PURIFICATION AND PROPERTIES OF DIMETHYL-SULFOXIDE REDUCTASE FROM RHODOBACTER-CAPSULATUS - A PERIPLASMIC MOLYBDOENZYME

被引:92
作者
MCEWAN, AG
FERGUSON, SJ
JACKSON, JB
机构
[1] UNIV BIRMINGHAM,SCH BIOCHEM,BIRMINGHAM B15 2TT,W MIDLANDS,ENGLAND
[2] UNIV OXFORD,DEPT BIOCHEM,OXFORD OX1 3QU,ENGLAND
关键词
D O I
10.1042/bj2740305
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Dimethyl sulphoxide reductase was purified from the photosynthetic bacterium Rhodobacter capsulatus. The enzyme is composed of a single polypeptide of M(r) 82000 and contains a pterin-type molybdenum cofactor as the only detectable prosthetic group. The oxidized molybdenum cofactor of dimethyl sulphoxide reductase is a weak chromophore and exhibits broad absorption bands in the u.v.-visible-absorption spectral region. A distinct spectrum was generated upon addition of dithionite.
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页码:305 / 307
页数:3
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