Structure of Vitamin B12: X-ray Crystallographic Evidence on the Structure of Vitamin B12

  title={Structure of Vitamin B12: X-ray Crystallographic Evidence on the Structure of Vitamin B12},
  author={C. Brink and Dorothy Mary Crowfoot Hodgkin and June Lindsey and Jenny Pickworth and John H. Robertson and JOHN G. White},
Cobalt binding in the photosynthetic bacterium R. sphaeroides by X-ray absorption spectroscopy
An X-ray absorption spectroscopy investigation was conducted on Rhodobacter sphaeroides cells to gain structural insights into the Co2+ binding to cellular components, suggesting the presence of carboxylate and sulfonate metal-binding functional groups, the latter arising from sulfolipids of the cell envelope.
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ARCIMBOLDO, an automated, fragment-based approach to structure determination, expands the reach of MicroED to presently inaccessible peptidic structures including segments of human amyloids, and yeast and mammalian prions, and portends a more general phasing solution while limiting model bias for a wider set of chemical structures.
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The present review is based on selected methodologies and applications supplying molecular structure, binding affinity and biological activity data for the development of new SARs in the context of proteins as epigenetic drug targets.
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Beitrag zur Kenntnis der Vitamins B12. 1. Mitteilung
Vitamin B12 wurde in einem Gemisch von verdunnter Salzsaure und Butanol mit Wasserstoff und PtO2 hydriert, wobei unter den angegebenen Reaktionsbedingungen 5–6 Mol NH3 (pro Mol B12), β-Amino-propanol