Shape-programmable soft materials that exhibit integrated multifunctional shape manipulations, including reprogrammable, untethered, fast, and reversible shape transformation and locking, are highly desirable for a plethora of applications, including soft robotics, morphing structures, and biomedical devices.Despite recent progress, it remains challenging to achieve multiple shape manipulations in one material system. Here, we report a novel magnetic shape memory polymer composite to achieve this. The composite consists of two types of magnetic particles in an amorphous shape memory polymer matrix. The matrix softens via magnetic inductive heating of low-coercivity particles, and highremanence particles with reprogrammable magnetization profiles drive the rapid and reversible shape change under actuation magnetic fields. Once cooled, the actuated shape can be locked. Additionally, varying the particle loadings for heating enables sequential actuation. The integrated multifunctional shape manipulations are further exploited for applications including soft magnetic grippers with large grabbing force, sequential logic for computing, and reconfigurable antennas.

Magnetically responsive soft materials are soft composites where magnetic fillers are embedded into soft polymeric matrices. These active materials have attracted extensive research and industrial interest due to their ability to realize fast and programmable shape changes through remote and untethered control under the application of magnetic fields. They would have many high-impact potential applications in soft robotics/devices, metamaterials, and biomedical devices. With a broad range of functional magnetic fillers, polymeric matrices, and advanced fabrication techniques, the material properties can be programmed for integrated functions, including programmable shape morphing, dynamic shape deformation-based locomotion, object manipulation and assembly, remote heat generation, as well as reconfigurable electronics. In this review, an overview of state-of-the-art developments and future perspectives in the multifunctional magnetically responsive soft materials is presented.

ISU-type proteins mediate cluster transfer to apo protein targets. Rate constants have been determined for cluster transfer from ISU to apo Fd for both Homo sapiens and Schizosaccharomyces pombe proteins, and cross reactions have also been examined. Substitution of a key aspartate residue of ISU is found to decrease the rate of cluster transfer by at least an order of magnitude (for wild-type Hs ISU cluster transfer to Hs apo Fd, k(2) approximately 540 M(-1) min(-1), relative 56 M(-1) min(-1) for D37A ISU). This change in rate constant does not reflect any change in binding affinity of the ISU and Fd proteins. The pH dependencies of cluster transfer rates are similar for WT and D37A ISU, arguing against a role for Asp37 as a catalytic base, although evidence for general base catalysis mediating deprotonation of Cys from the apo target is supported by an observed pK(a) of 6.9 determined from the pH profiles for both WT and D37A ISU. Such a pK(a) value is at the lower limit for Cys and is common for solvent-accessible Cys thiols. The temperature dependence of the rate constant defining the cluster transfer reaction for wild type versus the aspartate derivative is distinct. Thermal activation parameters (DeltaH and DeltaS) are consistent with a solvent-accessible ISU-bound cluster, with desolvation as a principle barrier to cluster transfer. Experiments to determine the dependence of reaction rate constants on viscosity indicate cluster transfer to be rate-limiting. Fully oxidized cluster appears to be the natural state for transfer to target proteins. Reduced Fd does not readily reduce ISU-bound [2Fe-2S](2+) and does not promote cluster transfer to an apo Fd target.

Mechanical metamaterials are architected manmade materials that allow for unique behaviors not observed in nature, making them promising candidates for a wide range of applications. Existing metamaterials lack tunability as their properties can only be changed to a limited extent after the fabrication. Herein, a new magneto-mechanical metamaterial is presented that allows great tunability through a novel concept of deformation mode branching. The architecture of this new metamaterial employs an asymmetric joint design using hard-magnetic soft active materials that permits two distinct actuation modes (bending and folding) under opposite-direction magnetic fields. The subsequent application of mechanical compression leads to the deformation mode branching where the metamaterial architecture transforms into two distinctly different shapes, which exhibit very different deformations and enable great tunability in properties such as mechanical stiffness and acoustic bandgaps. Furthermore, this metamaterial design can be incorporated with magnetic shape memory polymers with global stiffness tunability, which also allows for the global shift of the acoustic behaviors. The combination of magnetic and mechanical actuations, as well as shape memory effects, impart wide tunable properties to a new paradigm of metamaterials.

Genetic studies of bacteria and eukaryotes have led to identification of several gene products that are involved in the biosynthesis of protein-bound iron-sulfur clusters. One of these proteins, ISU, is homologous to the N-terminus of bacterial NifU. The mature forms of His-tagged wild-type and D37A Schizosaccharomyces pombe ISU1 were cloned and overexpressed as inclusion bodies in Escherichia coli. The recombinant D37A protein was purified under denaturing conditions and subsequently reconstituted in vitro. By use of a 5-fold excess of iron and sulfide the reconstituted product was found to be red-brown in color, forming a homodimer of 17 kDa per subunit with approximately two iron atoms per monomer determined by protein and iron quantitation. UV-vis absorption and Mössbauer spectroscopies (delta = 0.29 +/- 0.05 mm/s; DeltaE(Q) = 0.59 +/- 0.05 mm/s) were used to characterize D37A ISU1 and show the presence of [2Fe-2S](2+) clusters in each subunit. Formation of the holo form of wild-type ISU1 was significantly less efficient using the same reconstitution conditions and is consistent with prior observations that the D37A substitution can stabilize protein-bound clusters. Relative to the human homologue, the yeast ISU is significantly less soluble at ambient temperatures. In both cases the native ISU1 is more sensitive to proton-mediated degradation relative to the D37A derivative. The lability of this family of proteins relative to [2Fe-2S] bearing ferredoxins most likely is of functional relevance for cluster transfer chemistry. Mössbauer parameters obtained for wild-type ISU1 (delta = 0.31 +/- 0.05 mm/s; DeltaE(Q) = 0.64 +/- 0.05 mm/s) were similar to those obtained for the D37A derivative. Cluster transfer from ISU1 to apo Fd is demonstrated: the first example of transfer from an ISU-type protein. A lower limit for k(2) of 80 M(-1) min(-1) was established for WT cluster transfer and a value of 18 M(-1) min(-1) for the D37A derivative. Finally, we have demonstrated through cross-linking studies that ferredoxin, an electron-transport protein, forms a complex with ISU1 in both apo and holo states. Cross-linking of holo ISU1 with holo Fd is consistent with a role for redox chemistry in cluster assembly and may mimic the intramolecular complex already defined in NifU.

Shape-morphing magnetic soft materials, composed of magnetic particles in a soft polymer matrix, can transform shape reversibly, remotely, and rapidly, finding diverse applications in actuators, soft robotics, and biomedical devices. To achieve on-demand and sophisticated shape morphing, the manufacture of structures with complex geometry and magnetization distribution is highly desired. Here, a magnetic dynamic polymer (MDP) composite composed of hard-magnetic microparticles in a dynamic polymer network with thermally responsive reversible linkages, which permits functionalities including targeted welding for magnetic-assisted assembly, magnetization reprogramming, and permanent structural reconfiguration, is reported. These functions not only provide highly desirable structural and material programmability and reprogrammability but also enable the manufacturing of functional soft architected materials such as 3D kirigami with complex magnetization distribution. The welding of magnetic-assisted modular assembly can be further combined with magnetization reprogramming and permanent reshaping capabilities for programmable and reconfigurable architectures and morphing structures. The reported MDP are anticipated to provide a new paradigm for the design and manufacture of future multifunctional assemblies and reconfigurable morphing architectures and devices.

Biogenesis of pyrroloquinoline quinone (PQQ) in Klebsiella pneumoniae requires the expression of six genes (pqqA-F). One of these genes (pqqE) encodes a 43 kDa protein (PqqE) that plays a role in the initial steps in PQQ formation (Veletrop et al. (1995) J. Bacteriol. 177, 5088-5098). PqqE contains two highly conserved cysteine motifs at the N and C-termini, with the N-terminal motif comprised of a consensus sequence of CX 3 CX 2 C that is unique to a family of proteins known as radical Sadenosyl-L-methionine (SAM) enzymes (Sofia et al. (2001) Nucleic Acids Res. 29, 1097-1106. PqqE from K. pneumoniae was cloned into E. coli and expressed as the native protein and with an Nterminal His 6 -tag. Anaerobic expression and purification of the His 6 -tag PqqE results in an enzyme with a brownish-red hue indicative of Fe-S cluster formation. Spectroscopic and physical analyses indicate that PqqE contains a mixture of Fe-S clusters, with the predominant form of the enzyme containing two [4Fe-4S] clusters. PqqE isolated anaerobically yields active enzyme capable of cleaving SAM to methionine and 5′-deoxyadenosine in an uncoupled reaction (k obs = 0.011 ± 0.001 min -1 ). In this reaction, the 5′-deoxyadenosyl radical either abstracts a hydrogen atom from a solvent accessible position in the enzyme or obtains a proton and electron from buffer. The putative PQQ substrate PqqA has not yet been shown to be modified by PqqE, implying either that PqqA must be modified before becoming the substrate for PqqE and/or that another protein in the biosynthetic pathway is critical for the initial steps in PQQ biogenesis. KeywordsQuinones; cofactor; biogenesis; S-adenosyl-methionine; pyrroloquinoline quinone; radicals; ironsulfur clusters † This work was supported by research grants from the National Institutes of Health (GM39296 to JPK, GM073789 to DB and F32GM080795 to SRW) and Howard Hughes Medical Institute (to DK). *To whom correspondence should be sent: tel: 510-642-7460; fax: 510-643-6232; klinman@berkeley.edu. # Present address: Decode Genetics, Sturlagata 8, IS-101 Reykjavik, Iceland. Δ Present address: Department of Applied Chemistry, National Chiao Tung University, 1001 Hsueh Road, Hsinchu, Taiwan, Republic of China.Supporting Information Available: Methods for the aerobic and anaerobic growth and induction of E. coli BL21(DE3) cells harboring the pET24b-pqqE plasmid, aerobic purification of PqqE, anaerobic reconstitution of PqqE with iron and sulfide ions, synthesis and purification of SAM, and a detailed description of the high resolution mass spectrometry experiments. This material is available free of charge via the Internet at http://pubs.acs.org. NIH Public Access Author ManuscriptBiochemistry. Author manuscript; available in PMC 2010 October 27. NIH-PA Author ManuscriptNIH-PA Author Manuscript NIH-PA Author ManuscriptThe broad spectrum of chemical reactions catalyzed by enzymes frequently requires functional groups that are unavailable from the side chains of the 20 naturally occurring amino acids. In particula...

A BODIPY-based fluorescent probe, HCSe, has been successfully developed for the rapid detection of hypochlorous acid based on the specific HOCl-promoted oxidation of diphenyl selenide in response to the amount of HOCl. Confocal fluorescence microscopy imaging using RAW264.7 cells showed that the new probe HCSe could be used as an effective fluorescent probe for detecting HOCl in living cells.