TL;DR: In this article, the authors describe two simple and sensitive spectrophotometric methods that have the advantage of detecting authentic hydroperoxides selectively, referred to as "FOX methods 1 and 2" (ferrous oxidation in xylenol orange).
Abstract: Publisher Summary Hydroperoxides in biological systems can be measured by electroanalytical determination using high-performance liquid chromatography (HPLC), chemiluminescence using microperoxidase-luminol, activation of cyclooxygenase, techniques based on thiobarbituric acid (TBA) conjugation of malonaldehyde, iodide oxidation: conjugated diene formation, and alkane expiration. Of these, the TBA methods are most widely used. They require the least sophisticated instrumentation, but they are the most criticized on grounds of their ambiguity. This chapter describes two simple and sensitive spectrophotometric methods that have the advantage of detecting authentic hydroperoxides selectively. These methods are referred to as “FOX methods 1 and 2” (ferrous oxidation in xylenol orange). Method FOX1 is extremely sensitive [ɛ560(H2O2) = 2.2 × 105M-1 cm-1] and is readily applied to the measurement of low levels of water-soluble hydroperoxides present in aqueous phase; FOX2 [ɛ560(ROOH) = 4.5 × 104M-1 cm-1] is used to determine levels of hydroperoxides present in the lipid phase, such as in lipoproteins, membranes, and fats.
TL;DR: Three of the four major thyroid-specific proteins have been cloned, namely thyroglobulin (TG), TPO (see below), and the TSH receptor (5–8), and molecular cloning of the thyroid iodide transporter may occur soon (9).
Abstract: I. Introduction THYROID peroxidase (TPO) is the primary enzyme involved in thyroid hormone synthesis, catalyzing iodide oxidation, iodination of tyrosine residues, and coupling of iodotyrosines to generate the iodothyronines T3 and T4 (1). It is a membrane-bound glycoprotein with a heme prosthetic group. In addition to the pivotal physiological role of TPO, there was strong immunological evidence, even before its molecular cloning, that this enzyme was the elusive “thyroid microsomal antigen” in autoimmune thyroid disease (discussed below). The molecular cloning of the complementary DNA for a protein provides powerful new opportunities for studying protein structure and function at an unprecedented level of detail. In t h e past decade, three of the four major thyroid-specific proteins have been cloned, namely thyroglobulin (TG) (2–4), TPO (see below), and the TSH receptor (5–8). Molecular cloning of the thyroid iodide transporter may occur soon (9). As might be expected, these advances have been followed...
TL;DR: In this paper, the potential energy needed to oxidize the halide, determined by their relative oxidation potentials (I−I−B−B), was investigated. And the authors showed that halide oxidation plays a major role in the physical demixing of alloyed halide compositions in perovskite films, ultimately directed by several underlying thermodynamic and kinetic driving forces operating in both concert and competition.
TL;DR: Photophysical measurements show that the high photocurrent observed for cis-Ru(dcb)(2)(NCS)(2)/TiO(2) is due to efficient and rapid iodide oxidation.
Abstract: New Ru(dcbH)(dcbH2)(L) sensitizers, where L is diethyldithiocarbamate, dibenzyldithiocarbamate, or pyrrolidinedithiocarbamate, dcbH is 4-(COOH)-4‘-(COO-)-2,2‘-bipyridine, and dcbH2 is 4,4‘-(COOH)2-2,2‘-bipyridine, have been synthesized, characterized, and anchored to nanocrystalline TiO2 films for light to electrical energy conversion in regenerative photoelectrochemical cells with I-/I2 acetonitrile electrolyte. The sensitizers have intense metal-to-ligand charge-transfer (MLCT) bands centered ∼380 and 535 nm that sensitize TiO2 over a notably broad spectral range. The photophysical and photoelectrochemical studies of these materials are contrasted with cis-Ru(dcbH2)2(NCS)2, which is one of the most efficient sensitizers reported to date. Photophysical measurements show that the high photocurrent observed for cis-Ru(dcb)2(NCS)2/TiO2 is due to efficient and rapid iodide oxidation.
TL;DR: The results of analyses of samples from the Bermuda Atlantic Time Series (BATS) and Hawaii Ocean Time-series (HOT) for dissolved iodine speciation are presented in this paper.
Abstract: The results of analyses of samples from the Bermuda Atlantic Time Series (BATS) and Hawaii Ocean Time-series (HOT) for dissolved iodine speciation are presented. At both sites iodate is reduced to iodide in surface waters by biological processes, but the iodide concentrations in the upper 100 m at the HOT site are approximately twice those at the BATS site. Using published estimates of surface water residence times and primary productivity at each station we use the differences between the two sites to derive an estimate of the in situ rate of iodide oxidation and the relationship between iodate reduction and primary production using a simple mass balance model. The model results suggest that on an annual basis iodide oxidation is relatively fast (half-life about 70 days) and that biological iodate reduction to iodide is about 100 times faster than iodide incorporation into particulate organic carbon.