The oxovanadium cation, V02+, has been successfully employed as a spin probe1 in electron-nuclear double resonance (ENDOR)2,3 and electron spin echo envelope modulation (ESEEM)3•4 studies of metalloprotein active sites. These techniques are often used to detect coordination by side chains of histidine residues.5•6 Interpretation usually relies on the ENDOR study by Mulks et al/ of oxovanadium complexes of imidazole or histidine. Unfortunately, the nitrogen ENDOR spectra were not completely analyzed, and the hyperfine coupling to the remote imidazole nitrogen has been questioned.8Here we demonstrate that the complex of V02+ with histidine has been misinterpreted and that the dominant ESEEM pattern is produced by the -amino group. Nevertheless, we show that

Solutions containing variable concentrations of sulfide (0 to 31 ppm) and arsenite (0.35 to 10 ppm) were subjected to several different preservation treatments. As predicted by equilibrium thermodynamics, at near-neutral pH the experimental solutions were undersaturated with respect to orpiment (As2S3). However, upon acidification to pH 2 with HCl or HNO3, instantaneous precipitation of poorly crystalline As2S3 occurred in sulfidic solutions which resulted in the loss of dissolved arsenite. These results have implications concerning the practice of acidifying water samples containing hydrogen sulfide with HCl or HNO3 for the purpose of preserving total arsenic values. If a near-neutral water sample contains 1 ppm arsenite and as little as 0.4 ppm sulfide, loss of dissolved arsenic will occur upon acidification. An alternative three-step preservation method involving base addition, oxidation, and acidification is proposed and investigated as an appropriate technique for preserving sulfide-bearing aqueous samples for total arsenic.

Radiolytic reduction at 77 K of oxo/hydroxo-bridged dinuclear iron(III) complexes in frozen solutions forms kinetically stabilized, mixed-valent species in high yields that model the mixed-valent sites of non-heme, diiron proteins. The mixed-valent species trapped at 77 K retain ligation geometry similar to the initial diferric clusters. The shapes of the mixed-valent EPR signals depend strongly on the bridging ligands. Spectra of the Fe(II)OFe(III) species reveal an S = 1/2 ground state with small g-anisotropy as characterized by the uniaxial component (gz-gav/2 < 0.03) observable at temperatures as high as approximately 100 K. In contrast, hydroxo-bridged mixed-valent species are characterized by large g-anisotropy (gz-gav/2 > 0.03) and are observable only below 30 K. Annealing at higher temperatures causes structural relaxation and changes in the EPR characteristics. EPR spectral properties allow the oxo- and hydroxo-bridged, mixed-valent diiron centers to be distinguished from each other and can help characterize the structure of mixed-valent centers in proteins.

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