Literature summary for 1.8.5.3 extracted from

Solomon, P.S.; Lane, I.; Hanson, G.R.; McEwan, A.G.
Characterisation of the pterin molybdenum cofactor in dimethylsulfoxide reductase of Rhodobacter capsulatus (1997), Eur. J. Biochem., 246, 200-203.

Search for more literature for 1.8.5.3

Organism

Organism	UniProt	Comment	Textmining
Rhodobacter capsulatus	-	-	-

Cofactor

Cofactor	Comment	Organism	Structure
molybdenum bis-molybdopterin guanine dinucleotide	the molybdenum cofactor in dimethylsulfoxide reductase is bis(molybdopterin guanine dinucleotide) molybdenum. Protein contains 1 mol Mo and 2 mol GMP. Approximately 2 mol. electrons/2 mol molybdopterin guanine dinucleotide reduce 2,6-dichloroindophenol. 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	Rhodobacter capsulatus

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)