Substrate Binding to a Nitrite Reductase Induces a Spin Transition

2010 ◽  
Vol 114 (16) ◽  
pp. 5563-5566 ◽  
Author(s):  
Gabriel Martins ◽  
Luisa Rodrigues ◽  
Filipa M. Cunha ◽  
Daniela Matos ◽  
Peter Hildebrandt ◽  
...  
Keyword(s):  
Nitrite Reductase ◽  
Substrate Binding ◽  
Spin Transition

The nature of the substrate binding site in copper nitrite reductase from Achromobacter xylosoxidans (AxNiR)

1995 ◽  
Vol 59 (2-3) ◽  
pp. 711
Author(s):  
R.W. Strange ◽  
J.G. Grossmann ◽  
F.E. Dodd ◽  
S.S. Hasnain ◽  
Z.H.L. Abraham ◽  
...  
Keyword(s):  
Binding Site ◽  
Nitrite Reductase ◽  
Substrate Binding ◽  
Achromobacter Xylosoxidans ◽  
Substrate Binding Site

The substrate-binding site in Cu nitrite reductase and its similarity to Zn carbonic anhydrase

1995 ◽  
Vol 2 (4) ◽  
pp. 287-292 ◽  
Author(s):  
Richard W. Strange ◽  
Fraser E. Dodd ◽  
Zelda H.L. Abraham ◽  
J. Günter Grossmann ◽  
Thomas Brüser ◽  
...  
Keyword(s):  
Carbonic Anhydrase ◽  
Binding Site ◽  
Nitrite Reductase ◽  
Substrate Binding ◽  
Substrate Binding Site

scholarly journals The purification and some equilibrium properties of the nitrite reductase of the bacterium Wolinella succinogenes

1986 ◽  
Vol 233 (2) ◽  
pp. 547-552 ◽  
Author(s):  
R Blackmore ◽  
A M Roberton ◽  
T Brittain
Keyword(s):  
High Spin ◽  
Nitrite Reductase ◽  
Reductase Activity ◽  
Spin Transition ◽  
Spectral Characteristics ◽  
High Yield ◽  
Wolinella Succinogenes ◽  
Hydrophobic Binding ◽  
Nitrite Reductase Activity ◽  
Oxygen Reductase

The bacterium Wolinella succinogenes produces a nitrite reductase enzyme that can be purified to homogeneity in high yield by a combination of detergent extraction, hydroxyapatite chromatography and Mr fractionation. Nitrite reductase activity is found to be present in both a high- and a low-Mr fraction. The high-Mr fraction has been shown to consist of the low-Mr nitrite reductase enzyme associated with a hydrophobic ‘binding protein’. The amino acid composition for both proteins is reported. The nitrite reductase enzyme shows spectral characteristics indicative of the presence of c-type haem groups. Measurements at 610 nm indicate the presence of some high-spin haem groups at neutral pH. This haem subgroup undergoes a pH-linked high-spin - low-spin transition at alkaline pH. Approximately two of the six haem groups present within the enzyme bind CO with low affinity (KD = 0.4 mM). The enzyme also shows a range of redox activities with various inorganic reagents. The enzyme has been shown to exhibit dithionite reductase, oxygen reductase and CO2 reductase activities.

Insights into Redox Partner Interactions and Substrate Binding in Nitrite Reductase fromAlcaligenes xylosoxidans: Crystal Structures of the Trp138His and His313Gln Mutants†,‡

Biochemistry ◽  
2004 ◽  
Vol 43 (51) ◽  
pp. 16311-16319 ◽  
Author(s):  
Mark L. Barrett ◽  
Roger L. Harris ◽  
Svetlana Antonyuk ◽  
Michael A. Hough ◽  
Mark J. Ellis ◽  
...  
Keyword(s):  
Crystal Structures ◽  
Nitrite Reductase ◽  
Substrate Binding ◽  
Redox Partner
Sign in / Sign up

Export Citation Format

Share Document