Resonance Raman spectra of three-iron centers in ferredoxins from Desulfovibrio gigas.

Johnson, Michael K.; Hare, Jeffrey W.; Spiro, Thomas G.; Moura, José J. G.; Xavier, António V.; LeGall, Jean

doi:10.1016/s0021-9258(19)68696-5

Cited by 31 publications

(1 citation statement)

References 17 publications

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“…The three bands at 288, 339, and 391 cm -1 are characteristic of [2Fe-2S] 2+ ferredoxins (). It is important to note that the spectrum displays a relatively strong band at 288 cm -1 , which is diagnostic of ferredoxins harboring a [2Fe-2S] 2+ cluster, but it is absent in ferredoxins containing [3Fe-3S] or [4Fe-4S] clusters ( − ). In addition, the assignments of vibrational frequencies in the RR spectrum of pa -Bfd (Table ) compare very well with vibrational frequencies from previously characterized [2Fe-2S] 2+ ferredoxins ( − ) and synthetic analogue complexes ().…”

Section: Resultsmentioning

confidence: 99%

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^,

et al. 2007

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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).

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Section: Resultsmentioning

confidence: 99%

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^,

et al. 2007

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Ferredoxins Containing One [3Fe–4S] Cluster.Desulfovibrio GigasFerredoxinII– Solution Structure

Moura

Macedo

Goodfellow

et al. 2004

Handbook of Metalloproteins

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Ferredoxins Containing One [3Fe–4S] Cluster.Desulfovibrio GigasFerredoxinII– Solution Structure

Moura¹,

Macedo²,

Goodfellow³

et al. 2004

Encyclopedia of Inorganic and Bioinorganic Chemistry

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Functional Class Occurrence Biological Function Amino Acid Sequence Information Protein Production, Purification and Molecular Characterization Metal Content and Cluster Type Spectroscopy NMR Solution Structure of Native D . Gigas Fd II Functional Aspects Structural Cluster Interconversions: Synthesis of Heterometal Clusters Acknowledgements Related Articles

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Resonance Raman spectra of three-iron centers in ferredoxins from Desulfovibrio gigas.

Cited by 31 publications

References 17 publications

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^,

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^,

Ferredoxins Containing One [3Fe–4S] Cluster.Desulfovibrio GigasFerredoxinII– Solution Structure

Ferredoxins Containing One [3Fe–4S] Cluster.Desulfovibrio GigasFerredoxinII– Solution Structure

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Resonance Raman spectra of three-iron centers in ferredoxins from Desulfovibrio gigas.

Cited by 31 publications

References 17 publications

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,

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,

Ferredoxins Containing One [3Fe–4S] Cluster.Desulfovibrio GigasFerredoxinII– Solution Structure

Ferredoxins Containing One [3Fe–4S] Cluster.Desulfovibrio GigasFerredoxinII– Solution Structure

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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^,

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^,