Related ArticlesSome structural features of cluster-coordinating cysteines of Clostridium pasteurianum ferredoxin are revealed by 2D TOCSY 1H NMR on the oxidized protein.
Biochem Biophys Res Commun. 1994 Jul 15;202(1):591-5
Different sets of geminal J coupling constants for the eight beta-CH2 protons in the iron-coordinating cysteines in Clostridium pasteurianum ferredoxin were detected by 2D TOCSY 1H NMR experiments on the oxidized protein. Four resonances were characterized by quite similar high values of J, two more resonances had a J value about half of the former ones, while the last two had extremely low J values. These findings suggest that the cysteines required for cubane symmetry around the iron atoms are constrained into different geometries. The simplified model used for fine tuning of tau m in these TOCSY experiments is also presented and discussed.
Structural Features of Cytochromes P450 and Ligands that Affect Drug Metabolism as Re
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Structural Features of Cytochromes P450 and Ligands that Affect Drug Metabolism as Revealed by X-ray Crystallography and NMR.
Future Med Chem. 2010 Sep 1;2(9):1451-1468
Authors: Gay SC, Roberts AG, Halpert JR
Cytochromes P450 (P450s) play a major role in the clearance of drugs, toxins, and environmental pollutants. Additionally, metabolism by P450s can result in toxic or carcinogenic products. The metabolism of...
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[NMR paper] Exploration of the structural environment of the iron-sulfur cluster in putidaredoxin
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Biochem Biophys Res Commun. 1998 Aug 28;249(3):773-80
Authors: Sari N, Holden MJ, Mayhew MP, Vilker VL, Coxon B
Putidaredoxin is a di-iron protein whose paramagnetic region is not well characterized by 1H...
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[NMR paper] Structural features of the binding site for ribosomal protein S8 in Escherichia coli
Structural features of the binding site for ribosomal protein S8 in Escherichia coli 16S rRNA defined using NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-custom-pnas_full_free.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles Structural features of the binding site for ribosomal protein S8 in Escherichia coli 16S rRNA defined using NMR spectroscopy.
Proc Natl Acad Sci U S A. 1997 Mar 18;94(6):2139-44
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[NMR paper] Structural features of the epsilon subunit of the Escherichia coli ATP synthase deter
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Nat Struct Biol. 1995 Nov;2(11):961-7
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The tertiary fold of the epsilon subunit of the Escherichia coli F1F0 ATPsynthase (ECF1F0) has been determined by two- and three-dimensional heteronuclear (13C, 15N) NMR spectroscopy. The epsilon...
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[NMR paper] Proton NMR and structural features of a 24-nucleotide RNA hairpin.
Proton NMR and structural features of a 24-nucleotide RNA hairpin.
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The three-dimensional conformation of a 24-nucleotide variant of the RNA binding sequence for the coat protein of bacteriophage R17 has been analyzed using NMR, molecular dynamics, and energy minimization. The imino proton spectrum is consistent with base pairing...
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[NMR paper] Redox-dependent 1H NMR spectral features and tertiary structural constraints on the C
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Biochemistry. 1994 May 31;33(21):6433-41
Authors: Pochapsky TC, Ratnaswamy G, Patera A
Putidaredoxin (Pdx) is a 106-residue Fe2S2 ferredoxin which acts as the physiological reductant and effector of cytochrome P-450cam. Pdx has two accessible oxidation states, Fe+3-Fe+3 (oxidized) and...
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[NMR paper] Redox-dependent 1H NMR spectral features and tertiary structural constraints on the C
Redox-dependent 1H NMR spectral features and tertiary structural constraints on the C-terminal region of putidaredoxin.
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Biochemistry. 1994 May 31;33(21):6433-41
Authors: Pochapsky TC, Ratnaswamy G, Patera A
Putidaredoxin (Pdx) is a 106-residue Fe2S2 ferredoxin which acts as the physiological reductant and effector of cytochrome P-450cam. Pdx has two accessible oxidation states, Fe+3-Fe+3 (oxidized) and...
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[NMR paper] Structural features of the protoporphyrin-apomyoglobin complex: a proton NMR spectros
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Biochemistry. 1990 Dec 18;29(50):11057-67
Authors: Lecomte JT, Cocco MJ
The structural properties of the complex formed by apomyoglobin and protoporphyrin IX (des-iron myoglobin) were studied to probe the influence of iron-to-histidine coordination on the native myoglobin fold and the heme binding site geometry. Standard two-dimensional...
Some structural features of cluster-coordinating cysteines of Clostridium pasteurianu
Linear Mode
