New enzyme belonging to the family of molybdenum-free nitrate reductases

Антипов, А. Н.; Sorokin, Dimitry Y.; L'vov, N. P.; Kuenen, J.G.

doi:10.1042/bj20021193

Cited by 45 publications

(35 citation statements)

References 22 publications

(24 reference statements)

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“…X-ray diffraction studies show the Schiff base pyr 2 The complexes prepared are slightly soluble in water and the order of stability of the complexes formed is pyridoxamine < H 2 pyr 2 en < H 2 Rpyr 2 en. Pyridoxal and pyridoxamine are forms of vitamin B 6 and are nontoxic metabolites. Their vanadium complexes may therefore be good candidates for therapeutic use.…”

Section: Resultsmentioning

confidence: 99%

“…T h e H 2 pyr 2 en and H 2 Rpyr 2 en ligands contain six protons that dissociate in the measurable pH range, so the totally protonated species correspond to [H 6 . The corresponding protonation constants are included in Table 3.…”

Section: Ligand Protonation By Ph-potentiometry and 1 H Nmr Spectroscmentioning

confidence: 99%

“…[11,12] To date, only [V IV O(sal 2 en)] has been tested in vivo for insulin-mimetic activity. Pyridoxal and pyridoxamine are forms of vitamin B 6 , known cofactors required by many enzymes. They are nontoxic metabolites and fairly soluble in aqueous solution.…”

Section: Introductionmentioning

confidence: 99%

“…[3] Three types of vanadiumcontaining enzymes are known: vanadium nitrogenases, [4] vanadium-dependent haloperoxidases, [5] and vanadium-containing nitrate reductases. [6,7] Among other biological effects, vanadium×s insulin-like action [8] and anticancer activity [9] have stimulated a considerable amount of research. However, our understanding of the role of vanadium in living organisms is far from complete.…”

Section: Introductionmentioning

confidence: 99%

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N,N′‐Ethylenebis(pyridoxylideneiminato) and N,N′‐Ethylenebis(pyridoxylaminato): Synthesis, Characterization, Potentiometric, Spectroscopic, and DFT Studies of Their Vanadium(IV) and Vanadium(V) Complexes

Correia¹,

Pessoa²,

Duarte³

et al. 2004

Chemistry A European J

128

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The Schiff base N,N'-ethylenebis(pyridoxylideneiminato) (H 2 pyr 2 en, 1) was synthesized by reaction of pyridoxal with ethylenediamine; reduction of H 2 pyr 2 en with NaBH 4 yielded the reduced Schiff base N,N'-ethylenebis-(pyridoxylaminato) (H 2 Rpyr 2 en, 2); their crystal structures were determined by X-ray diffraction. The totally protonated forms of 1 and 2 correspond to H 6 L 4 + , and all protonation constants were determined by pH-potentiometric and Supporting information for this article is available on the WWW under http://www.chemeurj.org/ or from the author. Some additional X-ray data for 1, 2, 4, and 9 (SI-1); further discussion of IR spectra (

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Section: Resultsmentioning

confidence: 99%

Section: Ligand Protonation By Ph-potentiometry and 1 H Nmr Spectroscmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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N,N′‐Ethylenebis(pyridoxylideneiminato) and N,N′‐Ethylenebis(pyridoxylaminato): Synthesis, Characterization, Potentiometric, Spectroscopic, and DFT Studies of Their Vanadium(IV) and Vanadium(V) Complexes

Correia¹,

Pessoa²,

Duarte³

et al. 2004

Chemistry A European J

128

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“…This implies that strain ALEN 2 T possesses both nitrate and nitrite reductase activities despite the fact that it is unable to use nitrite as an electron acceptor in vivo. Antipov et al (2003) have demonstrated the presence of a nitrate/nitrite reductase in strain ALEN 2 T with unusual properties. Activities of the sulfur-metabolizing enzymes thiosulfate reductase, sulfite dehydrogenase and sulfide dehydrogenase were found in the soluble fraction of cell-free extract of strain ALEN 2 T at pH 10 [690, 260 and 60 nmol (mg protein) 21 min 21 , respectively].…”

mentioning

confidence: 99%

Thialkalivibrio nitratireducens sp. nov., a nitrate-reducing member of an autotrophic denitrifying consortium from a soda lake

Sorokin

Tourova

Sjollema

et al. 2003

INTERNATIONAL JOURNAL OF SYSTEMATIC AND EVOLUTIONARY MICROBIOLO

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Strain ALEN 2 T was isolated from a mixed culture capable of complete autotrophic denitrification with thiosulfate as electron donor at pH 10; the mixed culture was enriched from sediment from Lake Fazda (Wadi Natrun, Egypt), a hypersaline alkaline lake. The isolate had large, non-motile, coccoid or barrel-shaped cells with intracellular sulfur globules. The bacterium was obligately chemolithoautotrophic. It grew with reduced sulfur compounds aerobically and anaerobically with nitrate as electron acceptor, nitrate being reduced to nitrite. It was moderately halophilic and obligately alkaliphilic. On the basis of genetic analysis and its unique phenotype, strain ALEN 2 T (=DSM 14787 T =UNIQEM 213 T ) is proposed as the type strain of a novel species of the genus Thialkalivibrio, Thialkalivibrio nitratireducens.

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Octaheme CytochromecNitrite Reductase

Tikhonova¹,

Polyakov²,

Boyko³

et al. 2004

Handbook of Metalloproteins

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Octaheme cytochrome c nitrite reductase (TvNiR) from bacterium Thioalkalivibrio nitratireducens catalyzes the six‐electron reduction of nitrite and two‐electron reduction of hydroxylamine to ammonium without release of any intermediates. TvNiR also catalyzes the six‐electron reduction of sulfite to sulfide. High‐resolution structures of the TvNiR apo‐form and its complexes with the substrates (nitrite and sulfite) and inhibitors (azide and phosphate) were obtained. The subunit of TvNiR consists of two domains. The N‐terminal domain has a unique fold and contains three hemes. The remaining five hemes are located in the catalytic C‐terminal domain, with the heme arrangement, including the catalytic heme, being identical to that found in pentaheme cytochrome c nitrite reductases (ccNiRs). The catalytic machinery of TvNiR resembles that of ccNiRs. It comprises the lysine residue in the proximal position of the catalytic heme, the catalytic triad of tyrosine, histidine, and arginine on the distal side, channels for the substrate and product transport, and two conserved Ca 2+ ‐binding sites. The complete set of eight hemes forms a spatial pattern characteristic of other structurally characterized octaheme cytochromes. In the crystalline state and in solution, TvNiR exists as a stable hexamer containing 48 hemes, which are clustered into three isolated groups, each group comprising 16 interacting hemes.

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New enzyme belonging to the family of molybdenum-free nitrate reductases

Cited by 45 publications

References 22 publications

N,N′‐Ethylenebis(pyridoxylideneiminato) and N,N′‐Ethylenebis(pyridoxylaminato): Synthesis, Characterization, Potentiometric, Spectroscopic, and DFT Studies of Their Vanadium(IV) and Vanadium(V) Complexes

N,N′‐Ethylenebis(pyridoxylideneiminato) and N,N′‐Ethylenebis(pyridoxylaminato): Synthesis, Characterization, Potentiometric, Spectroscopic, and DFT Studies of Their Vanadium(IV) and Vanadium(V) Complexes

Thialkalivibrio nitratireducens sp. nov., a nitrate-reducing member of an autotrophic denitrifying consortium from a soda lake

Octaheme CytochromecNitrite Reductase

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