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Interaction of CO Dehydrogenase with the Cytoplasmic Membrane Monitored by Fluorescence Correlation Spectroscopy
Author(s) -
Spreitler Florian,
Brock Christian,
Pelzmann Astrid,
Meyer Ortwin,
Köhler Jürgen
Publication year - 2010
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201000431
Subject(s) - membrane , cytoplasm , chemistry , carbon monoxide dehydrogenase , enzyme , fluorescence spectroscopy , fluorescence correlation spectroscopy , fluorescence , biochemistry , spectroscopy , carbon monoxide , biophysics , biology , molecule , organic chemistry , catalysis , physics , quantum mechanics
We have investigated the interaction of carbon monoxide dehydrogenase (CODH), an enzyme that catalyses the oxidation of CO in the aerobic eubacterium Oligotropha carboxidovorans , with the cytoplasmic membrane by using fluorescence correlation spectroscopy (FCS). Our results reveal that in vitro this interaction of CODH is specific for cytoplasmic membranes from CO‐grown bacteria.