Literature DB >> 9752001

Identification of slow motions in the reduced recombinant high-potential iron sulfur protein I (HiPIP I) from Ectothiorhodospira halophila via 15N rotating-frame NMR relaxation measurements.

L Banci1, I C Felli, D Koulougliotis.   

Abstract

Rotating-frame 15N relaxation rate (R1 rho) NMR experiments have been performed in order to study the dynamic behavior of the reduced recombinant high-potential iron-sulfur protein iso I (HiPIP I) from Ectothiorhodospira halophila, in the microsecond to ms time range. Measurements of R1 rho were performed as a function of the effective spinlock magnetic field amplitude by using both on and off-resonance radio frequency irradiation. The two data sets provided consistent results and were fit globally in order to identify possible exchange processes in an external loop of the reduced HiPIP I. The loop consists of residues 43-45 and the correlation time of the exchange process was determined to be 50 +/- 8 microseconds for the backbone nitrogen of Gln 44.

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Year:  1998        PMID： 9752001     DOI： 10.1023/a:1008232919515

Source DB:  PubMed          Journal:  J Biomol NMR        ISSN： 0925-2738            Impact factor:   2.835


  30 in total

1.  A complete relaxation matrix refinement of the solution structure of a paramagnetic metalloprotein: reduced HiPIP I from Ectothiorhodospira halophila.

Authors:  I Bertini; I C Felli; C Luchinat; A Rosato
Journal:  Proteins       Date:  1996-02

2.  Mössbauer spectroscopy of non-heme iron proteins.

Authors:  T H Moss; A J Bearden; R G Bartsch; M A Cusanovich; A San Pietro
Journal:  Biochemistry       Date:  1968-04       Impact factor: 3.162

3.  The three-dimensional structure in solution of the paramagnetic high-potential iron-sulfur protein I from Ectothiorhodospira halophila through nuclear magnetic resonance.

Authors:  L Banci; I Bertini; L D Eltis; I C Felli; D H Kastrau; C Luchinat; M Piccioli; R Pierattelli; M Smith
Journal:  Eur J Biochem       Date:  1994-10-15

4.  Purification of (4Fe-4S)1--2--ferredoxins (high-potential iron--sulfur proteins) from bacteria.

Authors:  R G Bartsch
Journal:  Methods Enzymol       Date:  1978       Impact factor: 1.600

5.  Pervasive conformational fluctuations on microsecond time scales in a fibronectin type III domain.

Authors:  M Akke; J Liu; J Cavanagh; H P Erickson; A G Palmer
Journal:  Nat Struct Biol       Date:  1998-01

6.  Protein dynamics studied by rotating frame 15N spin relaxation times.

Authors:  T Szyperski; P Luginbühl; G Otting; P Güntert; K Wüthrich
Journal:  J Biomol NMR       Date:  1993-03       Impact factor: 2.835

7.  The electronic structure of [Fe4S4]3+ clusters in proteins. An investigation of the oxidized high-potential iron-sulfur protein II from Ectothiorhodospira vacuolata.

Authors:  L Banci; I Bertini; S Ciurli; S Ferretti; C Luchinat; M Piccioli
Journal:  Biochemistry       Date:  1993-09-14       Impact factor: 3.162

8.  An investigation of Chromatium vinosum high-potential iron-sulfur protein by EPR and Mossbauer spectroscopy; evidence for a freezing-induced dimerization in NaCl solutions.

Authors:  W R Dunham; W R Hagen; J A Fee; R H Sands; J B Dunbar; C Humblet
Journal:  Biochim Biophys Acta       Date:  1991-09-20

9.  The molecular structure of the high potential iron-sulfur protein isolated from Ectothiorhodospira halophila determined at 2.5-A resolution.

Authors:  D R Breiter; T E Meyer; I Rayment; H M Holden
Journal:  J Biol Chem       Date:  1991-10-05       Impact factor: 5.157

10.  1H-NMR investigation of oxidized and reduced high-potential iron-sulfur protein from Rhodopseudomonas globiformis.

Authors:  I Bertini; F Capozzi; C Luchinat; M Piccioli
Journal:  Eur J Biochem       Date:  1993-02-15
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  3 in total

1.  Microsecond time scale dynamics in the RXR DNA-binding domain from a combination of spin-echo and off-resonance rotating frame relaxation measurements.

Authors:  F A Mulder; P J van Tilborg; R Kaptein; R Boelens
Journal:  J Biomol NMR       Date:  1999-03       Impact factor: 2.835

2.  NMR exchange broadening arising from specific low affinity protein self-association: analysis of nitrogen-15 nuclear relaxation for rat CD2 domain 1.

Authors:  M Pfuhl; H A Chen; S M Kristensen; P C Driscoll
Journal:  J Biomol NMR       Date:  1999-08       Impact factor: 2.835

3.  NMR studies of the dynamics of high-spin nitrophorins: comparative studies of NP4 and NP2 at close to physiological pH.

Authors:  Robert E Berry; Dhanasekaran Muthu; Fei Yang; F Ann Walker
Journal:  Biochemistry       Date:  2014-12-24       Impact factor: 3.162
  3 in total

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