Vanadyl ribonucleoside explained

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 [<nowiki/>[[Argon|Ar]]] 3d³ 4s² electron configuration allows it to make five sigma bonds and two pi bonds with adjacent atoms.^[2]

History

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.^[3]

Production

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

Use

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.

Notes and References

1. 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. en. 18. 23. 5143–5149. 10.1021/bi00590a018. 497174. 0006-2960.
2. Ballhausen. C. J.. Gray. Harry B.. February 1962. The Electronic Structure of the Vanadyl Ion. Inorganic Chemistry. en. 1. 1. 111–122. 10.1021/ic50001a022. 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. 10.1016/0014-5793(73)80515-0. 4589558. 36443453. 0014-5793. free.
4. Seith. W.. Kottmann. A.. 1952-07-21. Über die Diffusion in festen Metallen. Angewandte Chemie. 64. 14. 379–391. 10.1002/ange.19520641402. 1952AngCh..64..379S. 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. 10.1101/sqb.1972.036.01.009. 4508159. 0091-7451.