The adrenodoxin-like ferredoxin of Schizosaccharomyces pombe mitochondria

Schiffler, Burkhard; Bureik, Matthias; Reinle, Wolfgang; Müller, Eva‐Christina; Hannemann, Frank; Bernhardt, Rita

doi:10.1016/j.jinorgbio.2004.02.006

Cited by 40 publications

(38 citation statements)

References 26 publications

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“…Therefore, we prepared two UV-vis and EPR spectra indicated that both proteins assembled as holoproteins, because the typical signals of ferredoxins due to the FeS cluster were present in all spectra recorded (Fig.1, Fig.2). The protein solutions displayed the characteristic brown color of the iron-sulfur cluster and showed Qvalues (A 415 /A 276 ) of more than 0.85 as described earlier [21]. Protein yields reached more than 20 mg l -1 of expression culture for both forms.…”

Section: Expression and Functionality Of Etp1 Fdsupporting

confidence: 68%

“…Expression of the full-length Etp1 fd (127 amino acid residues) using E. coli strain BL21 as expression host has been described recently [21]. Because crystallization trials failed with the full-length Etp1 fd ,…”

Section: Cloning Gene Expression and Protein Purificationmentioning

confidence: 99%

“…Recombinant Adx, Etp1 fd and Arh1 were purified as described [7,21,22]. The protein concentrations were calculated with ε 414 = 9.8 (mM cm) -1 for Etp1 fd [21] and Adx with ε 450 = 11.3 (mM cm) -1 for Arh1 [7].…”

Section: Cloning Gene Expression and Protein Purificationmentioning

confidence: 99%

“…The protein concentrations were calculated with ε 414 = 9.8 (mM cm) -1 for Etp1 fd [21] and Adx with ε 450 = 11.3 (mM cm) -1 for Arh1 [7]. …”

Section: Cloning Gene Expression and Protein Purificationmentioning

confidence: 99%

“…Interaction site II is somewhat more distant from the AdR surface in Etp1 fd than in Adx, but a slight rigid-body movement of Etp1 fd may close the gap. The slightly changed structure of Etp1 fd could be one reason for the reduced efficiency in the substrate conversion with AdR and CYP11A1 [21].…”

Section: Structural Comparison Of Etp1 Fd (516-618) and Adx(4-108)mentioning

confidence: 99%

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Structural and thermodynamic characterization of the adrenodoxin-like domain of the electron-transfer protein Etp1 from Schizosaccharomyces pombe

Müller

Hannemann

Schiffler

et al. 2011

Journal of Inorganic Biochemistry

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The protein Etp1 of Schizosaccharomyces pombe consists of an amino-terminal COX15-like domain and a carboxy-terminal ferredoxin-like domain, Etp1 fd , which is cleaved off after mitochondrial import. The physiological function of Etp1 fd is supposed to lie in the participation in the assembly of iron-sulfur clusters and the synthesis of heme A. In addition, the protein was shown to be the first microbial ferredoxin being able to support electron transfer in mitochondrial steroid hydroxylating cytochrome P450 systems in vivo and in vitro, replacing thereby the native redox partner, adrenodoxin. Despite a sequence similarity of 39% and the fact that fission yeast is a mesophilic organism, thermodynamic studies revealed that Etp1 fd has a melting temperature more than 20 °C higher than adrenodoxin. The three-dimensional structure of Etp1 fd has been determined by crystallography. To the best of our knowledge it represents the first three-dimensional structure of a mitochondrial ferredoxin. The structure-based sequence alignment of Etp1 fd with adrenodoxin yields a rational explanation for their observed mutual exchangeability in the cytochrome P450 system.Analysis of the electron exchange with the S. pombe redox partner Arh1 revealed differences between Etp1 fd and adrenodoxin, which might be linked to their different physiological functions in the mitochondria of mammals and yeast.

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Section: Expression and Functionality Of Etp1 Fdsupporting

confidence: 68%

Section: Cloning Gene Expression and Protein Purificationmentioning

confidence: 99%

Section: Cloning Gene Expression and Protein Purificationmentioning

confidence: 99%

“…The protein concentrations were calculated with ε 414 = 9.8 (mM cm) -1 for Etp1 fd [21] and Adx with ε 450 = 11.3 (mM cm) -1 for Arh1 [7]. …”

Section: Cloning Gene Expression and Protein Purificationmentioning

confidence: 99%

Section: Structural Comparison Of Etp1 Fd (516-618) and Adx(4-108)mentioning

confidence: 99%

See 3 more Smart Citations

Structural and thermodynamic characterization of the adrenodoxin-like domain of the electron-transfer protein Etp1 from Schizosaccharomyces pombe

Müller

Hannemann

Schiffler

et al. 2011

Journal of Inorganic Biochemistry

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Mitochondrial [2Fe‐2S] ferredoxins: new functions for old dogs

et al. 2022

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Ferredoxins (FDXs) comprise a large family of iron–sulfur proteins that shuttle electrons from NADPH and FDX reductases into diverse biological processes. This review focuses on the structure, function and specificity of mitochondrial [2Fe‐2S] FDXs that are related to bacterial FDXs due to their endosymbiotic inheritance. Their classical function in cytochrome P450‐dependent steroid transformations was identified around 1960, and is exemplified by mammalian FDX1 (aka adrenodoxin). Thirty years later the essential function in cellular Fe/S protein biogenesis was discovered for the yeast mitochondrial FDX Yah1 that is additionally crucial for the formation of haem a and ubiquinone CoQ6. In mammals, Fe/S protein biogenesis is exclusively performed by the FDX1 paralog FDX2, despite the high structural similarity of both proteins. Recently, additional and specific roles of human FDX1 in haem a and lipoyl cofactor biosyntheses were described. For lipoyl synthesis, FDX1 transfers electrons to the radical S‐adenosyl methionine‐dependent lipoyl synthase to kickstart its radical chain reaction. The high target specificity of the two mammalian FDXs is contained within small conserved sequence motifs, that upon swapping change the target selection of these electron donors.

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Resin Acid Conversion with CYP105A1: An Enzyme with Potential for the Production of Pharmaceutically Relevant Diterpenoids

et al. 2013

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Cytochrome P450s are very versatile enzymes with great potential for biotechnological applications because of their ability to oxidize unactivated CH bonds. CYP105A1 from Streptomyces griseolus was first described as a herbicide-inducible sulfonylurea hydroxylase, but it is also able to convert other substrates such as vitamin D(3) . To extend the substrate pool of this interesting enzyme further, we screened a small diterpenoid compound library and were able to show the conversion of several resin acids. Binding of abietic acid, dehydroabietic acid, and isopimaric acid to the active site was assayed, and V(max) and K(m) values were calculated. The products were analyzed by NMR spectroscopy and identified as 15-hydroxyabietic acid, 15-hydroxydehydroabietic acid, and 15,16-epoxyisopimaric acid. As the observed products are difficult to obtain by chemical synthesis, CYP105A1 has proved to be a promising candidate for biotechnological applications that combine bioconversion and chemical synthesis to obtain functionalized resin acids.

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The adrenodoxin-like ferredoxin of Schizosaccharomyces pombe mitochondria

Cited by 40 publications

References 26 publications

Structural and thermodynamic characterization of the adrenodoxin-like domain of the electron-transfer protein Etp1 from Schizosaccharomyces pombe

Structural and thermodynamic characterization of the adrenodoxin-like domain of the electron-transfer protein Etp1 from Schizosaccharomyces pombe

Mitochondrial [2Fe‐2S] ferredoxins: new functions for old dogs

Resin Acid Conversion with CYP105A1: An Enzyme with Potential for the Production of Pharmaceutically Relevant Diterpenoids

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