Ammonia-Forming, Dissimilatory Nitrite Reductases as a Homologous Group of Hexaheme C-Type Cytochromes in Metabolically Diverse Bacteria

Author(s):  
Ming-Cheh Liu ◽  
Harry D. Peck
Genes ◽  
2020 ◽  
Vol 11 (11) ◽  
pp. 1308
Author(s):  
Mercedes Sánchez-Costa ◽  
Alba Blesa ◽  
José Berenguer

Genes coding for enzymes of the denitrification pathway appear randomly distributed among isolates of the ancestral genus Thermus, but only in few strains of the species Thermus thermophilus has the pathway been studied to a certain detail. Here, we review the enzymes involved in this pathway present in T. thermophilus NAR1, a strain extensively employed as a model for nitrate respiration, in the light of its full sequence recently assembled through a combination of PacBio and Illumina technologies in order to counteract the systematic errors introduced by the former technique. The genome of this strain is divided in four replicons, a chromosome of 2,021,843 bp, two megaplasmids of 370,865 and 77,135 bp and a small plasmid of 9799 pb. Nitrate respiration is encoded in the largest megaplasmid, pTTHNP4, within a region that includes operons for O2 and nitrate sensory systems, a nitrate reductase, nitrate and nitrite transporters and a nitrate specific NADH dehydrogenase, in addition to multiple insertion sequences (IS), suggesting its mobility-prone nature. Despite nitrite is the final product of nitrate respiration in this strain, the megaplasmid encodes two putative nitrite reductases of the cd1 and Cu-containing types, apparently inactivated by IS. No nitric oxide reductase genes have been found within this region, although the NorR sensory gene, needed for its expression, is found near the inactive nitrite respiration system. These data clearly support that partial denitrification in this strain is the consequence of recent deletions and IS insertions in genes involved in nitrite respiration. Based on these data, the capability of this strain to transfer or acquire denitrification clusters by horizontal gene transfer is discussed.


1993 ◽  
Vol 236-236 (2-3) ◽  
pp. 203-208 ◽  
Author(s):  
Jocelyne Kronenberger ◽  
Andrée Lepingle ◽  
Michel Caboche ◽  
Hervé Vaucheret

2008 ◽  
Vol 36 (6) ◽  
pp. 1155-1159 ◽  
Author(s):  
Serena Rinaldo ◽  
Alessandro Arcovito ◽  
Giorgio Giardina ◽  
Nicoletta Castiglione ◽  
Maurizio Brunori ◽  
...  

The cytochrome cd1 nitrite reductases are enzymes that catalyse the reduction of nitrite to nitric oxide (NO) in the bacterial energy conversion denitrification process. These enzymes contain two different redox centres: one covalently bound c-haem, which is reduced by external donors, and one peculiar d1-haem, where catalysis occurs. In the present paper, we summarize the current understanding of the reaction of nitrite reduction in the light of the most recent results on the enzyme from Pseudomonas aeruginosa and discuss the differences between enzymes from different organisms. We have evidence that release of NO from the ferrous d1-haem occurs rapidly enough to be fully compatible with the turnover, in contrast with previous hypotheses, and that the substrate nitrite is able to displace NO from the d1-haem iron. These results shed light on the mechanistic details of the activity of cd1 nitrite reductases and on the biological role of the d1-haem, whose presence in this class of enzymes has to date been unexplained.


2018 ◽  
Vol 169 (6) ◽  
pp. 343-347 ◽  
Author(s):  
Lea Wittorf ◽  
Christopher M. Jones ◽  
Germán Bonilla-Rosso ◽  
Sara Hallin

2009 ◽  
Vol 284 (38) ◽  
pp. 25973-25983 ◽  
Author(s):  
Sibylle Brenner ◽  
Derren J. Heyes ◽  
Sam Hay ◽  
Michael A. Hough ◽  
Robert R. Eady ◽  
...  

2020 ◽  
Vol 11 (23) ◽  
pp. 5909-5921
Author(s):  
Sk Amanullah ◽  
Abhishek Dey

Ferrous nitrosyl {FeNO}7 species is an intermediate common to the catalytic cycles of Cd1NiR and CcNiR, two heme-based nitrite reductases (NiR), and its reactivity varies dramatically in these enzymes.


1982 ◽  
Vol 215 (1) ◽  
pp. 47-58 ◽  
Author(s):  
Russell Timkovich ◽  
Rahul Dhesi ◽  
Kazys J. Martinkus ◽  
Mary K. Robinson ◽  
Timothy M. Rea

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