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| - | [[Image:2qdx.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_2qdx| PDB=2qdx | SCENE= }} | | {{STRUCTURE_2qdx| PDB=2qdx | SCENE= }} |
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| - | '''P.Aeruginosa Fpr with FAD'''
| + | ===P.Aeruginosa Fpr with FAD=== |
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| - | ==Overview==
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| - | Among the 118 genes upregulated by Pseudomonas aeruginosa in response to iron starvation [Ochsner, U. A., Wilderman, P. J., Vasil, A. I., and Vasil, M. L. (2002) Mol. Microbiol. 45, 1277-1287], we focused on the products of the two genes encoding electron transfer proteins, as a means of identifying the redox partners of the heme oxygenase (pa-HO) expressed under low-iron stress conditions. Biochemical and spectroscopic investigations demonstrated that the bfd gene encodes a 73-amino acid protein (pa-Bfd) that incorporates a [2Fe-2S]2+/+ center, whereas the fpr gene encodes a 258-residue NADPH-dependent ferredoxin reductase (pa-FPR) that utilizes FAD as a cofactor. In vitro reconstitution of pa-HO catalytic activity with the newly characterized proteins led to the surprising observation that pa-FPR efficiently supports the catalytic cycle of pa-HO, without the need of a ferredoxin. In comparison, electron transfer from pa-Bfd to pa-HO is sluggish, which strongly argues against the possibility that the seven electrons needed by pa-HO to degrade biliverdin are transferred from NADPH to pa-HO in a ferredoxin (Bfd)-dependent manner. Given that pa-HO functions to release iron from exogenous heme acquired under iron-starvation conditions, the use of a flavoenzyme rather than an iron-sulfur center-containing protein to support heme degradation is an efficient use of resources in the cell. The crystal structure of pa-FPR (1.6 A resolution) showed that its fold is comparable that of the superfamily of ferredoxin reductases and most similar to the structure of Azotobacter vinelandii FPR and Escherichia coli flavodoxin reductase. The latter two enzymes interact with distinct redox partners, a ferredoxin and a flavodoxin, respectively. Hence, findings reported herein extend the range of redox partners recognized by the fold of pa-FPR to include a heme oxygenase (pa-HO).
| + | The line below this paragraph, {{ABSTRACT_PUBMED_17915950}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 17915950 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_17915950}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Schonbrunn, E.]] | | [[Category: Schonbrunn, E.]] |
| | [[Category: Oxidoreductase]] | | [[Category: Oxidoreductase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 14:47:32 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 12:46:02 2008'' |
Revision as of 09:46, 27 July 2008
Template:STRUCTURE 2qdx
P.Aeruginosa Fpr with FAD
Template:ABSTRACT PUBMED 17915950
About this Structure
2QDX is a Single protein structure of sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.
Reference
Biochemical and structural characterization of Pseudomonas aeruginosa Bfd and FPR: ferredoxin NADP+ reductase and not ferredoxin is the redox partner of heme oxygenase under iron-starvation conditions., Wang A, Zeng Y, Han H, Weeratunga S, Morgan BN, Moenne-Loccoz P, Schonbrunn E, Rivera M, Biochemistry. 2007 Oct 30;46(43):12198-211. Epub 2007 Oct 4. PMID:17915950
Page seeded by OCA on Sun Jul 27 12:46:02 2008
