Unknown

Dataset Information

0

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


ABSTRACT: 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.

SUBMITTER: Blackmore R 

PROVIDER: S-EPMC1153060 | biostudies-other | 1986 Jan

REPOSITORIES: biostudies-other

Similar Datasets

| S-EPMC1153061 | biostudies-other
| S-EPMC1149542 | biostudies-other
| S-EPMC1149576 | biostudies-other
| S-EPMC1149541 | biostudies-other
| S-EPMC208819 | biostudies-literature
| S-EPMC94697 | biostudies-literature
| S-EPMC3089676 | biostudies-literature
| PRJNA35271 | ENA
| S-EPMC27176 | biostudies-literature
| S-EPMC1409705 | biostudies-literature