scholarly journals Conversion of Nitric Oxide to Nitrous Oxide: Structure and Function of Nitric Oxide Reductase

2004 ◽  
Vol 44 (4) ◽  
pp. 155-160
Author(s):  
Hideyuki KUMITA ◽  
Yoshitsugu SHIRO
Keyword(s):  
Nitric Oxide ◽  
Nitrous Oxide ◽  
Structure And Function ◽  
Nitric Oxide Reductase ◽  
Oxide Structure ◽  
And Function

scholarly journals Molecular structure and function of bacterial nitric oxide reductase

2012 ◽  
Vol 1817 (4) ◽  
pp. 680-687 ◽  
Author(s):  
Tomoya Hino ◽  
Shingo Nagano ◽  
Hiroshi Sugimoto ◽  
Takehiko Tosha ◽  
Yoshitsugu Shiro
Keyword(s):  
Molecular Structure ◽  
Nitric Oxide ◽  
Structure And Function ◽  
Nitric Oxide Reductase ◽  
And Function ◽  
Molecular Structure And Function

Structure and Function of the Rat Basilar Artery During Chronic Nitric Oxide Synthase Inhibition

Stroke ◽  
1995 ◽  
Vol 26 (10) ◽  
pp. 1922-1929 ◽  
Author(s):  
Pierre Moreau ◽  
Hiroyuki Takase ◽  
Christoph F. Küng ◽  
Menno-M. van Rooijen ◽  
Thomas Schaffner ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Nitric Oxide Synthase ◽  
Basilar Artery ◽  
Structure And Function ◽  
And Function ◽  
Oxide Synthase

scholarly journals Analysis of multiple haloarchaeal genomes suggests that the quinone-dependent respiratory nitric oxide reductase is an important source of nitrous oxide in hypersaline environments

2017 ◽  
Vol 9 (6) ◽  
pp. 788-796 ◽  
Author(s):  
Javier Torregrosa-Crespo ◽  
Pedro González-Torres ◽  
Vanesa Bautista ◽  
Julia M. Esclapez ◽  
Carmen Pire ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Nitrous Oxide ◽  
Nitric Oxide Reductase ◽  
Hypersaline Environments

Effect of ionophores on denitrification inFlexibacter canadensis

1995 ◽  
Vol 41 (3) ◽  
pp. 227-234 ◽  
Author(s):  
Qitu Wu ◽  
Roger Knowles ◽  
Donald F. Niven
Keyword(s):  
Nitric Oxide ◽  
Nitrous Oxide ◽  
Proton Motive Force ◽  
Nitrate Transport ◽  
Nitric Oxide Reductase ◽  
Anaerobic Conditions ◽  
Intact Cells ◽  
Nitrite Production ◽  
Carbonyl Cyanide ◽  
No Consumption

Denitrification by Flexibacter canadensis was investigated by measuring the production and (or) consumption of nitrite, nitric oxide (NO), and nitrous oxide (N2O) under anaerobic conditions. Carbonyl cyanide m-chlorophenylhydrazone (CCCP), carbonyl cyanide p-trifluoromethoxyphenylhydrazone (FCCP), 2,4-dinitrophenol, and nigericin, but not valinomycin-K+inhibited the production of nitrite and N2O from nitrate by intact cells. However, CCCP, FCCP, 2,4-dinitrophenol, nigericin, and valinomycin-K+did not affect nitrite production from nitrate by cell-free extracts. These results suggest that nitrate transport was dependent on the transmembrane pH gradient but not on the membrane potential. CCCP, FCCP, and nigericin but not 2,4-dinitrophenol and valinomycin-K+caused NO accumulation during the reduction of nitrite, and also inhibited NO consumption and N2O production from nitrite by intact cells. These results preclude an explanation for NO accumulation based on the collapse of the proton motive force by ionophores, and imply that CCCP, FCCP, and nigericin perhaps dissociated a nitrite reductase–nitric oxide reductase complex, and (or) inhibited nitric oxide reductase specifically. 2,4-Dinitrophenol and CCCP did not inhibit the reduction of N2O to dinitrogen. Addition of ≤ 1.16 μM dissolved NO did not affect the production of nitrite from nitrate, or the disappearance of nitrite or N2O. The rate of NO consumption was linear with concentrations of dissolved NO up to 67 nM. Above 67 nM NO, NO consumption was inhibited, suggesting that NO is toxic to nitric oxide reductase.Key words: ionophores, denitrification, nitric oxide, Flexibacter canadensis.

scholarly journals Determining Roles of Accessory Genes in Denitrification by Mutant Fitness Analyses

2015 ◽  
Vol 82 (1) ◽  
pp. 51-61 ◽  
Author(s):  
Brian J. Vaccaro ◽  
Michael P. Thorgersen ◽  
W. Andrew Lancaster ◽  
Morgan N. Price ◽  
Kelly M. Wetmore ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Nitrous Oxide ◽  
Electron Acceptor ◽  
Pseudomonas Stutzeri ◽  
Basic Function ◽  
Nitric Oxide Reductase ◽  
Content Type ◽  
Nitric Oxide Release ◽  
Peripheral Proteins ◽  
Cofactor Biosynthesis

ABSTRACTEnzymes of the denitrification pathway play an important role in the global nitrogen cycle, including release of nitrous oxide, an ozone-depleting greenhouse gas. In addition, nitric oxide reductase, maturation factors, and proteins associated with nitric oxide detoxification are used by pathogens to combat nitric oxide release by host immune systems. While the core reductases that catalyze the conversion of nitrate to dinitrogen are well understood at a mechanistic level, there are many peripheral proteins required for denitrification whose basic function is unclear. A bar-coded transposon DNA library fromPseudomonas stutzeristrain RCH2 was grown under denitrifying conditions, using nitrate or nitrite as an electron acceptor, and also under molybdenum limitation conditions, with nitrate as the electron acceptor. Analysis of sequencing results from these growths yielded gene fitness data for 3,307 of the 4,265 protein-encoding genes present in strain RCH2. The insights presented here contribute to our understanding of how peripheral proteins contribute to a fully functioning denitrification pathway. We propose a new low-affinity molybdate transporter, OatABC, and show that differential regulation is observed for two MoaA homologs involved in molybdenum cofactor biosynthesis. We also propose that NnrS may function as a membrane-bound NO sensor. The dominant HemN paralog involved in heme biosynthesis is identified, and a CheR homolog is proposed to function in nitrate chemotaxis. In addition, new insights are provided into nitrite reductase redundancy, nitric oxide reductase maturation, nitrous oxide reductase maturation, and regulation.

scholarly journals Structural basis for nitrous oxide generation by bacterial nitric oxide reductases

2012 ◽  
Vol 367 (1593) ◽  
pp. 1195-1203 ◽  
Author(s):  
Yoshitsugu Shiro ◽  
Hiroshi Sugimoto ◽  
Takehiko Tosha ◽  
Shingo Nagano ◽  
Tomoya Hino
Keyword(s):  
Nitric Oxide ◽  
Nitrous Oxide ◽  
Structural Basis ◽  
Nitric Oxide Reductase ◽  
Respiratory Enzymes ◽  
Functional Differences ◽  
Cytochrome Oxidases ◽  
Structural Differences ◽  
Nitric Oxide Reduction ◽  
Copper Oxidase

The crystal structure of the bacterial nitric oxide reductase (cNOR) from Pseudomonas aeruginosa is reported. Its overall structure is similar to those of the main subunit of aerobic and micro-aerobic cytochrome oxidases (COXs), in agreement with the hypothesis that all these enzymes are members of the haem-copper oxidase superfamily. However, substantial structural differences between cNOR and COX are observed in the catalytic centre and the delivery pathway of the catalytic protons, which should be reflected in functional differences between these respiratory enzymes. On the basis of the cNOR structure, we propose a possible reaction mechanism of nitric oxide reduction to nitrous oxide as a working hypothesis.

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