Structural characterization of novel cobalt corrinoids synthesized by enzymes of the vitamin B12 anaerobic pathway.
Investigation on the use of the oxidized form (factor 3 (3a)) of the trimethylated intermediate (precorrin 3 (2)) as a substrate for the enzymes of the anaerobic pathway to vitamin B12 led to the synthesis of three pairs of novel cobalt corrinoids. The products were made with the aid of the Salmonella typhimurium enzymes CbiH, CbiF, CbiG, and CbiT, were synthesized in several 13C labeled versions, and were isolated as methylesters after esterification. Structures were determined by detailed NMR and MS analyses. Each set of products was obtained in the decarboxylated (RMe) and non-decarboxylated (R=CH2COOCH3) forms (at the C-12 position of the porphyrinoid).
Santander
Patricio J
PJ
Center for Biological NMR, Department of Chemistry, Texas A&M University, PO Box 3255, College Station, TX 77843-3255, USA. patricio@tamu.edu
Kajiwara
Yasuhiro
Y
Williams
Howard J
HJ
Scott
A Ian
AI
D000693:Anaerobiosis; D003035:Cobalt / Q000737:chemistry; D045728:Corrinoids / Q000096:biosynthesis* / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D015394:Molecular Structure; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D012486:Salmonella typhimurium / Q000201:enzymology / Q000235:genetics; D014805:Vitamin B 12 / Q000096:biosynthesis*
D045728:Corrinoids; D011994:Recombinant Proteins; D003035:Cobalt; D014805:Vitamin B 12