Gene sequence and crystal structure of the aldehyde oxidoreductase from Desulfovibrio desulfuricans ATCC 27774

Rebelo, Jorge; Macieira, Sofia; Dias, João M.; Huber, Robert; Ascenso, Carla; Rusnak, Frank; Moura, José J. G.; Moura, Isabel; Romão, Maria João

doi:10.1006/jmbi.2000.3552

Cited by 65 publications

(41 citation statements)

References 37 publications

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“…However, crystallization of as-prepared DgAOR [7,8] and DdAOR [9,16] samples results in the desulfo form of the enzyme and a similar process could occur in the crystallization of the samples giving signal A. Hence, we cannot confirm with this experiment the involvement of the sulfido ligand in the MoAs complex giving signal A, as previously suggested for milk XO [22,28].…”

Section: Structural Datamentioning

confidence: 50%

“…After 1 h of incubation, a new EPR signal was detected. Also, using the same methods, samples that exhibited EPR signals A and B were prepared in Tris-DCl buffered D 2 O solutions, as [8,9]. b ''Resulfurated'' DgAOR, as determined by Huber et al [19].…”

Section: Preparation Of Samples For Epr Spectroscopymentioning

confidence: 99%

“…Preparation of DdAOR-A and DdAOR-B crystals Crystalline arsenite-inhibited forms of DdAOR were prepared from EPR samples exhibiting pure signal A or B, as described for DgAOR-A and DgAOR-B, using conditions similar to those described previously [9]. These crystals are referred to as DdAOR-A and DdAOR-B, respectively.…”

Section: Preparation Of Dgaor-a and Dgaor-b Crystalsmentioning

confidence: 99%

“…Several crystal structures of other members of the family have also been determined [9][10][11][12][13][14]. The combination of structural and spectroscopic data on enzymes of this family has shown that the active site consists, in the Mo(VI) state, of a molybdenum atom in a squarepyramidal geometry that coordinates the two sulfur atoms from one pyranopterin ligand, one oxo ligand, one hydroxyl/water molecule and one sulfido ligand.…”

Section: Introductionmentioning

confidence: 99%

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Correlating EPR and X-ray structural analysis of arsenite-inhibited forms of aldehyde oxidoreductase

et al. 2006

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Two arsenite-inhibited forms of each of the aldehyde oxidoreductases from Desulfovibrio gigas and Desulfovibrio desulfuricans have been studied by X-ray crystallography and electron paramagnetic resonance (EPR) spectroscopy. The molybdenum site of these enzymes shows a distorted square-pyramidal geometry in which two ligands, a hydroxyl/water molecule (the catalytic labile site) and a sulfido ligand, have been shown to be essential for catalysis. Arsenite addition to active as-prepared enzyme or to a reduced desulfo form yields two different species called A and B, respectively, which show different Mo(V) EPR signals. Both EPR signals show strong hyperfine and quadrupolar couplings with an arsenic nucleus, which suggests that arsenic interacts with molybdenum through an equatorial ligand. X-ray data of single crystals prepared from EPR-active samples show in both inhibited forms that the arsenic atom interacts with the molybdenum ion through an oxygen atom at the catalytic labile site and that the sulfido ligand is no longer present. EPR and X-ray data indicate that the main difference between both species is an equatorial ligand to molybdenum which was determined to be an oxo ligand in species A and a hydroxyl/water ligand in species B. The conclusion that the sulfido ligand is not essential to determine the EPR properties in both MoAs complexes is achieved through EPR measurements on a substantial number of randomly oriented chemically reduced crystals immediately followed by X-ray studies on one of those crystals. EPR saturation studies show that the electron transfer pathway, which is essential for catalysis, is not modified upon inhibition.

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Section: Structural Datamentioning

confidence: 50%

Section: Preparation Of Samples For Epr Spectroscopymentioning

confidence: 99%

Section: Preparation Of Dgaor-a and Dgaor-b Crystalsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Correlating EPR and X-ray structural analysis of arsenite-inhibited forms of aldehyde oxidoreductase

et al. 2006

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“…Mammalian molybdo-iron-sulfur-flavoproteins (henceforth referred as molybdo-flavoproteins for simplicity) are widely distributed enzymes requiring a molybdo-pterin and a flavin cofactor for their catalytic activity (1)(2)(3)(4)(5)(6). In mammals, this family was originally thought to consist of two members, xanthine oxidoreductase (XOR) 1 and aldehyde oxidase (AO) (1).…”

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confidence: 99%

Purification of the Aldehyde Oxidase Homolog 1 (AOH1) Protein and Cloning of the AOH1 and Aldehyde Oxidase Homolog 2 (AOH2) Genes

Terao¹,

Kurosaki²,

Marini³

et al. 2001

Journal of Biological Chemistry

111

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We report the cloning of the AOH1 and AOH2 genes, which encode two novel mammalian molybdo-flavoproteins. We have purified the AOH1 protein to homogeneity in its catalytically active form from mouse liver. Twenty tryptic peptides, identified or directly sequenced by mass spectrometry, confirm the primary structure of the polypeptide deduced from the AOH1 gene. The enzyme contains one molecule of FAD, one atom of molybdenum, and four atoms of iron per subunit and shows spectroscopic features similar to those of the prototypic molybdo-flavoprotein xanthine oxidoreductase. The AOH1 and AOH2 genes are 98 and 60 kilobases long, respectively, and consist of 35 coding exons. The AOH1 gene has the potential to transcribe an extra leader non-coding exon, which is located downstream of exon 26, and is transcribed in the opposite orientation relative to all the other exons. AOH1 and AOH2 map to chromosome 1 in close proximity to each other and to the aldehyde oxidase gene, forming a molybdo-flavoenzyme gene cluster. Conservation in the position of exon/ intron junctions among the mouse AOH1, AOH2, aldehyde oxidase, and xanthine oxidoreductase loci indicates that these genes are derived from the duplication of an ancestral precursor.

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Aldehyde Oxidoreductase (MOP)

Romão

Moura

2004

Handbook of Metalloproteins

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The aldehyde oxido‐reductase from Desulfovibrio gigas (MOP) is a member of the xanthine oxidase family but simpler since it lacks the flavin–adenine dinucleotide (FAD) domain. It is composed of a single polypeptide chain of 907 amino acids and contains one molybdenum atom bound to a molybdopterin cytosine dinucleotide (MCD) cofactor, as well as two spectroscopically distinguishable [2Fe2S] clusters involved in electron transfer. The Mo atom is pentacoordinated by the two sulfurs of the cis ‐dithiolene group of the molybdopterin, plus two oxo and one hydroxyl/water ligand. It hydroxylates a wide range of aldehydes with little specificity but its physiological role is not totally clear.

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Gene sequence and crystal structure of the aldehyde oxidoreductase from Desulfovibrio desulfuricans ATCC 27774

Cited by 65 publications

References 37 publications

Correlating EPR and X-ray structural analysis of arsenite-inhibited forms of aldehyde oxidoreductase

Correlating EPR and X-ray structural analysis of arsenite-inhibited forms of aldehyde oxidoreductase

Purification of the Aldehyde Oxidase Homolog 1 (AOH1) Protein and Cloning of the AOH1 and Aldehyde Oxidase Homolog 2 (AOH2) Genes

Aldehyde Oxidoreductase (MOP)

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