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J. Biol. Chem., Vol. 275, Issue 51, 40202-40210, December 22, 2000
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From the Department of Biochemistry, Duke University Medical
Center, Durham, North Carolina 27710
A fully defined in vitro system has
been developed for studying the mechanism of assembly of the
bis(molybdopterin guanine dinucleotide)molybdenum cofactor in
Rhodobacter sphaeroides dimethyl sulfoxide reductase
(DMSOR). R. sphaeroides DMSOR expressed in a
mobA- Escherichia coli strain lacks
molybdopterin and molybdenum but contains a full complement of guanine
in the form of GMP and GDP. Escherichia coli MobA,
molybdopterin-Mo, GTP, and MgCl2 are required and
sufficient for the in vitro activation of purified DMSOR
expressed in the absence of MobA. High levels of MobA inhibit the
in vitro activation. A chaperone is not required for the
in vitro activation process. The reconstituted DMSOR can
exhibit up to 73% of the activity observed in recombinant DMSOR
purified from a wild-type strain. The use of radiolabeled GTP has
demonstrated incorporation of the guanine moiety from the GTP into the
activated DMSOR. No role was observed for E. coli MobB in
the in vitro activation of apo-DMSOR. This work also
represents the first time that the MobA-mediated conversion of
molybdopterin to molybdopterin guanine dinucleotide has been
demonstrated directly without using the activation of a molybdoenzyme
as an indicator for cofactor formation.
Mechanism of Assembly of the Bis(Molybdopterin Guanine
Dinucleotide)Molybdenum Cofactor in Rhodobacter sphaeroides
Dimethyl Sulfoxide Reductase*
*
This work was supported by National Institutes of Health
Grant GM00091.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.: 919-681-8845;
Fax: 919-684-8919; E-mail: raj@biochem.duke.edu.
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