Pulsed ENDOR and ESEEM spectroscopic evidence for unusual nitrogen coordination to the novel hydrogen-activating iron-sulfur center in hydrogenase

1991 ◽  
Vol 113 (18) ◽  
pp. 7044-7046 ◽  
Author(s):  
Hans Thomann ◽  
Marcelino Bernardo ◽  
Michael W. W. Adams
Keyword(s):  
The Novel ◽  
Spectroscopic Evidence ◽  
Iron Sulfur ◽  
Iron Sulfur Center

On the novel H2-activating iron-sulfur center of the “Fe-only” hydrogenases

Biochimie ◽  
1986 ◽  
Vol 68 (1) ◽  
pp. 35-42 ◽  
Author(s):  
Michael W.W. Adams ◽  
Michael K. Johnson ◽  
Isabel C. Zambrano ◽  
Leonard E. Mortenson
Keyword(s):  
The Novel ◽  
Iron Sulfur ◽  
Iron Sulfur Center

A Moessbauer analysis of the low-potential iron-sulfur center in photosystem I: spectroscopic evidence that FX is a iron-sulfur [4Fe-4S] cluster

Biochemistry ◽  
1989 ◽  
Vol 28 (23) ◽  
pp. 8980-8983 ◽  
Author(s):  
Vasili Petrouleas ◽  
Jerry J. Brand ◽  
Kevin G. Parrett ◽  
John H. Golbeck
Keyword(s):  
Photosystem I ◽  
Spectroscopic Evidence ◽  
Iron Sulfur ◽  
Iron Sulfur Center

Spectroscopic evidence for the presence of an iron-sulfur center similar to Fx of Photosystem I inHeliobacillus mobilis

1994 ◽  
Vol 41 (1) ◽  
pp. 115-123 ◽  
Author(s):  
Frank A. M. Kleinherenbrink ◽  
Hung-Cheng Chiou ◽  
Russell LoBrutto ◽  
Robert E. Blankenship
Keyword(s):  
Photosystem I ◽  
Spectroscopic Evidence ◽  
Iron Sulfur ◽  
Iron Sulfur Center

The role of an iron-sulfur center and siroheme in spinach nitrite reductase

1975 ◽  
Vol 169 (1) ◽  
pp. 102-107 ◽  
Author(s):  
Pedro J. Aparicio ◽  
David B. Knaff ◽  
Richard Malkin
Keyword(s):  
Nitrite Reductase ◽  
Iron Sulfur ◽  
Iron Sulfur Center

scholarly journals Atypical effect of temperature tuning on the insertion of the catalytic iron−sulfur center in a recombinant [FeFe]-hydrogenase

2015 ◽  
Vol 24 (12) ◽  
pp. 2090-2094 ◽  
Author(s):  
Simone Morra ◽  
Alessandro Cordara ◽  
Gianfranco Gilardi ◽  
Francesca Valetti
Keyword(s):  
Effect Of Temperature ◽  
Iron Sulfur ◽  
Iron Sulfur Center ◽  
Temperature Tuning

scholarly journals Transcription Activation at Escherichia coli FNR-Dependent Promoters by the Gonococcal FNR Protein: Effects of a Novel S18F Substitution and Comparisons with the Corresponding Substitution in E. coli FNR

2003 ◽  
Vol 185 (16) ◽  
pp. 4734-4747 ◽  
Author(s):  
Tim Overton ◽  
Eleanor G. F. Reid ◽  
Robin Foxall ◽  
Harry Smith ◽  
Stephen J. W. Busby ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Nitrate Reductase ◽  
Neisseria Gonorrhoeae ◽  
Transcription Activation ◽  
The Other ◽  
E Coli ◽  
Iron Sulfur ◽  
Fnr Protein ◽  
Iron Sulfur Center ◽  
After Error

ABSTRACT The Neisseria gonorrhoeae genome encodes a homologue of the Escherichia coli FNR protein (the fumarate and nitrate reductase regulator). Despite its similarity to E. coli FNR, the gonococcal FNR only partially complemented an E. coli fnr mutation. After error-prone PCR mutagenesis of the gonococcal fnr gene, we identified four mutant fnr derivatives carrying the same S18F substitution, and we showed that the mutant FNR could activate transcription from a range of class I and class II FNR-dependent promoters in E. coli. Prompted by the similarities between gonococcal and E. coli FNR, we made changes in gonococcal fnr that created substitutions that are equivalent to previously characterized substitutions in E. coli FNR. First, our experiments showed that cysteine, C116, in the gonococcal FNR, equivalent to C122 in E. coli FNR, is essential, presumably because, as in E. coli FNR, it binds to an iron-sulfur center. Second, the L22H and D148A substitutions in gonococcal FNR were made. These changes are equivalent to the L28H and D154A changes in E. coli FNR, which had been shown to increase FNR activity in the presence of oxygen. We show that the effects of these substitutions in gonococcal FNR are distinct from those of the S18F substitution. Similarly, substitutions in the putative activating regions of gonococcal FNR were made. We show that the activity of gonococcal FNR in E. coli can be increased by transplanting certain activating regions from E. coli FNR. The effects of these substitutions are additive to those due to S18F. From these data, we conclude that the effects of the S18F substitution in gonococcal FNR are distinct from the effects of the other substitutions. S18 is immediately adjacent to one of three N-terminal cysteine residues that coordinate the iron-sulfur center, and thus the S18F substitution is most likely to stabilize this center. Support for this came from complementary experiments in which we created the S24F substitution in E. coli FNR, which is equivalent to the S18F substitution in gonococcal FNR. Our results show that the S24F substitution changes the activity of E. coli FNR and that the changes are distinct from those due to previously characterized substitutions.

scholarly journals Isolation of the intact photosystem I reaction center core containing P700 and iron-sulfur center FX

FEBS Letters ◽  
1988 ◽  
Vol 228 (2) ◽  
pp. 268-272 ◽  
Author(s):  
John H. Golbeck ◽  
Kevin G. Parrett ◽  
Tetemke Mehari ◽  
Karen L. Jones ◽  
Jerry J. Brand
Keyword(s):  
Reaction Center ◽  
Photosystem I ◽  
Iron Sulfur ◽  
Iron Sulfur Center
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