No abstract available

[en] A method of polarizing nuclei having a long relaxation time in a solid in a high dc magnetic field is described. The solid also contains nuclei having a short relaxation time. The method involves the step of applying a high dc magnetic field to the solid. Then the solid is swept with a radio frequency field which excites the nuclei with a short relaxation time; there results the polarization of the nuclei having a long relaxation time. 1 figure, 1 table

No abstract available

No abstract available

No abstract available

No abstract available

[en] In a unicellular cyanobacterium, the mobile fraction of phycobilisome (PBS) was found to be maximum at a particular redox value of Q_A (i.e., 0.52). An upward or downward shift in the redox value leads to a decrease in this mobile fraction of PBS. Furthermore, the regulatory effect of the redox state of Q_A on PBS mobility was found to be independent of the effect exerted by the plastoquinone pool. These findings indicate for the first time that PBS mobility is regulated by the Q_A redox state in cyanobacteria. A possible working mechanism underlying this control is discussed.

[en] Highlights: • Quinones show greater capacity than hydroquinones in nuclear Bach1 export. • Quinones show greater capacity than hydroquinones in Ub-dependent Bach1 degradation. • Quinones rather than hydroquinone activate Nrf2 through Bach1 arylation. • Electrophilic character of quinones is important for the downregulation of Bach1. - Abstract: The activation of nuclear factor erythroid 2-related factor 2 (Nrf2) is the most important cellular defense mechanisms against oxidative attack. BTB and CNC homology-1 (Bach1), like Kelch-like ECH-associated protein 1 (Keap1), is one of a negative regulator of Nrf2 that control antioxidant response elements (ARE)-dependent gene expressions. In the current study, we found that quinones show greater capacity than hydroquinones in nuclear Bach1 export, as well as ubiquitin-dependent Bach1 degradation in our experimental time frame. Consistently, quinones are easier than hydroquinones in Nrf2 activation and ARE-driven antioxidant protein expressions. Considering the redox cycling potential of quinone-hydroquinone couple, we investigated the effect of transit metal oxidation on the regulation of Nrf2 activity. As shown, Fe³⁺ enhanced hydroquinone-induced Nrf2 activation and ARE-driven gene expressions, suggesting quinones rather than hydroquinone activate Nrf2 through Bach1 arylation. Taking together, our investigation illustrated that the electrophilic character of quinones ensure their conjugation with Bach1, which is important for the downregulation of Bach1 and the upregulation of Nrf2 signaling.

[en] 1Abbreviations: cyt, cytochrome; cyt bL, low potential b cytochrome; cyt bH, high potential b cytochrome; DBMIB, 2,5-dibromo-3-methyl-6-isopropylbenzoquinone; DMSO, dimethylsulfoxide; DNP-INT, 2'-iodo-6-isopropyl-3-methyl-2',4,4'-trinitrodiphenylether; EPR, electron paramagnetic resonance; HEPES, n-(2-hydroxyethyl)piperazine-n'-(2-ethanesulfonic acid); NQNO, 2-nonyl-4-hydroxyquinoline n-oxide; ISP, iron-sulfur protein; MOA, E-b-methoxyacrylate; pmf, proton motive force; PC, plastocyanin; PQ, plastoquinone; PQH2, plastoquinol; PS, photosystem; Qi, quinol reductase; Qo, quinol oxidase; UHDBT, 5-n-undecyl-6-hydroxy-4,7-dioxobenzothiazole

[en] Past studies demonstrate that complexation will limit abiotic and biotic U(VI) reduction rates and the overall extent of reduction. However, the underlying basis for this behavior is not understood and presently unpredictable across species and ligand structure. The central tenets of these investigations are: (1) reduction of U(VI) follows the electron-transfer (ET) mechanism developed by Marcus; (2) the ET rate is the rate-limiting step in U(VI) reduction and is the step that is most affected by complexation; and (3) Marcus theory can be used to unify the apparently disparate U(VI) reduction rate data and as a computational tool to construct a predictive relationship