Sensor networks with battery-powered nodes can seldom simultaneously meet the design goals of lifetime, cost, sensing reliability and sensing and transmission coverage. Energy-harvesting, converting ambient energy to electrical energy, has emerged as an alternative to power sensor nodes. By exploiting recharge opportunities and tuning performance parameters based on current and expected energy levels, energy harvesting sensor nodes have the potential to address the conflicting design goals of lifetime and performance. This paper surveys various aspects of energy harvesting sensor systems-architecture, energy sources and storage technologies and examples of harvesting-based nodes and applications. The study also discusses the implications of recharge opportunities on sensor node operation and design of sensor network solutions.

In this position paper, we examine recent technology trends that have resulted in a broad spectrum of camera sensors, wireless radio technologies, and embedded sensor platforms with varying capabilities. We argue that future sensor applications will be hierarchical with multiple tiers, where each tier employs sensors with different characteristics. We argue that multi-tier networks are not only scalable, they offer a number of advantages over simpler, single-tier unimodal networks: lower cost, better coverage, higher functionality, and better reliability. However, the design of such mixed networks raises a number of new challenges that are not adequately addressed by current research. We discuss several of these challenges and illustrate how they can be addressed in the context of SensEye, a multi-tier video surveillance application that we are designing in our research group.

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COMMD1 (copper metabolism gene MURR1 (mouse U2af1-rs1 region1) domain) belongs to a family of multifunctional proteins that inhibit nuclear factor NF-kappaB. COMMD1 was implicated as a regulator of copper metabolism by the discovery that a deletion of exon 2 of COMMD1 causes copper toxicosis in Bedlington terriers. Here, we report the detailed characterization and specific copper binding properties of purified recombinant human COMMD1 as well as that of the exon 2 product, COMMD(61-154). By using various techniques including native-PAGE, EPR, UV-visible electronic absorption, intrinsic fluorescence spectroscopies as well as DEPC modification of histidines, we demonstrate that COMMD1 specifically binds copper as Cu(II) in 1:1 stoichiometry and does not bind other divalent metals. Moreover, the exon 2 product, COMMD(61-154), alone was able to bind Cu(II) as well as the wild type protein, with a stoichiometry of 1 mol of Cu(II) per protein monomer. The protection of DEPC modification of COMMD1 by Cu(II) implied that Cu(II) binding involves His residues. Further investigation by DEPC modification of COMMD(61-154) and subsequent MALDI MS mapping and MS/MS sequencing identified the protection of His101 and His134 residues in the presence of Cu(II). Fluorescence studies of single point mutants of the full-length protein revealed the involvement of M110 in addition to H134 in direct Cu(II) binding. Taken together, the data provide insight into the function of COMMD1 and especially COMMD(61-154), a product of exon 2 that is deleted in terriers affected by copper toxicosis, as a regulator of copper homeostasis.

The isolation and the X-ray crystal structure of physiological copper(II)-L-histidine complex are reported. The neutral five-coordinate complex shows distorted square pyramidal geometry with bidentate and tridentate L-histidine ligands. The basic character of the pendent imidazole group and H-bonding interactions of bidentate L-histidine ligand are important for copper transport. The unique structural features help explain the origin of its thermodynamic stability and kinetic reactivity in human blood along with the ternary copper(II)-amino acid complexes. The role of L-histidine in interaction with copper(II)-albumin, in cellular uptake of copper, and in treatment of Menkes disease can be studied using these results.

Molecular fluorophores based on N,C-chelate, four-coordinate organoborons exhibit tunable solid-state emission colors that cover the whole visible region from blue to red. The emission color can be tuned through the substituents on either quinolines or the boron center.