A Flavodiiron Protein and High Molecular Weight Rubredoxin fromMoorella thermoaceticawith Nitric Oxide Reductase Activity†

Biochemistry ◽  
2003 ◽  
Vol 42 (10) ◽  
pp. 2806-2815 ◽  
Author(s):  
Radu Silaghi-Dumitrescu ◽  
Eric D. Coulter ◽  
Amaresh Das ◽  
Lars G. Ljungdahl ◽  
Guy N. L. Jameson ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Molecular Weight ◽  
High Molecular Weight ◽  
Reductase Activity ◽  
Nitric Oxide Reductase

Detergent inhibition of nitric-oxide reductase activity

1987 ◽  
Vol 911 (3) ◽  
pp. 334-340 ◽  
Author(s):  
J.P. Shapleigh ◽  
K.J.P. Davies ◽  
W.J. Payne
Keyword(s):  
Nitric Oxide ◽  
Reductase Activity ◽  
Nitric Oxide Reductase

Nitric oxide production by high molecular weight water-soluble chitosan via nuclear factor-κB activation

2000 ◽  
Vol 22 (11) ◽  
pp. 923-933 ◽  
Author(s):  
Hyun-Ja Jeong ◽  
Hyun-Na Koo ◽  
Eun-Young Oh ◽  
Han-Jung Chae ◽  
Hyung-Ryong Kim ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Molecular Weight ◽  
High Molecular Weight ◽  
Nuclear Factor Κb ◽  
Water Soluble ◽  
Nitric Oxide Production ◽  
Nuclear Factor ◽  
Oxide Production

scholarly journals Introducing a 2-His-1-Glu Nonheme Iron Center into Myoglobin Confers Nitric Oxide Reductase Activity

2010 ◽  
Vol 132 (29) ◽  
pp. 9970-9972 ◽  
Author(s):  
Ying-Wu Lin ◽  
Natasha Yeung ◽  
Yi-Gui Gao ◽  
Kyle D. Miner ◽  
Lanyu Lei ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Reductase Activity ◽  
Nonheme Iron ◽  
Nitric Oxide Reductase ◽  
Iron Center

scholarly journals Nitric Oxide Reductase Activity in Heme–Nonheme Binuclear Engineered Myoglobins through a One-Electron Reduction Cycle

2018 ◽  
Vol 140 (50) ◽  
pp. 17389-17393 ◽  
Author(s):  
Sinan Sabuncu ◽  
Julian H. Reed ◽  
Yi Lu ◽  
Pierre Moënne-Loccoz
Keyword(s):  
Nitric Oxide ◽  
Reductase Activity ◽  
Nitric Oxide Reductase ◽  
Reduction Cycle ◽  
Electron Reduction

scholarly journals Activity of Chitosan and Its Derivatives against Leishmania major and Leishmania mexicana In Vitro

2019 ◽  
Vol 64 (3) ◽  
Author(s):  
Alaa Riezk ◽  
John G. Raynes ◽  
Vanessa Yardley ◽  
Sudaxshina Murdan ◽  
Simon L. Croft
Keyword(s):  
Nitric Oxide ◽  
Reactive Oxygen Species ◽  
Molecular Weight ◽  
High Molecular Weight ◽  
Leishmania Major ◽  
Oxygen Species ◽  
Leishmania Mexicana ◽  
Content Type ◽  
High Molecular Weight Chitosan

ABSTRACT There is an urgent need for safe, efficacious, affordable, and field-adapted drugs for the treatment of cutaneous leishmaniasis, which newly affects around 1.5 million people worldwide annually. Chitosan, a biodegradable cationic polysaccharide, has previously been reported to have antimicrobial, antileishmanial, and immunostimulatory activities. We investigated the in vitro activity of chitosan and several of its derivatives and showed that the pH of the culture medium plays a critical role in antileishmanial activity of chitosan against both extracellular promastigotes and intracellular amastigotes of Leishmania major and Leishmania mexicana. Chitosan and its derivatives were approximately 7 to 20 times more active at pH 6.5 than at pH 7.5, with high-molecular-weight chitosan being the most potent. High-molecular-weight chitosan stimulated the production of nitric oxide and reactive oxygen species by uninfected and Leishmania-infected macrophages in a time- and dose-dependent manner at pH 6.5. Despite the in vitro activation of bone marrow macrophages by chitosan to produce nitric oxide and reactive oxygen species, we showed that the antileishmanial activity of chitosan was not mediated by these metabolites. Finally, we showed that rhodamine-labeled chitosan is taken up by pinocytosis and accumulates in the parasitophorous vacuole of Leishmania-infected macrophages.

scholarly journals Identification, Functional Studies, and Genomic Comparisons of New Members of the NnrR Regulon in Rhodobacter sphaeroides

2009 ◽  
Vol 192 (4) ◽  
pp. 903-911 ◽  
Author(s):  
Angela Hartsock ◽  
James P. Shapleigh
Keyword(s):  
Nitric Oxide ◽  
Rhodobacter Sphaeroides ◽  
Nitrite Reductase ◽  
Reductase Activity ◽  
Nitrite Reduction ◽  
No Production ◽  
Nitric Oxide Reductase ◽  
New Members ◽  
Functional Studies ◽  
The Status

ABSTRACT Analysis of the Rhodobacter sphaeroides 2.4.3 genome revealed four previously unidentified sequences similar to the binding site of the transcriptional regulator NnrR. Expression studies demonstrated that three of these sequences are within the promoters of genes, designated paz, norEF, and cdgA, in the NnrR regulon, while the status of the fourth sequence, within the tat operon promoter, remains uncertain. nnrV, under control of a previously identified NnrR site, was also identified. paz encodes a pseudoazurin that is a donor of electrons to nitrite reductase. paz inactivation did not decrease nitrite reductase activity, but loss of pseudoazurin and cytochrome c2 together reduced nitrite reduction. Inactivation of norEF reduced nitrite and nitric oxide reductase activity and increased the sensitivity to nitrite in a taxis assay. This suggests that loss of norEF increases NO production as a result of decreased nitric oxide reductase activity. 2.4.3 is the only strain of R. sphaeroides with norEF, even though all four of the strains whose genomes have been sequenced have the norCBQD operon and nnrR. norEF was shown to provide resistance to nitrite when it was mobilized into R. sphaeroides strain 2.4.1 containing nirK. Inactivation of the other identified genes did not reveal any detectable denitrification-related phenotype. The distribution of members of the NnrR regulon in R. sphaeroides revealed patterns of coselection of structural genes with the ancillary genes identified here. The strong coselection of these genes indicates their functional importance under real-world conditions, even though inactivation of the majority of them does not impact denitrification under laboratory conditions.

scholarly journals Characterization of the norB Gene, Encoding Nitric Oxide Reductase, in the Nondenitrifying Cyanobacterium Synechocystis sp. Strain PCC6803

2002 ◽  
Vol 68 (2) ◽  
pp. 668-672 ◽  
Author(s):  
Andrea B�sch ◽  
B�rbel Friedrich ◽  
Rainer Cramm
Keyword(s):  
Nitric Oxide ◽  
Reductase Activity ◽  
Nitric Oxide Reductase ◽  
Wild Type ◽  
Gene Encoding ◽  
Single Subunit ◽  
Transcriptional Fusions ◽  
Synechocystis Sp ◽  
Negative Mutant

ABSTRACT A norB gene encoding a putative nitric oxide reductase is present in the genome of the nondenitrifying cyanobacterium Synechocystis sp. strain PCC6803. The gene product belongs to the quinol-oxidizing single-subunit class of nitric oxide reductases, discovered recently in the denitrifier Ralstonia eutropha. Heterologous complementation of a nitric oxide reductase-negative mutant of R. eutropha with norB from Synechocystis restored nitric oxide reductase activity. With reduced menadione as the electron donor, an enzymatic activity of 101 nmol of NO per min per mg of protein was obtained with membrane fractions of Synechocystis wild-type cells. Virtually no nitric oxide reductase activity was present in a norB-negative mutant of Synechocystis. Growing cells of this mutant are more sensitive toward NO than wild-type cells, indicating that the presence of a nitric oxide reductase is beneficial for Synechocystis when the cells are exposed to NO. Transcriptional fusions with the chloramphenicol acetyltransferase reporter gene were constructed to monitor norB expression in Synechocystis. Transcription of norB was not enhanced by the addition of the NO-generating agent sodium nitroprusside.

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