Rubredoxin from Desulfovibrio gigas

Frey, Michel; Sieker, L.C.; Payan, F.; Haser, R.; Bruschi, Mireille; Pèpe, Gérard; LeGall, Jean

doi:10.1016/0022-2836(87)90562-6

Cited by 110 publications

(45 citation statements)

References 52 publications

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“…An assessment can be made for single tryptophan containing iron-sulfur proteins. The crystal structures of M. elsdenii rubredoxin and spinach ferredoxin are not known but from a solvent-surface image of the crystal structures of the closely related Desulfovibrio gigas Nbredoxin [21] and Spirulina platensis ferredoxin (which contains Tyr in position 75 instead of tryptophan in spinach ferredoxin [22]) it is seen that the tryptophan (or tyrosine) residue and the iron-sulfur clusters are fully exposed to the solvent. The short component in the correlation time distribution of the studied proteins can be ascribed to rapid internal flexibility of the tryptophan residue.…”

Section: Discussionmentioning

confidence: 99%

A comparative picosecond‐resolved fluorescence study of tryptophan residues in iron‐sulfur proteins

et al. 1994

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The fluorescence intensity and anisotropy decays of the intrinsic tryptophan emission from six Fe/S proteins (ranging from the very simplest ones to enzyme complexes containing one, two or more Trp residues) were measured. All proteins were examined in the reduced and the oxidized state. In either redox state each protein exhibits ultrarapid tryptophan fluorescence decay on the picosecond timescale contributing up to 93% of the total decay. Correlation times in the range of 1 ns or less were found for all six iron-sulfur proteins reflecting internal Trp motion. In addition, some proteins exhibit longer correlation times reflecting segmental motion and overall protein tumbling. The ultrarapid fluorescence decay in iron-sulfur proteins indicates efficient radiationless energy transfer between distant tryptophan residues and iron-sulfur clusters. Such an energy transfer mechanism can be accounted for by referring to the three-dimensional structures of rubredoxin and ferredoxin in calculating the transfer efficiency of the single tryptophan-iron-sulfur couple.

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Section: Discussionmentioning

confidence: 99%

A comparative picosecond‐resolved fluorescence study of tryptophan residues in iron‐sulfur proteins

et al. 1994

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“…These figures suggest that the prismane protein may contain, besides the six irons in the [6Fe-6S] prismane cluster, one or possibly two additional irons. EPR data show no evidence for redox-active FeS4 centers (as found in rubredoxins [35], desulforedoxin [36], rubrerythrin [37]) or for [2Fe-2S] clusters. Additional iron(s) might be ligated to the prismane core as proposed for the two Mo atoms in a capped prismane model compound [Fe6Ss(C1)61Mo(C0)3}2]3 ~ [38].…”

Section: Overproduction Of Prismane Protein In D Vulgaris (Pjsp104) mentioning

confidence: 99%

Overproduction of prismane protein in Desulfovibrio vulgaris (Hildenborough): evidence for a second S= 1/2‐spin system in the one‐electron reduced state

Stokkermans

Houba

Pierik

et al. 1992

European Journal of Biochemistry

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The gene encoding the prismane protein from Desulfovibrio vulgaris (Hildenborough) was inserted into broad-host-range vector pSUP104. The recombinant plasmid, pJSP104, was transferred to D. vulgaris by conjugal plasmid transfer. In the transconjugant D. vulgaris cells the prismane protein was 25-fold overproduced. The overproduced prismane protein was characterized by molecular mass, isoelectric point, iron content and spectroscopical properties. Both the iron content and the ultraviolet/ visible spectrum are identical to the wild-type protein indicating that iron incorporation in the overproduced protein is complete. EPR spectra of the dithionite-reduced form of the overproduced protein indicated that the Fe-S cluster might occur in a similar structure as found in inorganic model compounds containing a [6Fe-6S] prismane core. The as-isolated overproduced protein showed the presence of a second S = 1/2 spin system that was also detected in the corresponding prismane protein from D . desuljiuricans (ATCC 27774), but not in the protein from wild-type D . vulgaris. This additional signal was irreversibly transformed to the 'wild-type' high-spin and low-spin systems upon two reduction/re-oxidation cycles. It is shown that the EPR spectroscopy of the overproduced prismane protein is very similar to that of the D. desulfuricans enzyme and, with the exception of the second S = 1/2 spin system, to that of the prismane protein from wild-type D. vulgaris. Contrary to claims for the D. desulfuricans protein, it is shown here that all data can be fully explained assuming a single [6Fe-6S] cluster, that might be titrated into four different redox states and occurs in up to three different spin systems in the one-electron reduced state.The prismane protein from Desulfovibrio vulgaris (Hildenborough) was the first example of a protein in which a Fe-S cluster with S = 9/2 paramagnetism was discovered [l -31. Since then, high-spin ('superspin') Fe-S clusters with spin systems S > 512 have been described in a number of enzymes: dissimilatory sulfite reductase from D . vulgaris (Hildenborough) [4], CO dehydrogenase from Methanothrix soehngenii [5, 61 and the nitrogenase MoFe protein (the Pclusters in this protein) from Azotobacter vinelandii [7, 81. However, these latter enzymes all contain large numbers of iron atoms (20-30), arranged in multiple, different, clusters. This makes a study of the redox properties and the spectroscopic analysis of the high-spin clusters in these proteins rather complicated. The prismane protcin, on the other hand, was shown to contain only six irons and six acid-labile sulfide ions! molecule [9]. Therefore, this protein was used as a relatively simple model protein for the study of these high-spin Fe-S clusters, although its function is as yet unknown [lo] In the 5+ state, the cluster occurs in two magnetic forms: approximately 90% of the clusters occurs in a high-spin S = 9/2 system and 10% in a S = 1/2 spin system. In the 3 + state, the cluster occurs in a S = 1/2 spin system; the EPR spectrum of...

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“…Several RdxR-like enzymes and many Rdxs have been extensively studied both structurally and biophysically (17)(18)(19)(20)(21)(22)(23)(24)(25)(26)(27)(28)(29)(30). Here, we present the crystal structure of a dedicated RdxR from P. aeruginosa strain PAO1 at 2.40-Å resolution.…”

mentioning

confidence: 99%

Crystal structure of the electron transfer complex rubredoxin–rubredoxin reductase of Pseudomonas aeruginosa

Hagelueken

Wiehlmann

Adams

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

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Crude oil spills represent a major ecological threat because of the chemical inertness of the constituent n-alkanes. The Gramnegative bacterium Pseudomonas aeruginosa is one of the few bacterial species able to metabolize such compounds. Three chromosomal genes, rubB, rubA1, and rubA2 coding for an NAD(P)H:rubredoxin reductase (RdxR) and two rubredoxins (Rdxs) are indispensable for this ability. They constitute an electron transport (ET) pathway that shuttles reducing equivalents from carbon metabolism to the membrane-bound alkane hydroxylases AlkB1 and AlkB2. The RdxR-Rdx system also is crucial as part of the oxidative stress response in archaea or anaerobic bacteria. The redox couple has been analyzed in detail as a model system for ET processes. We have solved the structure of RdxR of P. aeruginosa both alone and in complex with Rdx, without the need for crosslinking, and both structures were refined at 2.40-and 2.45-Å resolution, respectively. RdxR consists of two cofactor-binding domains and a C-terminal domain essential for the specific recognition of Rdx. Only a small number of direct interactions govern mutual recognition of RdxR and Rdx, corroborating the transient nature of the complex. The shortest distance between the redox centers is observed to be 6.2 Å.

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Rubredoxin from Desulfovibrio gigas

Cited by 110 publications

References 52 publications

A comparative picosecond‐resolved fluorescence study of tryptophan residues in iron‐sulfur proteins

A comparative picosecond‐resolved fluorescence study of tryptophan residues in iron‐sulfur proteins

Overproduction of prismane protein in Desulfovibrio vulgaris (Hildenborough): evidence for a second S= 1/2‐spin system in the one‐electron reduced state

Crystal structure of the electron transfer complex rubredoxin–rubredoxin reductase of Pseudomonas aeruginosa

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