Related ArticlesRedox behaviour of the haem domain of flavocytochrome c3 from Shewanella frigidimarina probed by NMR.
FEBS Lett. 2004 Dec 3;578(1-2):185-90
Authors: Pessanha M, Rothery EL, Louro RO, Turner DL, Miles CS, Reid GA, Chapman SK, Xavier AV, Salgueiro CA
Flavocytochrome c3 from Shewanella frigidimarina (fcc3) is a tetrahaem periplasmic protein of 64 kDa with fumarate reductase activity. This work reports the first example of NMR techniques applied to the assignment of the thermodynamic order of oxidation of the four individual haems for such large protein, expanding its applicability to a wide range of proteins. NMR data from partially and fully oxidised samples of fcc3 and a mutated protein with an axial ligand of haem IV replaced by alanine were compared with calculated chemical shifts, allowing the structural assignment of the signals and the unequivocal determination of the order of oxidation of the haems. As oxidation progresses the fcc3 haem domain is polarised, with haems I and II much more oxidised than haems III and IV, haem IV being the most reduced. Thus, during catalysis as an electron is taken by the flavin adenosine dinucleotide from haem IV, haem III is eager to re-reduce haem IV, allowing the transfer of two electrons to the active site.
[NMR paper] Study of the behaviour of amino acids in aqueous solution by time-domain NMR and high
Study of the behaviour of amino acids in aqueous solution by time-domain NMR and high-resolution NMR.
Related Articles Study of the behaviour of amino acids in aqueous solution by time-domain NMR and high-resolution NMR.
Magn Reson Chem. 2005 Apr;43(4):309-15
Authors: Khallouk M, Rutledge DN, Silva AM, Delgadillo I
The study of protein hydration by time-domain NMR is complicated by the great number of interactions involved, resulting from the presence of several amino acids and the possible modifications produced by the various structures....
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[NMR paper] NMR structure of the haem core of a novel tetrahaem cytochrome isolated from Shewanel
NMR structure of the haem core of a novel tetrahaem cytochrome isolated from Shewanella frigidimarina: identification of the haem-specific axial ligands and order of oxidation.
Related Articles NMR structure of the haem core of a novel tetrahaem cytochrome isolated from Shewanella frigidimarina: identification of the haem-specific axial ligands and order of oxidation.
FEBS Lett. 2001 Jan 26;489(1):8-13
Authors: Pessanha M, Brennan L, Xavier AV, Cuthbertson PM, Reid GA, Chapman SK, Turner DL, Salgueiro CA
The tetrahaem cytochrome isolated...
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[NMR paper] Flavin-protein interactions in flavocytochrome b2 as studied by NMR after reconstitut
Flavin-protein interactions in flavocytochrome b2 as studied by NMR after reconstitution of the enzyme with 13C- and 15N-labelled flavin.
Related Articles Flavin-protein interactions in flavocytochrome b2 as studied by NMR after reconstitution of the enzyme with 13C- and 15N-labelled flavin.
Eur J Biochem. 2000 Aug;267(16):5156-67
Authors: Fleischmann G, Lederer F, Müller F, Bacher A, Rüterjans H
A new procedure was devised for reversibly removing the flavin from flavocytochrome b2. It allowed reconstitution with selectively enriched 13C- and...
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[NMR paper] Assessment by 1H NMR spectroscopy of the structural behaviour of human parathyroid-ho
Assessment by 1H NMR spectroscopy of the structural behaviour of human parathyroid-hormone-related protein(1-34) and its close relationship with the N-terminal fragments of human parathyroid hormone in solution.
Related Articles Assessment by 1H NMR spectroscopy of the structural behaviour of human parathyroid-hormone-related protein(1-34) and its close relationship with the N-terminal fragments of human parathyroid hormone in solution.
Biol Chem. 1997 Dec;378(12):1501-8
Authors: Gronwald W, Schomburg D, Tegge W, Wray V
Human...
[NMR paper] Characterization of the haem environment in Methylophilus methylotrophus ferricytochr
Characterization of the haem environment in Methylophilus methylotrophus ferricytochrome c" by 1H-NMR.
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 Characterization of the haem environment in Methylophilus methylotrophus ferricytochrome c" by 1H-NMR.
Eur J Biochem. 1993 Aug 1;215(3):817-24
Authors: Costa HS, Santos H, Turner DL
Two-dimensional NMR techniques have been used to assign proton resonances in the haem cavity of...
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[NMR paper] Revision of the haem-core architecture in the tetraheam cytochrome c3 from Desulfovib
Revision of the haem-core architecture in the tetraheam cytochrome c3 from Desulfovibrio baculatus by two-dimensional 1H NMR.
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 Revision of the haem-core architecture in the tetraheam cytochrome c3 from Desulfovibrio baculatus by two-dimensional 1H NMR.
Eur J Biochem. 1992 Oct 1;209(1):329-33
Authors: Coutinho IB, Turner DL, Legall J, Xavier AV
The haem-core architecture in cytochrome...
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[NMR paper] NMR studies of the C-terminal secretion signal of the haem-binding protein, HasA.
NMR studies of the C-terminal secretion signal of the haem-binding protein, HasA.
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 NMR studies of the C-terminal secretion signal of the haem-binding protein, HasA.
Eur J Biochem. 1999 Apr;261(2):562-8
Authors: Izadi-Pruneyre N, Wolff N, Redeker V, Wandersman C, Delepierre M, Lecroisey A
HasA is a haem-binding protein which is secreted under iron-deficiency conditions by the...
Redox behaviour of the haem domain of flavocytochrome c3 from Shewanella frigidimarin
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