The Purification and Properties of a Copper Nitrite Reductase from Haloferax denitrificans

Inatomi, Ken-ichi; Hochstein, Lawrence I.

doi:10.1007/s002849900013

Cited by 48 publications

(26 citation statements)

References 14 publications

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“…The inhibition of Cu-NiR in the presence of low concentrations of DDC supported that this enzyme was a Cu-NiR. Even though the membranebound Cu-NiR was not totally purified, its characteristics were similar to those of the enzyme purified from the soluble fraction (Inatomi & Hochstein, 1996).…”

Section: Respiratory Nitrite Reductases In Haloferax Genusmentioning

confidence: 61%

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Anaerobic Metabolism in Haloferax Genus

Torregrosa-Crespo

Martínez‐Espinosa

Esclapez

et al. 2016

Advances in Microbial Physiology

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A number of species of Haloferax genus (halophilic Archaea) are able to grow micro aerobically or even anaerobically using different alternative electron acceptors such as fumarate, nitrate, chlorate, dimethyl sulphoxide, sulphide and/or trimethylamine. This metabolic capability is also shown by other species of the Halobacteriaceae and Haloferacaceae families (Archaea domain) and it has been mainly tested by physiological studies where cells growth is observed under anaerobic conditions in the presence of the mentioned compounds. This work summarises the main reported features on anaerobic metabolism in the Haloferax, one of the better described haloarchaeal genus with significant potential uses in Biotechnology and Bioremediation. Special attention has been paid to denitrification, also called nitrate respiration. This pathway has been studied so far from KEY WORDSHaloarchaea, denitrification, anaerobic metabolism, Nox emissions, bioremediation.

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Section: Respiratory Nitrite Reductases In Haloferax Genusmentioning

confidence: 61%

“…It was in 1996 when the first extremophilic respiratory nitrite reductase from Hfx. denitrificans was purified and characterised (Table 1) from soluble and membrane fractions (Inatomi & Hochstein, 1996).…”

Section: Respiratory Nitrite Reductases In Haloferax Genusmentioning

confidence: 99%

Anaerobic Metabolism in Haloferax Genus

Torregrosa-Crespo

Martínez‐Espinosa

Esclapez

et al. 2016

Advances in Microbial Physiology

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“…Interestingly, the Haloferax denitrificans nirK gene sequence is also available (CAD89521, Table 1), and is highly similar to both H. marismortui and N. gonorrhoeae Cu-Nir. However, antiserum against bacterial Cu-Nir does not recognize the H. denitrificans enzyme, suggesting possible structural differences (Inatomi & Hochstein, 1996).…”

Section: Nitrite Respirationmentioning

confidence: 99%

“…Therefore, knowledge of denitrification in archaea is of special interest from an evolutionary point of view. Denitrification has been described for several halophilic archaea, such as Haloferax and Haloarcula strains (Tomlinson et al, 1986;Inatomi & Hochstein, 1996;Ichiki et al, 2001), and extreme thermophilic archaea, such as Ferroglobus placidus (Vorholt et al, 1997) and Pyrobaculum aerophilum (Völkl et al, 1993;de Vries & Schröder, 2002). As the archaeal respiratory nitrate reductases that catalyse the first step of denitrification have been described above, we will focus now on the nitrite and N-oxide respiration processes in archaea.…”

Section: Denitrification In Archaeamentioning

confidence: 99%

Nitrate reduction and the nitrogen cycle in archaea

2004

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The nitrogen cycle (N-cycle) in the biosphere, mainly driven by prokaryotes, involves different reductive or oxidative reactions used either for assimilatory purposes or in respiratory processes for energy conservation. As the N-cycle has important agricultural and environmental implications, bacterial nitrogen metabolism has become a major research topic in recent years. Archaea are able to perform different reductive pathways of the N-cycle, including both assimilatory processes, such as nitrate assimilation and N 2 fixation, and dissimilatory reactions, such as nitrate respiration and denitrification. However, nitrogen metabolism is much less known in archaea than in bacteria. The availability of the complete genome sequences of several members of the eury-and crenarchaeota has enabled new approaches to the understanding of archaeal physiology and biochemistry, including metabolic reactions involving nitrogen compounds. Comparative studies reveal that significant differences exist in the structure and regulation of some enzymes involved in nitrogen metabolism in archaea, giving rise to important conclusions and new perspectives regarding the evolution, function and physiological relevance of the different N-cycle processes. This review discusses the advances that have been made in understanding nitrate reduction and other aspects of the inorganic nitrogen metabolism in archaea.

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“…In the eukaryotic microorganisms with denitrifying capability, CuNiR has been reported from the fungus Fusarium oxysporum (23). CuNiR has also been reported from the denitrifying halophilic archaeon Haloferax denitrificans (18). However, the gene structures of the fungal and the archaeal CuNiR have not been reported yet.…”

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confidence: 92%

Purification, Characterization, and Genetic Analysis of Cu-Containing Dissimilatory Nitrite Reductase from a Denitrifying Halophilic Archaeon, Haloarcula marismortui

et al. 2001

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Cu-containing dissimilatory nitrite reductase (CuNiR) was purified from denitrifying cells of a halophilic archaeon, Haloarcula marismortui. The purified CuNiR appeared blue in the oxidized state, possessing absorption peaks at 600 and 465 nm in the visible region. Electron paramagnetic resonance spectroscopy suggested the presence of type 1 Cu (g II ‫؍‬ 2.232; A II ‫؍‬ 4.4 mT) and type 2 Cu centers (g II ‫؍‬ 2.304; A II ‫؍‬ 13.3 mT) in the enzyme. The enzyme contained two subunits, whose apparent molecular masses were 46 and 42 kDa, according to sodium dodecyl sulfate-polyacrylamide gel electrophoresis. N-terminal amino acid sequence analysis indicated that the two subunits were identical, except that the 46-kDa subunit was 16 amino acid residues longer than the 42-kDa subunit in the N-terminal region. A nirK gene encoding the CuNiR was cloned and sequenced, and the deduced amino acid sequence with a residual length of 361 amino acids was homologous (30 to 41%) with bacterial counterparts. Cu-liganding residues His-133, Cys-174, His-182, and Met-187 (for type 1 Cu) and His-138, His-173, and His-332 (for type 2 Cu) were conserved in the enzyme. As generally observed in the halobacterial enzymes, the enzymatic activity of the purified CuNiR was enhanced during increasing salt concentration and reached its maximum in the presence of 2 M NaCl with the value of 960 M NO 2 ؊ ⅐ min ؊1 ⅐ mg ؊1 .

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The Purification and Properties of a Copper Nitrite Reductase from Haloferax denitrificans

Cited by 48 publications

References 14 publications

Anaerobic Metabolism in Haloferax Genus

Anaerobic Metabolism in Haloferax Genus

Nitrate reduction and the nitrogen cycle in archaea

Purification, Characterization, and Genetic Analysis of Cu-Containing Dissimilatory Nitrite Reductase from a Denitrifying Halophilic Archaeon, Haloarcula marismortui

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