Detection of the optical bands of molybdenum(V) in DMSO reductase (Rhodobacter capsulatus) by low-temperature MCD spectroscopy.

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 Lett

journal_title

FEBS letters

authors

Benson N,Farrar JA,McEwan AG,Thomson AJ

doi

10.1016/0014-5793(92)80760-e

keywords:

subject

Has Abstract

pub_date

1992-07-28 00:00:00

pages

169-72

issue

2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(92)80760-E

journal_volume

307

pub_type

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