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Redox modifications of spinach chloroplast fructose‐1,6‐bisphosphatase
Author(s) -
Chen Ye,
Xu Genjun
Publication year - 1996
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549600201092
Subject(s) - dithiothreitol , chemistry , thiol , fructose 1,6 bisphosphatase , reagent , enzyme , titration , benzoic acid , biochemistry , fructose , redox , chloroplast , reducing agent , tcep , organic chemistry , catalysis , phosphine , gene
Complete activation of chloroplast fructose‐1,6‐bisphosphatase by dithiothreitol involves the reduction of its four disulfide bonds as revealed by thiol titration and activity measurement. Both before and after reduction, the enzyme is inhibited by the thiol‐specific reagent 5,5′‐dithiobis (2‐nitrobenzoic acid) with complete inactivation upon modifications of the four accessible thiols. However, oxidative modification of the enzyme facillitates the reduction of the four mentioned disulfide bonds as the process of activation by DTT is accelerated.