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Biochemistry. 2008 Mar 25;47(12):3770-6. doi: 10.1021/bi702444r. Epub 2008 Feb 26.

Thermodynamic characterization of the redox centers within dimethylsulfide dehydrogenase.

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School of Molecular and Microbial Sciences and Centre for Metals in Biology, University of Queensland, Brisbane 4072, Australia.


Dimethylsulfide (DMS) dehydrogenase is a complex heterotrimeric enzyme that catalyzes the oxidation of DMS to DMSO and allows Rhodovulum sulfidophilum to grow under photolithotrophic conditions with DMS as the electron donor. The enzyme is a 164 kDa heterotrimer composed of an alpha-subunit that binds a bis(molybdopterin guanine dinucleotide)Mo cofactor, a polyferredoxin beta-subunit, and a gamma-subunit that contains a b-type heme. In this study, we describe the thermodynamic characterization of the redox centers within DMS dehydrogenase using EPR- and UV-visible-monitored potentiometry. Our results are compared with those of other bacterial Mo enzymes such as NarGHI nitrate reductase, selenate reductase, and ethylbenzene dehydrogenase. A remarkable similarity in the redox potentials of all Fe-S clusters is apparent.

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