Related ArticlesSolution structure of the B form of oxidized rat microsomal cytochrome b5 and backbone dynamics via 15N rotating-frame NMR-relaxation measurements. Biological implications.
Eur J Biochem. 1999 Mar;260(2):347-54
Authors: Arnesano F, Banci L, Bertini I, Felli IC, Koulougliotis D
Cytochrome b5 in solution has two isomers (A and B) differing by a 180 degrees rotation of the protoporphyrin IX plane around the axis defined by the alpha and gamma meso protons. Homonuclear and heteronuclear NMR spectroscopy has been employed in order to solve the solution structure of the minor (B) form of the oxidized state of the protein and to probe its backbone dynamics in the microsecond--ms timescale in both oxidation states. A family of 40 conformers has been obtained using 1302 meaningful NOEs and 220 pseudocontact shifts and is characterized by high quality and good resolution (rmsd to the mean structure of 0.055 +/- 0.009 nm and 0.103 +/- 0.011 nm for backbone and heavy atoms, respectively). Extensive comparisons of the structural and dynamics changes associated with the A-to-B form interconversion for both oxidation states were subsequently performed. Propionate 6 experiences a redox-state-dependent reorientation as does propionate 7 in the A form. Significant insights are obtained into the role of the protein frame for efficient biological function and backbone mobility is proposed to be one of the factors that could control the reduction potential of the heme.
[NMR paper] NMR solution structure of the monomeric form of the bacteriophage lambda capsid stabi
NMR solution structure of the monomeric form of the bacteriophage lambda capsid stabilizing protein gpD.
Related Articles NMR solution structure of the monomeric form of the bacteriophage lambda capsid stabilizing protein gpD.
J Biomol NMR. 2005 Apr;31(4):351-6
Authors: Iwai H, Forrer P, Plückthun A, Güntert P
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[NMR paper] 800 MHz 1H NMR solution structure refinement of oxidized cytochrome c7 from Desulfuro
800 MHz 1H NMR solution structure refinement of oxidized cytochrome c7 from Desulfuromonas acetoxidans.
Related Articles 800 MHz 1H NMR solution structure refinement of oxidized cytochrome c7 from Desulfuromonas acetoxidans.
Eur J Biochem. 1998 Sep 1;256(2):261-70
Authors: Assfalg M, Banci L, Bertini I, Bruschi M, Turano P
The solution structure of Desulfuromonas acetoxidans cytochrome c7 has been refined by using 1H-NMR spectra recorded at 800 MHz and by using pseudocontact shifts in the final energy minimization procedure. The protein,...
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[NMR paper] Probing the backbone dynamics of oxidized and reduced rat microsomal cytochrome b5 vi
Probing the backbone dynamics of oxidized and reduced rat microsomal cytochrome b5 via 15N rotating frame NMR relaxation measurements: biological implications.
Related Articles Probing the backbone dynamics of oxidized and reduced rat microsomal cytochrome b5 via 15N rotating frame NMR relaxation measurements: biological implications.
Biochemistry. 1998 Sep 1;37(35):12320-30
Authors: Banci L, Bertini I, Cavazza C, Felli IC, Koulougliotis D
Rotating frame 15N relaxation NMR experiments have been performed to study the local mobility of the...
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[NMR paper] NMR solution structure of the oxidized form of MerP, a mercuric ion binding protein i
NMR solution structure of the oxidized form of MerP, a mercuric ion binding protein involved in bacterial mercuric ion resistance.
Related Articles NMR solution structure of the oxidized form of MerP, a mercuric ion binding protein involved in bacterial mercuric ion resistance.
Biochemistry. 1998 Jun 30;37(26):9316-22
Authors: Qian H, Sahlman L, Eriksson PO, Hambraeus C, Edlund U, Sethson I
Mercuric ions are toxic to living organisms because of their strong affinity for cysteine residues in proteins. Some bacteria have developed a resistance...
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NMR structure note: oxidized microsomal human cytochrome b5.
NMR structure note: oxidized microsomal human cytochrome b5.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles NMR structure note: oxidized microsomal human cytochrome b5.
J Biomol NMR. 2010 Aug;47(4):289-95
Authors: Nunez M, Guittet E, Pompon D, van Heijenoort C, Truan G
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[NMR paper] NMR characterization and solution structure determination of the oxidized cytochrome
NMR characterization and solution structure determination of the oxidized cytochrome c7 from Desulfuromonas acetoxidans.
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 NMR characterization and solution structure determination of the oxidized cytochrome c7 from Desulfuromonas acetoxidans.
Proc Natl Acad Sci U S A. 1996 Dec 10;93(25):14396-400
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[NMR paper] The identification of cation-binding domains on the surface of microsomal cytochrome
The identification of cation-binding domains on the surface of microsomal cytochrome b5 using 1H-NMR paramagnetic difference spectroscopy.
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 The identification of cation-binding domains on the surface of microsomal cytochrome b5 using 1H-NMR paramagnetic difference spectroscopy.
Eur J Biochem. 1992 Jan 15;203(1-2):211-23
Authors: Whitford D
One-dimensional and two-dimensional 1H-NMR...