scholarly journals Dissimilatory Nitrite Reductase Genes from Autotrophic Ammonia-Oxidizing Bacteria

2001 ◽  
Vol 67 (5) ◽  
pp. 2213-2221 ◽  
Author(s):  
Karen L. Casciotti ◽  
Bess B. Ward

ABSTRACT The presence of a copper-containing dissimilatory nitrite reductase gene (nirK) was discovered in several isolates of β-subdivision ammonia-oxidizing bacteria using PCR and DNA sequencing. PCR primers Cunir3 and Cunir4 were designed based on published nirK sequences from denitrifying bacteria and used to amplify a 540-bp fragment of the nirK gene fromNitrosomonas marina and five additional isolates of ammonia-oxidizing bacteria. Amplification products of the expected size were cloned and sequenced. Alignment of the nucleic acid and deduced amino acid (AA) sequences shows significant similarity (62 to 75% DNA, 58 to 76% AA) between nitrite reductases present in these nitrifiers and the copper-containing nitrite reductase found in classic heterotrophic denitrifiers. While the presence of a nitrite reductase in Nitrosomonas europaea is known from early biochemical work, preliminary sequence data from its genome indicate a rather low similarity to the denitrifier nirKs. Phylogenetic analysis of the partial nitrifier nirK sequences indicates that the topology of the nirK tree corresponds to the 16S rRNA andamoA trees. While the role of nitrite reduction in the metabolism of nitrifying bacteria is still uncertain, these data show that the nirK gene is present in closely related nitrifying isolates from many oceanographic regions and suggest thatnirK sequences retrieved from the environment may include sequences from ammonia-oxidizing bacteria.

2002 ◽  
Vol 68 (5) ◽  
pp. 2140-2147 ◽  
Author(s):  
Dong Yun Lee ◽  
Adela Ramos ◽  
Lee Macomber ◽  
James P. Shapleigh

ABSTRACT The taxis response of Rhodobacter sphaeroides 2.4.1 and 2.4.3, Rhodopseudomonas palustris, and Agrobacterium tumefaciens to nitrate and nitrite was evaluated by observing the macroscopic behavior of cells suspended in soft agar and incubated under various conditions. R. sphaeroides 2.4.3, which is capable of both nitrate and nitrite reduction, showed a taxis response to both nitrate and nitrite. R. sphaeroides 2.4.1, which contains nitrate reductase but not nitrite reductase, did not show a taxis response towards either nitrogen oxide. Insertional inactivation of the nitrite reductase structural gene or its transcriptional regulator, NnrR, in strain 2.4.3 caused a loss of a taxis response towards both nitrate and nitrite. An isolate of 2.4.1 carrying a copy of the nitrite reductase gene from 2.4.3 showed a taxis response to both nitrogen oxides. The taxis response of 2.4.3 was observed under anaerobic conditions, suggesting that the taxis response was due to nitrate and nitrite respiration, not to inhibition of oxygen respiration by respiration of nitrogen oxides. Strain 2.4.3 showed a taxis response to nitrate and nitrite under photosynthetic and aerobic conditions. Changing the carbon source in the culture medium caused an unexpected subtle shift in the taxis response of 2.4.3 to nitrite. A taxis response to nitrogen oxides was also observed in R. palustris and A. tumefaciens. R. palustris exhibited a taxis response to nitrite but not to nitrate, while A. tumefaciens exhibited a response to both compounds.


2011 ◽  
Vol 37 (8) ◽  
pp. 1406-1414
Author(s):  
Xiao-Yan SHI ◽  
Yan-Da ZENG ◽  
Shi-Long LI ◽  
Yu-Bo WANG ◽  
Feng-Ming MA ◽  
...  

1995 ◽  
Vol 177 (21) ◽  
pp. 6137-6143 ◽  
Author(s):  
I Suzuki ◽  
H Kikuchi ◽  
S Nakanishi ◽  
Y Fujita ◽  
T Sugiyama ◽  
...  

2009 ◽  
Vol 24 (1) ◽  
pp. 76
Author(s):  
Chie Katsuyama ◽  
Naho Kondo ◽  
Yuichi Suwa ◽  
Takao Yamagishi ◽  
Masayuki Itoh ◽  
...  

1983 ◽  
Vol 38 (11-12) ◽  
pp. 933-938 ◽  
Author(s):  
Michaela Preuß ◽  
Jobst-Heinrich Klemme

A dissimilatory nitrite reductase from the facultatively phototrophic bacterium , Rhodopseudomonas palustris strain 1a1 was studied. A basic level of the enzyme (10 -50 mU/mg protein) was measured in dark, aerated and anaerobic, photosynthetic cultures. A marked derepression of enzyme synthesis occurred under conditions of oxygen limitation (200-300 mU/mg protein). The addition of nitrite (or nitrate) to the culture medium had only a slight effect on the maximal nitrite reductase titer of cells. The enzyme was purified from photosynthetically grown cells by precipitation with ammonium sulfate, gel filtration through Sepharose 6B and repeated chromatography on DE 52-cellulose. As estimated by gel filtration, the nitrite reductase had a molecular weight of about 120 000 ± 12 000 and yielded only one band (mol. wt. of about 68 000 ± 7000) in SDS-gel electrophoresis. The isoelectric point of the enzyme was at pH 5.1. Nitric oxide (NO) was identified as the reaction product of nitrite reduction. The enzyme also exhibited cytochrome c-oxidase activity and was active with chemically reduced viologen dyes, FMN and cytochrome c as electron donors. Highly purified nitrite reductase preparations contained 10 mol% of a c-type cytochrome. Trace metal analyses indicated the presence of Cu in the enzyme. Consistent with the detection of Cu was the finding that the Cu-chelator, diethyldithiocarbamate, strongly inhibited the nitrite reductase


2017 ◽  
Vol 19 (3) ◽  
pp. 1189-1208 ◽  
Author(s):  
Sara Coyotzi ◽  
Andrew C. Doxey ◽  
Ian D. Clark ◽  
David R. Lapen ◽  
Philippe Van Cappellen ◽  
...  

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