Probing the nitrite and nitric oxide reductase activity of cbb3 oxidase: resonance Raman detection of a six-coordinate ferrous heme–nitrosyl species in the binuclear b3/CuB center

2015 ◽  
Vol 51 (98) ◽  
pp. 17398-17401 ◽  
Author(s):  
Andreas Loullis ◽  
Eftychia Pinakoulaki
Keyword(s):  
Nitric Oxide ◽  
Nitrous Oxide ◽  
Reductase Activity ◽  
Resonance Raman ◽  
Nitric Oxide Reductase ◽  
Ferrous Heme

We present resonance Raman and FTIR evidence for the reduction of nitrite to nitrous oxide by cbb3 oxidase through the formation of a ferrous six-coordinate heme b3–nitrosyl species.

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

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

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

Unique Binding of Nitric Oxide to Ferric Nitric Oxide Reductase fromFusarium oxysporumElucidated with Infrared, Resonance Raman, and X-ray Absorption Spectroscopies

1997 ◽  
Vol 119 (33) ◽  
pp. 7807-7816 ◽  
Author(s):  
Eiji Obayashi ◽  
Koki Tsukamoto ◽  
Shin-ichi Adachi ◽  
Satoshi Takahashi ◽  
Masaharu Nomura ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Resonance Raman ◽  
Nitric Oxide Reductase ◽  
X Ray ◽  
X Ray Absorption

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 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 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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