Characterisation of the Pterin Molybdenum Cofactor in Dimethylsulfoxide Reductase of Rhodobacter capsulatus and the periplasmic Nitrate Reductase of Paracoccus denitrificans

Solomon, Peter S., Lane, Ian, Hanson, Graeme R. and McEwan, Alastair G. (1997) Characterisation of the Pterin Molybdenum Cofactor in Dimethylsulfoxide Reductase of Rhodobacter capsulatus and the periplasmic Nitrate Reductase of Paracoccus denitrificans. European Journal of Biochemistry, 246 1: 200-203. doi:10.1111/j.1432-1033.1997.t01-2-00200.x


Author Solomon, Peter S.
Lane, Ian
Hanson, Graeme R.
McEwan, Alastair G.
Title Characterisation of the Pterin Molybdenum Cofactor in Dimethylsulfoxide Reductase of Rhodobacter capsulatus and the periplasmic Nitrate Reductase of Paracoccus denitrificans
Journal name European Journal of Biochemistry   Check publisher's open access policy
ISSN 0014-2956
Publication date 1997-05
Sub-type Article (original research)
DOI 10.1111/j.1432-1033.1997.t01-2-00200.x
Volume 246
Issue 1
Start page 200
End page 203
Total pages 4
Place of publication Oxford, England
Publisher Blackwell Science for the Federation of European Biochemical Societies
Language eng
Subject 030201 Bioinorganic Chemistry
Abstract Analysis of dimethylsulfoxide reductase from Rhodobacter capsulatus showed that it contained 1 mol Mo and 2 mol GMP. This indicates that the molybdenum cofactor in dimethylsulfoxide reductase is bis(molybdopterin guanine dinucleotide) molybdenum. The absorption spectrum of the molybdopterin guanine dinucleotide released from dimethylsulfoxide reductase after denaturation of the holoenzyme was compared with those of pterin standards of known redox state. The spectra were most similar to pterin standards in the dihydro state and oxidised state. The reduction of 2,6-dichloroindophenol by molybdopterin guanine dinucleotide released from dimethylsulfoxide reductase and by pterin standards was also measured and approximately 2 mol electrons/2 mol molybdopterin guanine dinucleotide were found to reduce 2,6-dichloroindophenol. These results are consistent with the presence of one molybdopterin guanine dinucleotide moiety with a pyrazine ring at the oxidation level of a dihydropteridine and one molybdopterin guanine dinucleotide moiety with a pyrazine ring at the oxidation level of a fully aromatic pteridine. It is suggested that the pyrazine ring of Q-molybdopterin guanine dinucleotide is fully aromatic and contains a 5,6 double bond.
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: Centre for Advanced Imaging Publications
 
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