Open AccessThe redox centers in the molybdo iron‐sulfur flavoprotein CO dehydrogenase from the thermophilic carboxidotrophic bacterium Pseudomonas thermocarboxydovorans
Author(s) -
Hänzelmann Petra,
Hofmann Bettina,
Meisen Sabine,
Meyer Ortwin
Publication year - 1999
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 - 10.1111/j.1574-6968.1999.tb13654.x
Subject(s) - flavoprotein , cofactor , chemistry , redox , electron paramagnetic resonance , sulfur , thermophile , stereochemistry , biochemistry , inorganic chemistry , enzyme , organic chemistry , nuclear magnetic resonance , physics
The redox centers in the molybdo iron‐sulfur flavoprotein CO dehydrogenase from the thermophilic bacterium Pseudomonas thermocarboxydovorans were identified and characterized by electron paramagnetic resonance (EPR). One mol of the 279‐kDa dimer contained 1.9 mol of Mo, 2.2 mol of FAD, 6.9 mol of Fe and 6.7 mol of labile sulfide. The molybdenum cofactor is composed of a 1:1 mononuclear complex of molybdopterin‐cytosine dinucleotide and the Mo ion. EPR spectroscopy revealed signals typical for Mo(V), FADH • , and type I and type II [2Fe‐2S] centers.