JBC Avanti Polar Lipids

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Jung, Y.-S.
Right arrow Articles by Burgess, B. K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Jung, Y.-S.
Right arrow Articles by Burgess, B. K.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

J Biol Chem, Vol. 274, Issue 5, 2978-2987, January 29, 1999

Complex Formation between Azotobacter vinelandii Ferredoxin I and Its Physiological Electron Donor NADPH-Ferredoxin Reductase

Yean-Sung JungDagger , Victoria A. Roberts§, C. David Stout§, and Barbara K. BurgessDagger

From the Dagger  Department of Molecular Biology and Biochemistry, University of California, Irvine, California 92697 and the § Department of Molecular Biology, The Scripps Research Institute, La Jolla, California 92037

In Azotobacter vinelandii, deletion of the fdxA gene, which encodes ferredoxin I (FdI), leads to activation of the expression of the fpr gene, which encodes NADPH-ferredoxin reductase (FPR). In order to investigate the relationship of these two proteins further, the interactions of the two purified proteins have been examined. AvFdI forms a specific 1:1 cross-linked complex with AvFPR through ionic interactions formed between the Lys residues of FPR and Asp/Glu residues of FdI. The Lys in FPR has been identified as Lys258, a residue that forms a salt bridge with one of the phosphate oxygens of FAD in the absence of FdI. UV-Vis and circular dichroism data show that on binding FdI, the spectrum of the FPR flavin is hyperchromatic and red-shifted, confirming the interaction region close to the FAD. Cytochrome c reductase assays and electron paramagnetic resonance data show that electron transfer between the two proteins is pH-dependent and that the [3Fe-4S]+ cluster of FdI is specifically reduced by NADPH via FPR, suggesting that the [3Fe-4S] cluster is near FAD in the complex. To further investigate the FPR:FdI interaction, the electrostatic potentials for each protein were calculated. Strongly negative regions around the [3Fe-4S] cluster of FdI are electrostatically complementary with a strongly positive region overlaying the FAD of FPR, centered on Lys258. These proposed interactions of FdI with FPR are consistent with cross-linking, peptide mapping, spectroscopic, and electron transfer data and strongly support the suggestion that the two proteins are physiological redox partners.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
S. S. Mansy, G. Wu, K. K. Surerus, and J. A. Cowan
Iron-Sulfur Cluster Biosynthesis. THERMATOGA MARITIMA IscU IS A STRUCTURED IRON-SULFUR CLUSTER ASSEMBLY PROTEIN
J. Biol. Chem., June 7, 2002; 277(24): 21397 - 21404.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
K.-S. Yoon, C. Bobst, C. F. Hemann, R. Hille, and F. R. Tabita
Spectroscopic and Functional Properties of Novel 2[4Fe-4S] Cluster-containing Ferredoxins from the Green Sulfur Bacterium Chlorobium tepidum
J. Biol. Chem., November 16, 2001; 276(47): 44027 - 44036.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
Y.-S. Jung, H. S. Gao-Sheridan, J. Christiansen, D. R. Dean, and B. K. Burgess
Purification and Biophysical Characterization of a New [2Fe-2S] Ferredoxin from Azotobacter vinelandii, a Putative [Fe-S] Cluster Assembly/Repair Protein
J. Biol. Chem., November 5, 1999; 274(45): 32402 - 32410.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
K. Regnstrom, S. Sauge-Merle, K. Chen, and B. K. Burgess
In Azotobacter vinelandii, the E1 subunit of the pyruvate dehydrogenase complex binds fpr promoter region DNA and ferredoxin I
PNAS, October 26, 1999; 96(22): 12389 - 12393.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
Y.-S. Jung, C. A. Bonagura, G. J. Tilley, H. S. Gao-Sheridan, F. A. Armstrong, C. D. Stout, and B. K. Burgess
Structure of C42D Azotobacter vinelandii FdI. A Cys-X-X-Asp-X-X-Cys MOTIF LIGATES AN AIR-STABLE [4Fe-4S]2+/+ CLUSTER
J. Biol. Chem., November 17, 2000; 275(47): 36974 - 36983.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 1999 by the American Society for Biochemistry and Molecular Biology.