-ligand interactions.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Bis-methionine ligation to heme iron in mutants of cytochrome b562. 2. Characterization by NMR of heme-ligand interactions.
Biochemistry. 1996 Oct 22;35(42):13627-35
Authors: Barker PD, Freund SM
Previous work has shown that, in variants of cytochrome b562 containing the H102M mutation, methionine residues provide both...
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08-22-2010 02:20 PM
[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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[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...
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08-21-2010 11:16 PM
[NMR paper] Full assignment of heme redox potentials of cytochrome c3 of D. vulgaris Miyazaki F b
Full assignment of heme redox potentials of cytochrome c3 of D. vulgaris Miyazaki F by 1H-NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Full assignment of heme redox potentials of cytochrome c3 of D. vulgaris Miyazaki F by 1H-NMR.
FEBS Lett. 1991 Jul 8;285(1):149-51
Authors: Park JS, Kano K, Niki K, Akutsu H
Site-specific heme assignment of the 1H-NMR spectrum of cytochrome c3 of D. vulgaris Miyazaki F, a tetraheme protein, was established. The major reduction...
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08-21-2010 11:12 PM
[NMR paper] Full assignment of heme redox potentials of cytochrome c3 of D. vulgaris Miyazaki F b
Full assignment of heme redox potentials of cytochrome c3 of D. vulgaris Miyazaki F by 1H-NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Full assignment of heme redox potentials of cytochrome c3 of D. vulgaris Miyazaki F by 1H-NMR.
FEBS Lett. 1991 Jul 8;285(1):149-51
Authors: Park JS, Kano K, Niki K, Akutsu H
Site-specific heme assignment of the 1H-NMR spectrum of cytochrome c3 of D. vulgaris Miyazaki F, a tetraheme protein, was established. The major reduction...
Heme Trafficking and Modifications during System I Cytochrome c Biogenesis: Insights from Heme Redox Potentials of Ccm Proteins
Linear Mode
