cytochrome c nitrite reductase
Recently Published Documents


TOTAL DOCUMENTS

43
(FIVE YEARS 4)

H-INDEX

18
(FIVE YEARS 0)

Biochemistry ◽  
2021 ◽  
Author(s):  
Shahid Shahid ◽  
Mahbbat Ali ◽  
Desiree Legaspi-Humiston ◽  
Jarett Wilcoxen ◽  
A. Andrew Pacheco




Biochemistry ◽  
2021 ◽  
Author(s):  
Victor Sosa Alfaro ◽  
Julius Campeciño ◽  
Matthew Tracy ◽  
Sean J. Elliott ◽  
Eric L. Hegg ◽  
...  


2020 ◽  
Vol 295 (33) ◽  
pp. 11455-11465 ◽  
Author(s):  
Julius Campeciño ◽  
Satyanarayana Lagishetty ◽  
Zdzislaw Wawrzak ◽  
Victor Sosa Alfaro ◽  
Nicolai Lehnert ◽  
...  

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.



2019 ◽  
Vol 141 (34) ◽  
pp. 13358-13371 ◽  
Author(s):  
Mahbbat Ali ◽  
Natalia Stein ◽  
Yingxi Mao ◽  
Shahid Shahid ◽  
Marius Schmidt ◽  
...  


Acta Naturae ◽  
2018 ◽  
Vol 10 (3) ◽  
pp. 48-56 ◽  
Author(s):  
T. N. Baymukhametov ◽  
Yu. M. Chesnokov ◽  
E. B. Pichkur ◽  
K. M. Boyko ◽  
T. V. Tikhonova ◽  
...  

The structure of cytochrome c nitrite reductase from the bacterium Thioalkalivibrio nitratireducens was determined by cryo-electron microscopy (cryo-EM) at a 2.56 resolution. Possible structural heterogeneity of the enzyme was assessed. The backbone and side-chain orientations in the cryo-EM-based model are, in general, similar to those in the high-resolution X-ray diffraction structure of this enzyme.





Sign in / Sign up

Export Citation Format

Share Document