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Genetically introducing covalent bonds into proteins in vivo with residue specificity is affording innovative ways for protein research and engineering, yet latent bioreactive unnatural amino acids (Uaas) genetically encoded to date react with one to few natural residues only, limiting the variety of proteins and the scope of applications amenable to this technology. Here we report the genetic encoding of (2 R)-2-amino-3-fluoro-3-(4-((2-nitrobenzyl)oxy) phenyl) propanoic acid (FnbY) in Escherichia coli and mammalian cells. Upon photoactivation, FnbY generated a reactive quinone methide (QM), which selectively reacted with nine natural amino acid residues placed in proximity in proteins directly in live cells. In addition to Cys, Lys, His, and Tyr, photoactivated FnbY also reacted with Trp, Met, Arg, Asn, and Gln, which are inaccessible with existing latent bioreactive Uaas. FnbY thus dramatically expanded the number of residues for covalent targeting in vivo. QM has longer half-life than the intermediates of conventional photo-cross-linking Uaas, and FnbY exhibited cross-linking efficiency higher than p-azido-phenylalanine. The photoactivatable and multitargeting reactivity of FnbY with selectivity toward nucleophilic residues will be valuable for addressing diverse proteins and broadening the scope of applications through exploiting covalent bonding in vivo for chemical biology, biotherapeutics, and protein engineering.

Expansion of the genetic code with unnatural amino acids (Uaas) has significantly increased the chemical space available to proteins for exploitation. Due to the inherent limitation of translational machinery and the required compatibility with biological settings, function groups introduced via Uaas to date are restricted to chemically inert, bioorthogonal, or latent bioreactive groups. To break this barrier, here we report a new strategy enabling the specific incorporation of biochemically reactive amino acids into proteins. A latent bioreactive amino acid is genetically encoded at a position proximal to the target natural amino acid; they react via proximity-enabled reactivity, selectively converting the latter into a reactive residue in situ. Using this Genetically Encoded Chemical COnversion (GECCO) strategy and harnessing the sulfur-fluoride exchange (SuFEx) reaction between fluorosulfate-l-tyrosine and serine or threonine, we site-specifically generated the reactive dehydroalanine and dehydrobutyrine into proteins. GECCO works both inter- and intramolecularly, and is compatible with various proteins. We further labeled the resultant dehydroalanine-containing protein with thiol-saccharide to generate glycoprotein mimetics. GECCO represents a new solution for selectively introducing biochemically reactive amino acids into proteins and is expected to open new avenues for exploiting chemistry in live systems for biological research and engineering.

Introducing new chemical reactivity into proteins in living cells would endow innovative covalent bonding ability to proteins for research and engineering in vivo. Latent bioreactive unnatural amino acids (Uaas) can be incorporated into proteins to react with target natural amino acid residues via proximity-enabled reactivity. To expand the diversity of proteins amenable to such reactivity in vivo, a chemical functionality that is biocompatible and able to react with multiple natural residues under physiological conditions is highly desirable. Here we report the genetic encoding of fluorosulfate-l-tyrosine (FSY), the first latent bioreactive Uaa that undergoes sulfur-fluoride exchange (SuFEx) on proteins in vivo. FSY was found nontoxic to Escherichia coli and mammalian cells; after being incorporated into proteins, it selectively reacted with proximal lysine, histidine, and tyrosine via SuFEx, generating covalent intraprotein bridge and interprotein cross-link of interacting proteins directly in living cells. The proximity-activatable reactivity, multitargeting ability, and excellent biocompatibility of FSY will be invaluable for covalent manipulation of proteins in vivo. Moreover, genetically encoded FSY hereby empowers general proteins with the next generation of click chemistry, SuFEx, which will afford broad utilities in chemical biology, drug discovery, and biotherapeutics.

The mononuclear and dinuclear iron complexes are studied by using iron L-edge X-ray absorption spectroscopy. The sums of individual complex spectral features describe the trapped valence dinuclear complex spectra for the isolated Fe(II) and Fe(III). The atomic multiplet calculation enables the interpretation of the spectra for the oxidation states of the atoms.

High-resolution manganese X-ray fluorescence spectroscopy revealed the dependency of Kbeta(1,3) peak position and Kbeta' peak intensity on the oxidation state and spin state of Mn. Kbeta' satellite for high-spin compounds, which was not observed in low-spin compounds, was detected in Mn(III) compounds. The transformation of Mn(II) to Mn(III) and then to Mn(IV) resulted in a decrease in the Kbeta' peak intensity.

Ligand field atomic multiplet studies of L(sub 2,3) edges of structurally different Ni compounds reveal a correlation between NiL edge X-ray absorption spectra and the Ni-site electronic structure. The L edge is vulnerable to spin and oxidation states and structural symmetries of Ni sites. MCD analysis of an Ni-substituted rubredoxin reveals distorted T(sub d) symmetry and zero field splitting.

The O-antigen biosynthesis in Escherichia coli O86, an important bacterial strain that possesses strong blood group B activity is elucidated. A new bacterial glycosyltransferase equivalent to human blood group transferase B (GTB) is identified.

Currently, to obtain new ultraviolet (UV) nonlinear optical (NLO) materials with large second-harmonic generation (SHG) response and short SHG phase-matching cutoff wavelength (λ PM ) is still very challenging. Herein, through evolving the KBe 2 BO 3 F 2 (KBBF) structure to a carbonate system, a novel hydroxycarbonate UV NLO crystal, NaZnCO 3 (OH), was successfully synthesized. It not only possessed the typical structural characteristics of KBBF but also enhanced the bonding force between functional layers. Remarkably, in this crystal, the rare coexistence of a very large SHG response of 5.2 × KH 2 PO 4 (KDP, @1064 nm) and short type-I SHG λ PM of 201 nm had been achieved, indicating that it was a promising UV NLO crystal. This work showed the great significance of KBBF structure evolution and provided new opportunity to design UV NLO materials with good performance.

We improved the effectiveness of Pt monolayer electrocatalysts for the oxygen-reduction reaction (ORR) using a novel approach to fine-tuning the Pt monolayer interaction with its support, exemplified by an annealed Pd(3)Fe(111) single-crystal alloy support having a segregated Pd layer. Low-energy ion scattering and low-energy electron diffraction studies revealed that a segregated Pd layer, with the same structure as Pd (111), is formed on the surface of high-temperature-annealed Pd(3)Fe(111). This Pd layer is considerably more active than Pd(111); its ORR kinetics is comparable to that of a Pt(111) surface. The enhanced catalytic activity of the segregated Pd layer compared to that of bulk Pd apparently reflects the modification of Pd surface's electronic properties by underlying Fe. The Pd(3)Fe(111) suffers a large loss in ORR activity when the subsurface Fe is depleted by potential cycling (i.e., repeated excursions to high potentials in acid solutions). The Pd(3)Fe(111) surface is an excellent substrate for a Pt monolayer ORR catalyst, as verified by its enhanced ORR kinetics on PT(ML)/Pd/Pd(3)Fe(111). Our density functional theory studies suggest that the observed enhancement of ORR activity originates mainly from the destabilization of OH binding and the decreased Pt-OH coverage on the Pt/Pd/Pd(3)Fe(111) surface. The activity of Pt(ML)/Pd(111) and Pt(111) is limited by OH removal, whereas the activity of Pt(ML)/Pd/Pd(3)Fe(111) is limited by the O-O bond scission, which places these two surfaces on the two sides of the volcano plot.

Reaction of Pb(OH)3- with ClO- in the presence of surfactant CTAB under conventional conditions resulted in PbO2 nanorods, whereas the reaction under hydrothermal conditions afforded Pb3O4 nanorods, as confirmed by X-ray powder diffraction and transmission electron microscopy (TEM). Selected area electron diffraction (SEAD) and high-resolution TEM (HRTEM) revealed that both PbO2 and Pb3O4 nanorods are single crystalline. For the formation of Pb3O4 nanorods, it is reasonable that PbO2 slowly decomposes to Pb3O4 under hydrothermal conditions, while retaining the morphology of PbO2.