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Literature summary for 1.16.99.1 extracted from

  • Duerichen, H.; Diekert, G.; Studenik, S.
    Redox potential changes during ATP-dependent corrinoid reduction determined by redox titrations with europium(II)-DTPA (2019), Protein Sci., 28, 1902-1908 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.16.99.1

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + a [Co(II) dimethylamine-specific corrinoid protein] + reduced acceptor + H2O Acetobacterium dehalogenans
-
 ADP + phosphate + a [Co(I) dimethylamine-specific corrinoid protein] + acceptor
-
 ?
ATP + a [Co(II) methylamine-specific corrinoid protein] + reduced acceptor + H2O Acetobacterium dehalogenans
-
 ADP + phosphate + a [Co(I) methylamine-specific corrinoid protein] + acceptor
-
 ?
ATP + a [Co(II) trimethylamine-specific corrinoid protein] + reduced acceptor + H2O Acetobacterium dehalogenans
-
 ADP + phosphate + a [Co(I) trimethylamine-specific corrinoid protein] + acceptor
-
 ?

Organism

Organism UniProt Comment Textmining
Acetobacterium dehalogenans B8R2M5
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + a [Co(II) dimethylamine-specific corrinoid protein] + reduced acceptor + H2O
-
 Acetobacterium dehalogenans ADP + phosphate + a [Co(I) dimethylamine-specific corrinoid protein] + acceptor
-
 ?
ATP + a [Co(II) methylamine-specific corrinoid protein] + reduced acceptor + H2O
-
 Acetobacterium dehalogenans ADP + phosphate + a [Co(I) methylamine-specific corrinoid protein] + acceptor
-
 ?
ATP + a [Co(II) trimethylamine-specific corrinoid protein] + reduced acceptor + H2O
-
 Acetobacterium dehalogenans ADP + phosphate + a [Co(I) trimethylamine-specific corrinoid protein] + acceptor
-
 ?

Synonyms

Synonyms Comment Organism
OdmC
-
 Acetobacterium dehalogenans

General Information

General Information Comment Organism
physiological function enzyme activates methyltrophic corrinoid proteins by reducing cobalt(II) back to cobalt(I). The transfer of electrons to the corrinoid as the electron-accepting site is achieved by increasing the potential of the corrinoid cofactor from -530 mV to -250 mV. The first 50 to 100 mV of the shift of the redox potential are caused by the interaction of nucleotide-bound enzyme with the corrinoid protein or its cofactor. The remaining 1500-200 mV have to be overcome by the chemical energy of ATP hydrolysis Acetobacterium dehalogenans