Vanadyl ribonucleoside

From Wikipedia, the free encyclopedia

Vanadyl ribonucleoside is a potent transition-state analog of ribonucleic acid and potent inhibitor of many species of ribonuclease formed from a vanadium coordination complex and one ribonucleoside.[1] Vanadium's [Ar] 3d3 4s2 electron configuration allows it to make five sigma bonds and two pi bonds with adjacent atoms.[2]

History[edit]

RNA is notoriously unstable and vulnerable to ribonucleases, which has thus been an obstacle to the production and analysis of the cellular transcriptome. First referenced by Berger et al., the substance was used to prevent the digestion of RNA during isolation from white blood cells, and was rapidly adopted for such purposes as the acquisition of RNA from green beans.[1][3]

Production[edit]

Vanadyl ribonucleoside is produced by combining vanadyl sulphate with various ribonucleosides (such as guanosine) in a 1:10 molar ratio.[4][5]

Use[edit]

Vanadyl ribonucleoside, along with other RNase inhibitors, has been a staple of molecular biochemistry since its invention by allowing for the stability of RNA in its storage and use.

References[edit]

  1. ^ a b Berger, Shelby L.; Birkenmeier, Connie S. (1979-11-13). "Inhibition of intractable, nucleases with ribonucleoside-vanadyl complexes: isolation of messenger ribonucleic acid from resting lymphocytes". Biochemistry. 18 (23): 5143–5149. doi:10.1021/bi00590a018. ISSN 0006-2960. PMID 497174.
  2. ^ Ballhausen, C. J.; Gray, Harry B. (February 1962). "The Electronic Structure of the Vanadyl Ion". Inorganic Chemistry. 1 (1): 111–122. doi:10.1021/ic50001a022. ISSN 0020-1669.
  3. ^ Gray, J.C.; Kekwick, R.G.O. (1973-12-15). "Synthesis of the small subunit of ribulose 1, 5-diphosphate carboxylase on cytoplasmic ribosomes from greening bean leaves". FEBS Letters. 38 (1): 67–69. doi:10.1016/0014-5793(73)80515-0. ISSN 0014-5793. PMID 4589558. S2CID 36443453.
  4. ^ Seith, W.; Kottmann, A. (1952-07-21). "Über die Diffusion in festen Metallen". Angewandte Chemie. 64 (14): 379–391. Bibcode:1952AngCh..64..379S. doi:10.1002/ange.19520641402. ISSN 0044-8249.
  5. ^ Lienhard, G. E.; Secemski, I. I.; Koehler, K. A.; Lindquist, R. N. (1972-01-01). "Enzymatic Catalysis and the Transition State Theory of Reaction Rates: Transition State Analogs". Cold Spring Harbor Symposia on Quantitative Biology. 36: 45–51. doi:10.1101/sqb.1972.036.01.009. ISSN 0091-7451. PMID 4508159.