Literature summary for 1.8.2.6 extracted from

Drew, S.C.; Reijerse, E.; Quentmeier, A.; Rother, D.; Friedrich, C.G.; Lubitz, W.
Spectroscopic characterization of the molybdenum cofactor of the sulfane dehydrogenase SoxCD from Paracoccus pantotrophus (2011), Inorg. Chem., 50, 409-411 .

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Metals/Ions

Metals/Ions	Comment	Organism	Structure
Molybdenum	molybdenum cofactor exists as low- and high-pH species with g and A(95,97Mo) matrices nearly identical to those of sulfite oxidase. No sulfite-induced reduction to MoV is detected. The outer coordination sphere controls substrate binding in SoxCD, permitting access only to protein-bound sulfur via the C-terminal tail of SoxY	Paracoccus pantotrophus

Organism

Organism	UniProt	Comment	Textmining
Paracoccus pantotrophus	-	-	-

Synonyms

Synonyms	Comment	Organism
SoxCD	-	Paracoccus pantotrophus

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Release 2023.1 (January 2023)