Abstract:
:Dimethylsulphoxide (DMSO) reductase from R. capsulatus contains a molybdenum-pterin cofactor at its active site. As prepared the molybdenum is in the 6+ oxidation state, devoid of EPR signals. Stepwise reduction generates an EPR signal characteristic of Mo(V) having hyperfine coupling to a single proton and integrating to less than 25% of the total molybdenum. The low temperature MCD spectrum shows oppositely signed bands between approximately 550-700 nm. These bands are assigned as dithiolene-to-Mo(V) charge transitions. A simple theoretical model can satisfactorily account for the bands in the MCD spectrum. No evidence is found for cysteine coordination to Mo(V).
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Benson N,Farrar JA,McEwan AG,Thomson AJdoi
10.1016/0014-5793(92)80760-ekeywords:
subject
Has Abstractpub_date
1992-07-28 00:00:00pages
169-72issue
2eissn
0014-5793issn
1873-3468pii
0014-5793(92)80760-Ejournal_volume
307pub_type
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