Ca2+ stabilization of respiratory complex I from Escherichia coli
Author(s) -
Galina Belevich,
Nikolai Belevich,
Juho Knuuti,
Marina Verkhovskaya
Publication year - 2018
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1093/femsle/fny097
Subject(s) - chemistry , intracellular , oxidoreductase , escherichia coli , enzyme , biochemistry , biophysics , membrane , dilution , biology , physics , gene , thermodynamics
Stability of the membrane-bound and purified H+-translocating NADH:ubiquinone oxidoreductase, Complex I, was studied. The loss of the enzyme activity is strongly increased by alkaline pH and dilution of the sample. Complex I inactivation is prevented specifically by a low concentration of Ca2+ and/or an intracellular stabilization factor (ISF). The action of both, Ca2+ and ISF, on Complex I stability is interdependent. The data are discussed in terms of a release of structural Ca2+ as a reason for Complex I decay and an effect of ISF on the affinity and/or accessibility of Ca2+-binding site.
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