Vanadates biochemistry

Vanadate, dioxybis(oxamato)-bond-length ratios, 1,57 Vanadate, heptacyano-potassium salt structure, I, 72 Vanadate, hexafluoro-dipotassium salt history, I, 21 potassium salt history, 1,21 tripotassium salt history, 1,21 Vanadate, pentachloro-stereochemistry, 1,40 Vanadate, pentafluorooxy-stereochemistry, I, 50 Vanadates biochemistry, 3,456 calcium/magnesium ATPase inhibition, 6, 567 competition with phosphates physiology, 6,665 protonation, 3,1026 sodium pump, 6, 557 in uranium purification from ore, 6, 899 Vanadates, hexafluoro-, 3. 482,531 Vanadates, oxoperoxo-, 3,501 Vanadates, pentacarbonyl-, 3, 457 Vanadium biology, 6,665 determination, 1. 548 extraction... 

Smith, C. A., Rayment, 1. X-ray structure of the magnesium (11). ADP-vanadate complex of the Dictyostelium discoideum myosin motor domain to 1.9 A resolution. Biochemistry 35 5404-5407, 1996. 

Gresser MJ, Tracey AS (1990) Vanadates as Phosphate Analogs in Biochemistry. In Chastcen ND (ed) Vanadium in Biological Systems. Physiology and Biochemistry. Kluwer Academic, Dordrecht, p 63... 

Werber MM, Peyser YM, Muhlrad A. 1992. Characterization of stable beryllium fluoride, aluminum fluoride, and vanadate containing myosin subfragment 1-Nucleotide complexes. Biochemistry 31 7190-7197. 

Gresser, M.J., A.S. Tracey, and N.D. Chasteen. 1990. Vanadates as phosphate analogs in biochemistry. Vanadium in biological systems. Dordrecht, Boston, London Kluwer Academic Publishers, pp 63-79. 

Kostrewa, D., H.W. Choe, U. Heinemann, and W. Saenger. 1989. Crystal structure of guanosine-free ribonuclease T1, complexed with vanadate(V), suggests conformation change upon substrate binding. Biochemistry 28 7592-7600. 

Figure 1.7 (a) UV-VIS absorption spectra of 100 /vanadium chloroperoxidase at pH 8.3. The lower solid line shows the apo-enzyme, the upper solid line the holo-enzyme after addition of 100 /xM vanadate. The dotted line is the peroxo-form of the enzyme after addition of 100 /optical absorbance at 316 nm ( ). Absorbance of free vanadate under the same buffer conditions (O). Reprinted with permission from Renirie, R., Hemrika, W., Piersma, S.R. and Wever, R. (2000). Biochemistry, 39, 11 33-1141. Copyright 2000 American Chemical Society. 

Figure 1.10 UV-VIS absorbance of the H404A mutant of VCPO and the effect of H2O2 at pH 8.3. (a) Spectrum a 200 /xM apo-H404A spectrum b mixture of holo- and apo-enzyme after addition of 200 fxM vanadate spectrum c the effect of addition of 200 (xM H2 O2. (b) Spectrum a titration of 200 fxM apo-H404A with 0-800 /xM vanadate the line shown is a fit to the data points for a simple dissociation equilibrium spectrum b absorbance of 0-200 fxM free vanadate. Source Renirie, R., Hemrika, W. and Wever, R. (2000). Journal of Biological Chemistry, 275, 11650-11657. Reprinted with permission from The American Society for Biochemistry and Molecular Biology.

Erdmann E, Werdan K, Krawietz W, et al. 1984. Vanadate and its significance in biochemistry and pharmacology. Biochem Pharmacol 33 945-950. 

Figure 8. (A) Frozen solution (T = 223 K) EPR spectra of vanadate-loaded adipocytes incubated with 15 mM glucose and 100 nM insulin, with (Resistant + NAC) or without (Resistant) 30 mM N-acetylcysteine pretreatment, with 80 pM BSO (GSH-synthase inhibited), or with 5.6 mM glucose (Resistant). (B) EPR spectral intensity expressed as an average of 3 experiments ( p < 0.05 compared with control and R+NAC). Reprinted with permission from [65]. Copyright 2001, American Society for Biochemistry and Molecular Biology.

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