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NADPH oxidases: molecular mechanisms and clinical implications.
Superoxide production by NADPH oxidase (NOX) is implicated in the pathogenesis of various cardiovascular diseases. Most of the enzymes that have been identified as belonging to the NOX family are membrane bound, and the cytosolic component of the active complex (gp91(phox), p47(phox), p67(phox), p40(phox), and Rac-2) is composed of a cytosolic portion (p40(phox)/p47(phox) heterodimer) and a transmembrane component (gp91(phox)). The cytosolic components are associated with each other in a noncovalent manner via two separate domains, the cysteine-rich domain (CSRD) and the p22(phox)-homologous domain (PH domain), respectively. The cytosolic components function as a complex and their activities are regulated by phosphorylation, protein-protein interactions, and calcium. The cytosolic components are located on the cytoplasmic face of the membrane where they interact with one another and with membrane phospholipids. Recently, crystal structure analysis of cytochrome b(558) has revealed that a motif called the membrane-binding motif (MBM) composed of four conserved residues binds to the membrane phospholipids. In contrast to the cytosolic components, the transmembrane component is a transmembrane protein, which exhibits unique sequence homology to the p22(phox) protein. The molecular mechanisms underlying the regulation of the transmembrane component remain to be elucidated. The transmembrane component exhibits considerable complexity because the amino acid sequence is composed of multiple homologous domains and phosphorylation sites. Protein-protein interactions are important for the activation of the cytosolic components. Therefore, the transmembrane components are involved in the dynamic assembly and disassembly of the enzyme complex. We herein review the progress in our understanding of the molecular mechanisms of NOX and its clinical implications.A spectroscopic probe for studying photophysical processes of DNA.
A combination of time-resolved and steady-state spectroscopic methods is applied to the study of the photophysics of DNA, which provides a unique opportunity to investigate DNA intercalation. We report the formation of two species with distinct photophysical properties. The stronger luminescence decays rapidly, leading to a 3125841983
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