Effects of freezing on purified nitrite reductase from a denitrifier, Alcaligenes sp. NCIB 11015.

Abstract:

:The effects of freezing on Alcaligenes sp. nitrite reductase [nitric-oxide: ferricytochrome c oxidoreductase, EC 1.7.2.1] dissolved in sodium phosphate (pH 7.2) were investigated. The nitrite reductase was gradually activated with time in the frozen state, resulting in an increase in its activity of 2.5-4.5 times. The final freezing temperature influenced the enzyme activation, maximal activation being observed at around -20 degrees C. All the enzymatic activities that the nitrite reductase is known to catalyze were enhanced by freeze-thawing. The activation was followed by neither association-dissociation nor any gross conformational change of the enzyme molecule, but was accompanied by an increase in the fluorescence intensity of 2-p-toluidinonaphthalene-6-sulfonate used as a hydrophobic probe. The results are consistent with the hypothesis that the activation of the NiR is due to a limited conformational change of the enzyme molecule, particularly in the hydrophobic region. The mechanism of the activation of NiR by freeze-thawing is discussed, in comparison with the mechanisms of inactivation by freeze-thawing of many enzymes reported by previous workers.

journal_name

J Biochem

journal_title

Journal of biochemistry

authors

Masuko M,Iwasaki H,Sakurai T,Suzuki S,Nakahara A

doi

10.1093/oxfordjournals.jbchem.a135395

subject

Has Abstract

pub_date

1985-11-01 00:00:00

pages

1285-91

issue

5

eissn

0021-924X

issn

1756-2651

journal_volume

98

pub_type

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