Proton NMR spectroscopy and the electronic structure of the high potential iron-sulfur protein from Chromatium vinosum [Erratum to document cited in CA114(9):77229m]

1991 ◽  
Vol 113 (18) ◽  
pp. 7084-7084 ◽  
Author(s):  
Ivano Bertini ◽  
Fabrizio Briganti ◽  
Claudio Luchinat ◽  
Andrea Scozzafava ◽  
Marco Sola
Keyword(s):  
Electronic Structure ◽  
Nmr Spectroscopy ◽  
Proton Nmr ◽  
High Potential ◽  
Chromatium Vinosum ◽  
Proton Nmr Spectroscopy ◽  
Iron Sulfur ◽  
Sulfur Protein ◽  
Iron Sulfur Protein

The three-dimensional solution structure of the reduced high-potential iron-sulfur protein from Chromatium vinosum through NMR

Biochemistry ◽  
1995 ◽  
Vol 34 (1) ◽  
pp. 206-219 ◽  
Author(s):  
Lucia Banci ◽  
Ivano Bertini ◽  
Alexander Dikiy ◽  
Dieter H. W. Kastrau ◽  
Claudio Luchinat ◽  
...  
Keyword(s):  
Solution Structure ◽  
Three Dimensional ◽  
High Potential ◽  
Chromatium Vinosum ◽  
Dimensional Solution ◽  
Iron Sulfur ◽  
Sulfur Protein ◽  
Iron Sulfur Protein

Oxidation-reduction properties of Chromatium vinosum high potential iron-sulfur protein

Biochemistry ◽  
1976 ◽  
Vol 15 (2) ◽  
pp. 343-348 ◽  
Author(s):  
Isaac A. Mizrahi ◽  
Fern E. Wood ◽  
Michael A. Cusanovich
Keyword(s):  
High Potential ◽  
Chromatium Vinosum ◽  
Iron Sulfur ◽  
Oxidation Reduction ◽  
Sulfur Protein ◽  
Iron Sulfur Protein

The Electronic Structure of the Fe4S3+4Cluster in Proteins: The Importance of Double Exchange Parameter

1995 ◽  
Vol 50 (1) ◽  
pp. 75-80 ◽  
Author(s):  
Moshe Belinskii ◽  
Ivano Bertini ◽  
Oleg Galas ◽  
Claudio Luchinat
Keyword(s):  
Electronic Structure ◽  
Double Exchange ◽  
Exchange Parameter ◽  
High Potential ◽  
Iron Sulfur ◽  
Upper Limit ◽  
Sulfur Protein ◽  
Epr Parameters ◽  
Iron Sulfur Protein

The recently obtained Mössbauer and EPR parameters of the Fe4S43+ polymetallic center in the High Potential Iron-Sulfur Protein (HiPIP) II from E. halophila have been reproduced with models based on pure Heisenberg exchange. The role of double exchange versus ./-inequivalence is discussed. An evaluation of the upper limit of the double exchange parameter in the Fe4S43+ bimetallic center is also presented. The present calculations shed further light on the electronic structure of the Fe4S43+ center.

Sequential resonance assignments of oxidized high-potential iron-sulfur protein from Chromatium vinosum

Biochemistry ◽  
1992 ◽  
Vol 31 (4) ◽  
pp. 1234-1244 ◽  
Author(s):  
David G. Nettesheim ◽  
Scott R. Harder ◽  
Benjamin A. Feinberg ◽  
James D. Otvos
Keyword(s):  
Resonance Assignments ◽  
High Potential ◽  
Chromatium Vinosum ◽  
Iron Sulfur ◽  
Sulfur Protein ◽  
Iron Sulfur Protein
Sign in / Sign up

Export Citation Format

Share Document