The (2<i>R</i>)‐hydroxycarboxylate‐viologen‐oxidoreductase from <i>Proteus vulgaris</i> is a molybdenum‐containing iron‐sulphur protein

Trautwein, Thomas; Krauss, Friedrich; Lottspeich, Friedrich; Simon, Helmut

doi:10.1111/j.1432-1033.1994.tb18954.x

Cited by 27 publications

(24 citation statements)

References 52 publications

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“…2). The latter enzyme is an 80-kDa protein, containing one molybdenum, four iron, and four sulfur atoms, as well as a mononucleotide (pterin) molybdenum cofactor (29). Although tungsten proteins are present in some Bacteria (22), one might speculate that the unidentified E. coli oxidoreductase possesses a molybdopterin cofactor.…”

Section: Discussionmentioning

confidence: 99%

The Ferredoxin-dependent Conversion of Glyceraldehyde-3-phosphate in the Hyperthermophilic ArchaeonPyrococcus furiosus Represents a Novel Site of Glycolytic Regulation

Oost¹,

Schut²,

Kengen³

et al. 1998

Journal of Biological Chemistry

102

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The fermentative conversion of glucose in anaerobic hyperthermophilic Archaea is a variant of the classical Embden-Meyerhof pathway found in Bacteria and Eukarya. A major difference of the archaeal glycolytic pathway concerns the conversion of glyceraldehyde-3-phosphate. In the hyperthermophilic archaeon Pyrococcus furiosus, this reaction is catalyzed by an unique enzyme, glyceraldehyde-3-phosphate ferredoxin oxidoreductase (GAPOR). Here, we report the isolation, characterization, and transcriptional analysis of the GAPOR-encoding gene. GAPOR is related to a family of ferredoxin-dependent tungsten enzymes in (hyper)thermophilic Archaea and, in addition, to a hypothetical protein in Escherichia coli. Electron paramagnetic resonance analysis of the purified P. furiosus GAPOR protein confirms the anticipated involvement of tungsten in catalysis. During glycolysis in P. furiosus, GAPOR gene expression is induced, whereas the activity of glyceraldehyde-3-phosphate dehydrogenase is repressed. It is discussed that this unprecedented unidirectional reaction couple in the pyrococcal glycolysis and gluconeogenesis gives rise to a novel site of glycolytic regulation that might be widespread among Archaea.

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Section: Discussionmentioning

confidence: 99%

The Ferredoxin-dependent Conversion of Glyceraldehyde-3-phosphate in the Hyperthermophilic ArchaeonPyrococcus furiosus Represents a Novel Site of Glycolytic Regulation

Oost¹,

Schut²,

Kengen³

et al. 1998

Journal of Biological Chemistry

102

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“…Similar observations have been made for the assimilatory Mo-containing NR of plants (see below, [204,[217][218][219]). P. vulgaris contains another Mo-containing enzyme, (2R)-hydroxycarboxylate-viologenoxidoreductase (HVOR) [220]. Interestingly, HVOR is phylogenetically related to the family of W-containing aldehyde oxidoreductases as judged N-terminal amino acid sequence comparisons (see below).…”

Section: Aerobic and Facultatively Aerobic Bacteriamentioning

confidence: 99%

Tungsten in biological systems

Kletzin

Adams

1996

FEMS Microbiology Reviews

134

144

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Tungsten (atomic number 74) and the chemically analogous and very similar metal molybdenum (atomic number 42) are minor yet equally abundant elements on this planet. The essential role of molybdenum in biology has been known for decades and molybdoenzymes are ubiquitous. Yet, it is only recently that a biological role for tungsten has been established in prokaryotes, although not as yet in eukaryotes. The best characterized organisms with regard to their metabolism of tungsten are certain species of hyperthermophilic archaea (Pyrococcus furiosus and Thermococcus litoralis), methanogens (Methanobacterium thermoautotrophicum and Mb. wolfei), Gram-positive bacteria (Clostridium thermoaceticum, C. formicoaceticum and Eubacterium acidaminophilum), Gram-negative anaerobes (Desulfovibrio gigas and Pelobacter acetylenicus) and Gram-negative aerobes (Methylobacterium sp. RXM). Of these, only the hyperthermophilic archaea appear to be obligately tungsten-dependent. Four different types of tungstoenzyme have been purified: formate dehydrogenase, formyl methanofuran dehydrogenase, acetylene hydratase, and a class of phylogenetically related oxidoreductases that catalyze the reversible oxidation of aldehydes. These are carboxylic reductase, and three ferredoxin-dependent oxidoreductases which oxidize various aldehydes, formaldehyde and glyceraldehyde 3-phosphate. All tungstoenzymes catalyze redox reactions of very low potential (< -420 mV) except one (acetylene hydratase) which catalyzes a hydration reaction. The tungsten in these enzymes is bound by a pterin moiety similar to that found in molybdoenzymes. The first crystal structure of a tungsten-or pterin-containing enzyme, that of aldehyde ferredoxin oxidoreductase from P. furiosus, has revealed a catalytic site with one W atom coordinated to two pterin molecules which are themselves bridged by a magnesium ion. The geochemical, ecological, biochemical and phylogenetic basis for W-vs. Mo-dependent organisms is discussed.

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“…strain ES-4 (10), and Thermococcus sp. strain ES-1 (4) and the FORs of P. furiosus (10) and T. litoralis (8) are homologous to the W-containing GAPOR from P. furiosus (9), the W-containing carboxylic acid reductases (CARs) from Clostridium thermoaceticum and Clostridium formicoaceticum (16,18), and surprisingly, the Mo-containing (2R)-hydroxycarboxylate viologen oxidoreductase (HVOR) from Proteus vulgaris (15). This high degree of similarity suggests that domain I of AOR, which provides a structural backbone for the tungstodipterin site (2) and is highly conserved in FOR, might also be conserved in these other oxidoreductases.…”

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Molecular characterization of the genes encoding the tungsten-containing aldehyde ferredoxin oxidoreductase from Pyrococcus furiosus and formaldehyde ferredoxin oxidoreductase from Thermococcus litoralis

et al. 1995

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The hyperthermophilic archaea Pyrococcus furiosus and Thermococcus litoralis contain the tungstoenzymes aldehyde ferredoxin oxidoreductase, a homodimer, and formaldehyde ferredoxin oxidoreductase, a homotetramer. Herein we report the cloning and sequencing of the P. furiosus gene aor (605 residues; M r , 66,630) and the T. litoralis gene for (621 residues; M r , 68,941).Enzymes containing tungsten (W) are rare in biology, yet the hyperthermophilic archaea contain three distinct types, all of which catalyze aldehyde oxidation (6-9). The homodimeric aldehyde ferredoxin oxidoreductase (AOR) of Pyrococcus furiosus (maximum growth temperature [T max ], 105ЊC [3]) oxidizes a wide range of aliphatic and aromatic, nonphosphorylated aldehydes (7). Recent crystallographic analysis (refined at 2.3 Å [2]) demonstrated that the two subunits of AOR are bridged by a monomeric iron site and that each subunit contains a [4Fe-4S] cluster and a mononuclear W cofactor. The W site is coordinated by four dithiolene-sulfur ligands from two pterin molecules (2). In contrast to AOR, the homotetrameric formaldehyde ferredoxin oxidoreductase (FOR) of Thermococcus litoralis (T max , 98ЊC [11]) oxidizes only C 1 to C 3 aldehydes, although it also contains one W atom and one [4Fe-4S] cluster per subunit (8). The third W-containing oxidoreductase (GAPOR) is monomeric and specifically oxidizes glyceraldehyde-3-phosphate (9). We have now cloned and sequenced the genes encoding P. furiosus AOR and T. litoralis FOR. The primary structure of a tungstoenzyme has not been previously reported.P. furiosus AOR. For aor, a 7.2-kbp EcoRI P. furiosus (DSM 3638 [3]) genomic fragment was cloned into pBluescript II KS ϩ (pAOR 3-1), using probes derived from the amino-terminal sequence and standard procedures (Southern blotting and hybridization and colony lifts) (12). From pAOR 3-1, 4,951 bp were sequenced, beginning 90 bp upstream of a unique internal EcoRV site and ending at the downstream EcoRI site (Fig. 1). Sequencing was performed with a mixture of deletion clones constructed with appropriate restriction enzymes and by primer walking. The fragment contained the genetic information for the entire AOR polypeptide ( Fig. 1 and 2) together with (i) a P. furiosus gene, termed cmo for cofactor modification, which may code for a cofactor-modifying protein; (ii) the first 169 amino acid residues of a P. furiosus ahc gene encoding an S-adenosylhomocysteine hydrolase; and (iii) a short open reading frame and a partially sequenced long open reading frame of unknown function ( Fig. 1) (5).The gene for AOR contained 605 codons which correspond to a protein with a molecular weight of 66,630 (compared with 85,000 by sodium dodecyl sulfate (SDS)-gel analysis [7]) or 136,066 for the homodimer, including cofactors (Fig. 2). The [4Fe-4S] cluster in each AOR subunit is liganded by the cysteinyl residues at positions 288, 290, 295, and 494 (Fig. 2). The remote Cys-494 residue forms a hydrogen bond to a ring nitrogen of one pterin, thus linking the two metal centers at the...

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The (2R)‐hydroxycarboxylate‐viologen‐oxidoreductase from Proteus vulgaris is a molybdenum‐containing iron‐sulphur protein

Cited by 27 publications

References 52 publications

The Ferredoxin-dependent Conversion of Glyceraldehyde-3-phosphate in the Hyperthermophilic ArchaeonPyrococcus furiosus Represents a Novel Site of Glycolytic Regulation

The Ferredoxin-dependent Conversion of Glyceraldehyde-3-phosphate in the Hyperthermophilic ArchaeonPyrococcus furiosus Represents a Novel Site of Glycolytic Regulation

Tungsten in biological systems

Molecular characterization of the genes encoding the tungsten-containing aldehyde ferredoxin oxidoreductase from Pyrococcus furiosus and formaldehyde ferredoxin oxidoreductase from Thermococcus litoralis

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