Calculation of the Redox Potentials of Iron-Sulfur Proteins: The 2-/3- Couple of [Fe4S4Cys4] Clusters in Peptococcus aerogenes Ferredoxin, Azotobacter vinelandii Ferredoxin I, and Chromatium vinosum High-Potential Iron Protein

Biochemistry ◽  
1994 ◽  
Vol 33 (36) ◽  
pp. 10911-10924 ◽  
Author(s):  
G. M. Jensen ◽  
A. Warshel ◽  
P. J. Stephens
Keyword(s):  
Azotobacter Vinelandii ◽  
High Potential ◽  
Chromatium Vinosum ◽  
Redox Potentials ◽  
Iron Protein ◽  
Iron Sulfur ◽  
Iron Sulfur Proteins ◽  
Ferredoxin I

Ab initio solution and refinement of two high-potential iron protein structures at atomic resolution

1999 ◽  
Vol 55 (11) ◽  
pp. 1773-1784 ◽  
Author(s):  
Emilio Parisini ◽  
Francesco Capozzi ◽  
Paolo Lubini ◽  
Victor Lamzin ◽  
Claudio Luchinat ◽  
...  
Keyword(s):  
Ab Initio ◽  
Protein Structures ◽  
Direct Methods ◽  
High Potential ◽  
Chromatium Vinosum ◽  
Atomic Resolution ◽  
Crystal Modification ◽  
Redox Potentials ◽  
Asymmetric Unit ◽  
Iron Protein

The crystal structure of the reduced high-potential iron protein (HiPIP) from Chromatium vinosum has been redetermined in a new orthorhombic crystal modification, and the structure of its H42Q mutant has been determined in orthorhombic (H42Q-1) and cubic (H42Q-2) modifications. The first two were solved by ab initio direct methods using data collected to atomic resolution (1.20 and 0.93 Å, respectively). The recombinant wild type (rc-WT) with two HiPIP molecules in the asymmetric unit has 1264 protein atoms and 335 solvent sites, and is the second largest structure reported so far that has been solved by pure direct methods. The solutions were obtained in a fully automated way and included more than 80% of the protein atoms. Restrained anisotropic refinement for rc-WT and H42Q-1 converged to R_1=\sum\big||F_o|-|F_c|\big|\big/\sum|F_o| of 12.0 and 13.6%, respectively [data with I>2\sigma(I)], and 12.8 and 15.5% (all data). H42Q-2 contains two molecules in the asymmetric unit and diffracted only to 2.6 Å. In both molecules of rc-WT and in the single unique molecule of H42Q-1 the [Fe4S4]2+ cluster dimensions are very similar and show a characteristic tetragonal distortion with four short Fe—S bonds along four approximately parallel cube edges, and eight long Fe—S bonds. The unique protein molecules in H42Q-2 and rc-WT are also very similar in other respects, except for the hydrogen bonding around the mutated residue that is at the surface of the protein, supporting the hypothesis that the difference in redox potentials at lower pH values is caused primarily by differences in the charge distribution near the surface of the protein rather than by structural differences in the cluster region.

Influence of Charge and Polarity on the Redox Potentials of High-Potential Iron-Sulfur Proteins: Evidence for the Existence of Two Groups

Biochemistry ◽  
1995 ◽  
Vol 34 (45) ◽  
pp. 14675-14686 ◽  
Author(s):  
H. A. Heering ◽  
Y. B. M. Bulsink ◽  
W. R. Hagen ◽  
T. E. Meyer
Keyword(s):  
High Potential ◽  
Redox Potentials ◽  
Iron Sulfur ◽  
Iron Sulfur Proteins

STERICALLY HINDERED FERREDOXIN COMPLEXES AS A MODEL OF HIGH POTENTIAL IRON-SULFUR PROTEINS

1984 ◽  
Vol 13 (8) ◽  
pp. 1287-1290 ◽  
Author(s):  
Norikazu Ueyama ◽  
Toshistugu Terakawa ◽  
Takashi Sugawara ◽  
Michiaki Fuji ◽  
Akira Nakamura
Keyword(s):  
High Potential ◽  
Iron Sulfur ◽  
Iron Sulfur Proteins ◽  
Sterically Hindered

Site-specific oxidation of the [Fe4S4] cubanes in high-potential iron sulfur proteins as probed by EPR and orientation-selective proton ENDOR spectroscopy:Ectothiorhodospira halophila I versusRhodocyclus tenuis

2007 ◽  
Vol 31 (3-4) ◽  
pp. 483-507
Author(s):  
R. Kappl ◽  
L. D. Eltis ◽  
M. B. Caspersen ◽  
H. E. M. Christensen ◽  
J. Hüttermann
Keyword(s):  
High Potential ◽  
Site Specific ◽  
Iron Sulfur ◽  
Iron Sulfur Proteins ◽  
Specific Oxidation

Polarographic studies of Chromatium vinosum high-potential iron protein

1991 ◽  
Vol 26 (1) ◽  
pp. 123-129 ◽  
Author(s):  
M. Borsari ◽  
M. Sola ◽  
J.A. Cowan
Keyword(s):  
High Potential ◽  
Chromatium Vinosum ◽  
Iron Protein
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