The Structure of the Soluble Domain of an Archaeal Rieske Iron–Sulfur Protein at 1.1Å Resolution

Bönisch, Heiko; Schmidt, Christian; Schäfer, Günter; Ladenstein, Rudolf

doi:10.1016/s0022-2836(02)00323-6

Cited by 73 publications

(78 citation statements)

References 57 publications

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“…In conjunction with recent structural information of Rieske and Rieske-type proteins (6,7,9,10), it is expected that the excited state of electrons localized around the (N imid ) 2 Fe(S b ) 2 portion in the Rieske-type [2Fe-2S] cluster contributes to the higher frequency region in the UV-visible spectra than those around the (S b ) 2 Fe(S t ) 2 moiety, essentially being off resonance in the RR spectra upon excitation in the visible region. Thus, overall contributions of the Fe-N imid vibrations to the RR spec- 6 For Rieske-type [2Fe-2S] proteins, the EXAFS is a measure of the average coordination environment of both iron atoms in the cluster (27).…”

Section: Resultsmentioning

confidence: 97%

Engineering a Three-cysteine, One-histidine Ligand Environment into a New Hyperthermophilic Archaeal Rieske-type [2Fe-2S] Ferredoxin from Sulfolobus solfataricus

Kounosu

Cosper

et al. 2004

Journal of Biological Chemistry

128

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We heterologously overproduced a hyperthermostable archaeal low potential (E m ‫؍‬ ؊62 mV) Rieske-type ferredoxin (ARF) from Sulfolobus solfataricus strain P-1 and its variants in Escherichia coli to examine the influence of ligand substitutions on the properties of the [2Fe-2S] cluster. While two cysteine ligand residues (Cys 42 and Cys 61 ) are essential for the cluster assembly and/or stability, the contributions of the two histidine ligands to the cluster assembly in the archaeal Riesketype ferredoxin appear to be inequivalent as indicated by much higher stability of the His 64 Proteins containing Rieske-type [2Fe-2S] clusters are widespread in nature from hyperthermophilic Archaea and Bacteria to Eukarya and play critical electron transfer roles in various pathways such as aerobic respiration, photosynthesis, and biodegradation of various alkene and aromatic compounds (1-4). In contrast to regular plant-and vertebrate-type ferredoxins having complete cysteinyl ligations, the Rieske-type cluster has an asymmetric iron-sulfur core with the S ␥ atom of each of the two cysteine residues coordinated to one iron site and the N ␦ atom of each of the two histidine residues coordinated to the other iron site. This asymmetric ligation results in some unique redox and spectroscopic properties (for reviews, see Refs. 1 and 3-5). This cluster coordination was firmly established by recent x-ray crystal structures of several different Rieske-type protein domains (6 -11).Two different types of Rieske clusters are observed in proteins. One type displays higher reduction potentials (E m ) 1 of approximately ϩ150 to ϩ490 mV and occurs in proton-translocating respiratory complexes (cytochrome bc 1 /b 6 f complexes and their archaeal homologs without c-type cytochromes), being involved in not only electron transfer but also substrate binding and oxidation at the quinol-oxidizing Q o site (2-5, 12-15). The other type displays lower E m values of approximately Ϫ150 to Ϫ50 mV and has been found in a diverse group of bacterial multicomponent terminal oxygenases and soluble Rieske-type ferredoxins (1, 3, 8, 9, 16 -27). However, none of the latter class has been characterized in detail from any archaeal species.We recently found that the genomic DNA sequence of the thermoacidophilic archaeon Sulfolobus solfataricus strain P-1 (DSM 1616T) encodes an archaeal homolog of bacterial small Rieske-type ferredoxins with no consensus disulfide signature (DDBJ accession number AB047031 (27)). This arf gene was found by homology search against the deduced amino acid sequence of Sulfolobus tokodaii sulredoxin, a water-soluble homolog of a high potential Rieske protein (E m,low pH ϳ ϩ190 mV) with a consensus disulfide linkage (DDBJ accession number AB023295) 2 (28 -30) (Fig. 1). Subsequent cloning and heterologous overexpression in Escherichia coli of this S. solfataricus arf gene encoding the archaeal Rieske-type ferredoxin (ARF) (27) have provided an opportunity to define the influence of surrounding amino acid residues on the electronic and s...

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Section: Resultsmentioning

confidence: 97%

Engineering a Three-cysteine, One-histidine Ligand Environment into a New Hyperthermophilic Archaeal Rieske-type [2Fe-2S] Ferredoxin from Sulfolobus solfataricus

Kounosu

Cosper

et al. 2004

Journal of Biological Chemistry

128

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“…This motif appears as an insertion within a region that corresponds to a loop in dioxygenase Rieske proteins, and is present in five other sequences from Archaea, which share a rather high amino acid identity (approximately 37-52%) among themselves, but not against other types of Rieske proteins (less than 15%). The disulfide bond now identified within this family is a novel structural feature in the Rieske fold, and is unrelated to the disulfides described in respiratory and photosynthetic Rieske domains [17] and in the archaeal respiratory-type SoxF [5], whose cysteines are intertwined within the Fe-S binding motif (CXHXXC…CPCH), and the one presumed to be present in sulredoxin [18].…”

Section: Discussionmentioning

confidence: 99%

“…In summary, the cysteines within the C-terminal SKTPCX (2)(3) C motif are involved in a disulfide bridge, which is novel within the Rieske fold. The other types of disulfides known in Rieske proteins are discussed further later, and are found in respiratory Rieske domains, namely, on the prototypic complex III domains [17] and on the SoxF protein from S. acidocaldarius [5,30].…”

Section: Spectroscopic Characterization Of the Fe-s Cluster In Rfd2mentioning

confidence: 99%

“…Examples include N-and C-terminal amino acid extensions within dicluster ferredoxins [2,3], insertion of a structural zinc site [4], and incorporation of a disulfide bond within the fold [5][6][7]. For instance, dicluster [3Fe-4S][4Fe-4S] ferredoxins [3] contain an N-terminal extension, which modulates the protein stability either by hosting an additional His/Asp zinc center [4,8] or by creating a stabilizing hydrophobic core [9].…”

Section: Introductionmentioning

confidence: 99%

“…It consists of a disulfide bond within the Rieske fold, whose redox status influences the properties of the [2Fe-2S] center and simultaneously stabilizes the protein. This particular disulfide is a novel feature within Rieske proteins, and is unrelated to the disulfides described in respiratory and photosynthetic Rieske domains [17] and in the archaeal respiratory-type SoxF [5] and sulredoxin [18] proteins, which have distinct locations in the fold. This finding illustrates how minor structural modifications modulate protein function and stability and is key to rationalizing the evolutionary adapation of simple Fe-S proteins to distinct conditions and to understanding how relatively simple folds may be finetuned for a particular function or for increased stability.…”

Section: Introductionmentioning

confidence: 99%

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Role of a novel disulfide bridge within the all-beta fold of soluble Rieske proteins

et al. 2009

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Rieske proteins and Rieske ferredoxins are present in the three domains of life and are involved in a variety of cellular processes. Despite their functional diversity, these small Fe-S proteins contain a highly conserved all-b fold, which harbors a [2Fe-2S] Rieske center. We have identified a novel subtype of Rieske ferredoxins present in hyperthermophilic archaea, in which a twocysteine conserved SKTPCX (2-3) C motif is found at the C-terminus. We establish that in the Acidianus ambivalens representative, Rieske ferredoxin 2 (RFd2), these cysteines form a novel disulfide bond within the Rieske fold, which can be selectively broken under mild reducing conditions insufficient to reduce the [2Fe-2S] cluster or affect the secondary structure of the protein, as shown by visible circular dichroism, absorption, and attenuated total reflection Fourier transform IR spectroscopies. RFd2 presents all the EPR, visible absorption, and visible circular dichroism spectroscopic features of the [2Fe-2S] Rieske center. The cluster has a redox potential of ?48 mV (25°C and pH 7) and a pK a of 10.1 ± 0.2. These shift to ?77 mV and 8.9 ± 0.3, respectively, upon reduction of the disulfide. RFd2 has a melting temperature near the boiling point of water (T m = 99°C, pH 7.0), but it becomes destabilized upon disulfide reduction (DT m = -9°C, DC m = -0.7 M guanidinium hydrochloride). This example illustrates how the incorporation of an additional structural element such as a disulfide bond in a highly conserved fold such as that of the Rieske domain may fine-tune the protein for a particular function or for increased stability.

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Thioredoxin‐Like [2Fe–2S] Ferredoxin

Meyer

Andrade

Einsle

2004

Handbook of Metalloproteins

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Putative electron transfer protein, may have regulatory function.The small size of the protein (3D structure) and the −300 mV reduction potential of its 2+,+ active site may suggest an electron transfer function among some of the more reducing redox reactions in microbial cells. In contrast, the dimeric structure and the protruding loop near the [2Fe-2S] cluster are more suggestive of a regulatory function, possibly in association with redox processes. O C C U R R E N C E

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The Structure of the Soluble Domain of an Archaeal Rieske Iron–Sulfur Protein at 1.1Å Resolution

Cited by 73 publications

References 57 publications

Engineering a Three-cysteine, One-histidine Ligand Environment into a New Hyperthermophilic Archaeal Rieske-type [2Fe-2S] Ferredoxin from Sulfolobus solfataricus

Engineering a Three-cysteine, One-histidine Ligand Environment into a New Hyperthermophilic Archaeal Rieske-type [2Fe-2S] Ferredoxin from Sulfolobus solfataricus

Role of a novel disulfide bridge within the all-beta fold of soluble Rieske proteins

Thioredoxin‐Like [2Fe–2S] Ferredoxin

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