scholarly journals Crystal structure of C-terminal desundecapeptide nitrite reductase from Achromobacter cycloclastes

2005 ◽  
Vol 338 (4) ◽  
pp. 1935-1942 ◽  
Author(s):  
Hai-Tao Li ◽  
Tschining Chang ◽  
Wen-Chang Chang ◽  
Chung-Jung Chen ◽  
Ming-Yih Liu ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Nitrite Reductase ◽  
Achromobacter Cycloclastes

scholarly journals pH-profile crystal structure studies of C-terminal despentapeptide nitrite reductase from Achromobacter cycloclastes

2004 ◽  
Vol 316 (1) ◽  
pp. 107-113 ◽  
Author(s):  
Hai-Tao Li ◽  
Chao Wang ◽  
Tschining Chang ◽  
Wen-Chang Chang ◽  
Ming-Yih Liu ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Nitrite Reductase ◽  
Ph Profile ◽  
Achromobacter Cycloclastes

scholarly journals Cytochrome c nitrite reductase from the bacterium Geobacter lovleyi represents a new NrfA subclass

2020 ◽  
Vol 295 (33) ◽  
pp. 11455-11465 ◽  
Author(s):  
Julius Campeciño ◽  
Satyanarayana Lagishetty ◽  
Zdzislaw Wawrzak ◽  
Victor Sosa Alfaro ◽  
Nicolai Lehnert ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Nitrite Reductase ◽  
Nitrate Reduction ◽  
Convergent Evolution ◽  
Nutrient Loss ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Cytochrome C Nitrite Reductase ◽  
Environmental Bacterium ◽  
Key Driver

Cytochrome c nitrite reductase (NrfA) catalyzes the reduction of nitrite to ammonium in the dissimilatory nitrate reduction to ammonium (DNRA) pathway, a process that competes with denitrification, conserves nitrogen, and minimizes nutrient loss in soils. The environmental bacterium Geobacter lovleyi has recently been recognized as a key driver of DNRA in nature, but its enzymatic pathway is still uncharacterized. To address this limitation, here we overexpressed, purified, and characterized G. lovleyi NrfA. We observed that the enzyme crystallizes as a dimer but remains monomeric in solution. Importantly, its crystal structure at 2.55-Å resolution revealed the presence of an arginine residue in the region otherwise occupied by calcium in canonical NrfA enzymes. The presence of EDTA did not affect the activity of G. lovleyi NrfA, and site-directed mutagenesis of this arginine reduced enzymatic activity to <3% of the WT levels. Phylogenetic analysis revealed four separate emergences of Arg-containing NrfA enzymes. Thus, the Ca2+-independent, Arg-containing NrfA from G. lovleyi represents a new subclass of cytochrome c nitrite reductase. Most genera from the exclusive clades of Arg-containing NrfA proteins are also represented in clades containing Ca2+-dependent enzymes, suggesting convergent evolution.

scholarly journals Laue crystal structure of Shewanella oneidensis cytochrome c nitrite reductase from a high-yield expression system

2012 ◽  
Vol 17 (4) ◽  
pp. 647-662 ◽  
Author(s):  
Matthew Youngblut ◽  
Evan T. Judd ◽  
Vukica Srajer ◽  
Bilal Sayyed ◽  
Tyler Goelzer ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Cytochrome C ◽  
Nitrite Reductase ◽  
Expression System ◽  
Shewanella Oneidensis ◽  
High Yield ◽  
Cytochrome C Nitrite Reductase

Crystal structure of a NO-forming nitrite reductase mutant: an analog of a transition state in enzymatic reaction

2003 ◽  
Vol 302 (3) ◽  
pp. 568-574 ◽  
Author(s):  
Sheng-Quan Liu ◽  
Tschining Chang ◽  
Ming-Yih Liu ◽  
Jean LeGall ◽  
Wen-Chang Chang ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Transition State ◽  
Nitrite Reductase ◽  
Enzymatic Reaction
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