Vanadate location

Describe the large conformational difference between myosin-ADP and myosin-ATP (same as myosin-ADP-vanadate). Locate switch 1, switch 11, and the relay helix in relation to the P-loop, and explain how they cause the protein to flex. 

Acylphosphate formation is characteristic for P-type ATPases and involves the transfer of the y-phosphate of ATP to an aspartic acid residue to form a high-energy enzyme intermediate. The phosphorylated aspartic acid residue is located in the sequence DKTGT, which is universally conserved in all members of the P-type superfamily. By this criterion, CopA and CopB of En. hirae are clearly members of the P-type superfamily of ATPases and probably function by the same underlying mechanism. Vanadate sensitivity is another hallmark of P-type ATPases. CopA and CopB were inhibited by vanadate with /50 values of around 0.1 mM. This is a low vanadate sensitivity compared to /50 values in the micromolar to submicromolar range observed for non-heavy metal P-type ATPases. 

The results in Table II suggest that molybdate- and vanadate-pillared hydrotalcites contain both acidic and basic sites, the basic sites located on the metal hydroxide sheets, and the acidic sites located on the polyoxometalate pillars. 

Several membrane-bound ATPases occur in the genus Sulfolobus. There are two ATP-hydrolyzing activities in S. acidocaldarius strain 7. One has a pH optimum at 6.5 in the absence of sulfate, and the presence of that anion activates the enzyme and shifts the pH optimum to 5.0. ATP hydrolysis is unaffected by DCCD, azide, NEM, /7-hydroxymercuribenzoate, or vanadate [59]. The other ATPase is most active at pH 2.5, is inhibited by sulfate, and appears to be a pyrophosphatase [16]. The purified sulfate-activated ATPase (M, 360000) is composed of three subunits (Mr 69000, 54000, and 28000). It is most active at 85 C, stimulated some three-fold by sulfate, sulfite, and bicarbonate, but is unaffected by chloride. There are two pH optima. One is located at pH 5 and the other at pH 8.5 and neither is affected by sulfite. ATPase activity is inhibited by nitrate (63% at 20 mM) and NBD-Cl (90% at 1 mM) but is not significantly affected by azide (5mM), vanadate (100 pM), and NEM (100pM)[28]. 

DRS measurements support the TPR results. The impregnated catalysts and steam treated (IMPV) did not show the presence of V after the reduction. Probably, the hydrogen consumption in the TPR profile is due to the reduction of cerium. The band in the d-d transition can be attributed to the formation of alloys like cerium vanadate, according to the literature [14]. Baugis et al. [15] reported that the presence of vanadate with rare earth decreases the diffusion of vanadium in the zeolite structure [14]. The existence of these compounds may affect the oxidation state, the dispersion, morphology and location of cerium species in the catalyst. 

The measured UV-VIS absorption spectra of the lead and samarium-vanadate-tellurate glasses are shown in Fig. 3. The spectra show that the maxima of the absorption are located in the UV region for all investigated glasses containing PbO or Sm203. 

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