Robustness of nitric oxide detoxification to nitrogen starvation in Escherichia coli requires RelA

Author(s):  
Xuanqing Wan ◽  
Mark P. Brynildsen
2002 ◽  
Vol 184 (16) ◽  
pp. 4640-4643 ◽  
Author(s):  
Matthew I. Hutchings ◽  
Neeraj Mandhana ◽  
Stephen Spiro

ABSTRACT The Escherichia coli norVW genes encode a flavorubredoxin and NADH:(flavo)rubredoxin reductase, respectively, which are involved in nitric oxide detoxification under anaerobic growth conditions. Here it is shown that the norVW genes also have a role in protection against reactive nitrogen intermediates generated from nitroprusside. Transcription from the norV promoter is activated by the presence of nitroprusside in the growth medium; activation requires the product of a divergently transcribed regulatory gene, norR.


2021 ◽  
Vol 14 (1) ◽  
Author(s):  
Darshan M. Sivaloganathan ◽  
Mark P. Brynildsen

Abstract Objective Bacteria are exposed to multiple concurrent antimicrobial stressors within phagosomes. Among the antimicrobials produced, hydrogen peroxide and nitric oxide are two of the most deleterious products. In a previous study, we discovered that when faced with both stressors simultaneously, Escherichia coli prioritized detoxification of hydrogen peroxide over nitric oxide. In this study, we investigated whether such a process was conserved in another bacterium, Pseudomonas aeruginosa. Results P. aeruginosa prioritized hydrogen peroxide detoxification in a dose-dependent manner. Specifically, hydrogen peroxide detoxification was unperturbed by the presence of nitric oxide, whereas larger doses of hydrogen peroxide produced longer delays in nitric oxide detoxification. Computational modelling revealed that the rate of nitric oxide consumption in co-treated cultures was biphasic, with cells entering the second phase of detoxification only after hydrogen peroxide was eliminated from the culture.


2010 ◽  
Vol 431 (1) ◽  
pp. 73-80 ◽  
Author(s):  
Gemma L. Kemp ◽  
Thomas A. Clarke ◽  
Sophie J. Marritt ◽  
Colin Lockwood ◽  
Susannah R. Poock ◽  
...  

NrfA is a pentahaem cytochrome present in a wide-range of γ-, δ- and ε-proteobacteria. Its nitrite and nitric oxide reductase activities have been studied extensively and contribute to respiratory nitrite ammonification and nitric oxide detoxification respectively. Sulfite is a third substrate for NrfA that may be encountered in the micro-oxic environments where nrfA is expressed. Consequently, we have performed quantitative kinetic and thermodynamic studies of the interactions between sulfite and Escherichia coli NrfA to provide a biochemical framework from which to consider their possible cellular consequences. A combination of voltammetric, spectroscopic and crystallographic analyses define dissociation constants for sulfite binding to NrfA in oxidized (~54 μM), semi-reduced (~145 μM) and reduced (~180 μM) states that are comparable with each other, and the Km (~70 μM) for sulfite reduction at pH 7. Under comparable conditions Km values of ~22 and ~300 μM describe nitrite and nitric oxide reduction respectively, whereas the affinities of nitrate and thiocyanate for NrfA fall more than 50-fold on enzyme reduction. These results are discussed in terms of the nature of sulfite co-ordination within the active site of NrfA and their implications for the cellular activity of NrfA.


Nitric Oxide ◽  
2006 ◽  
Vol 14 (4) ◽  
pp. 17-18
Author(s):  
Lovisa Svensson ◽  
Britt-Inger Marklund ◽  
Mirjana Poljakovic ◽  
Katarina Persson

FEBS Journal ◽  
2006 ◽  
Vol 274 (3) ◽  
pp. 677-686 ◽  
Author(s):  
João B. Vicente ◽  
Francesca M. Scandurra ◽  
João V. Rodrigues ◽  
Maurizio Brunori ◽  
Paolo Sarti ◽  
...  

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