Akira Onoda

The hydrogen-evolving diiron complex, (μ-S)2Fe2(CO)6 with a tethered maleimide moiety was synthesized and covalently embedded within the cavity of a rigid β-barrel protein matrix by coupling a maleimide moiety to a cysteine residue within the β-barrel. The (μ-S)2Fe2(CO)6 core within the cavity was characterized by UV–vis absorption and a characteristic CO vibration determined by IR measurements. The diiron complex embedded within the cavity retains the necessary catalytic activity (TON up to 130

The novel intramolecularly NH...O hydrogen-bonded Ca(II)-aryl sulfonate complex, [Ca2(SO3-2-t-BuCONHC6H4)2(H2O)4]n(2-t-BuCONHC6H4SO3)2n (1), sulfonate anion, (HNEt3)(SO3-2-t-BuCONHC6H4) (2a), (PPh4)(SO3-2-t-BuCONHC6H4) (2b), (n-Bu4N)(SO3-2-t-BuCONHC6H4) (2c), and sulfonic acid, 2-t-BuCONHC6H4SO3H (3), were synthesized. The structures of 1, 2a, and 2b depict the presence of the formation of NH...O hydrogen bonds between the amide NH and S-O oxygen for a series of compounds as determined by IR and

Our group recently prepared a hybrid catalyst containing a rhodium complex, Rh(Cp)(cod), with a maleimide moiety at the peripheral position of the Cp ligand. This compound was then inserted into a β-barrel protein scaffold of a mutant of aponitrobindin (Q96C) via a covalent linkage. The hybrid protein is found to act as a polymerization catalyst and preferentially yields trans-poly(phenylacetylene) (PPA), although the rhodium complex without the protein scaffold normally produces cis PPA.

All connected: a protein-immobilized electrode comprising hierarchical assemblies of photoactive cytochrome b(562) reconstituted with zinc protoporphyrin IX exhibits remarkably enhanced photocurrent generation relative to an electrode bearing a single zinc-substituted hemoprotein layer. The protein oligomers, which bear a covalently linked protoporphyrin group, assemble by a supramolecular heme/heme pocket interaction.

Cellobiose dehydrogenase (CDH) is a dual domain flavocytochrome, which consists of a dehydrogenase (DH) domain containing a flavin adenine dinucleotide and a cytochrome (CYT) domain containing <i>b</i>-type heme. To directly visualize the dynamic domain motion of class-I CDH from <i>Phanerochaete chrysosporium</i> (<i>Pc</i>CDH) during catalysis using high-speed atomic force microscopy, the apo-form of <i>Pc</i>CDH was anchored to a heme-immobilized flat gold surface that can specifically fix th

Abstract A unique π‐expanded reaction cavity tethering a polycyclic moiety which provides a platform for substrate binding was constructed within the robust β‐barrel structure of nitrobindin (NB). NB variants with cavities of different sizes and shapes are coupled with N ‐(1‐pyrenyl)maleimide ( Pyr ) to prepare a series of NB‐ Pyr conjugates. The orientation of the pyrene moiety is fixed within the cavity by the coupling reaction. The fluorescent quenching analysis of NB‐ Pyr indicates that azac

Interaction of apohemoprotein with a covalently immobilized heme moiety onto a gold nanoparticle surface resulted in supramolecular hemoprotein-gold nanoparticle conjugates. The addition of an apohemoprotein dimer further led to a densely-packed hemoprotein-gold nanoparticle assembly, which was visualized by TEM and AFM measurements.

Site-specific modification of peptides and proteins is a key aspect of protein engineering. We developed a method for modification of the N terminus of proteins using 1H-1,2,3-triazole-4-carbaldehyde (TA4C) derivatives, which can be prepared in one step. The N-terminal specific labeling of bioactive peptides and proteins with the TA4C derivatives proceeds under mild reaction conditions in excellent conversion (angiotensin I: 92 %, ribonuclease A: 90 %). This method enables site-specific conjugat

Nonprecious metal electrocatalysts are being explored as alternatives to platinum-group metal electrocatalysts for the oxygen reduction reaction (ORR) which is required for cathode materials in fuel cells. Herein, we describe a new method for preparing bimetallic nitrogen-containing carbon catalysts with high ORR activity using π-expanded M(salen) precursors. The M/N/C and bimetallic FeM/N/C ORR catalysts were obtained by pyrolysis of a mixture of a carbon support (Vulcan XC-72R) and the metal c

Pyrolytically prepared iron and nitrogen codoped carbon (Fe/N/C) catalysts are promising nonprecious metal electrocatalysts for the oxygen reduction reaction (ORR) in fuel cell applications. Fabrication of the Fe/N/C catalysts with Fe-N<i>_x</i> active sites having precise structures is now required. We developed a strategy for thermally controlled construction of the Fe-N<i>_x</i> structure in Fe/N/C catalysts by applying a bottom-up synthetic methodology based on a N-doped

Three new polynuclear Ca(II)- and Na(I) phosphate complexes with two strategically oriented bulky amide groups, 2,6-(PhCONH)(2)C(6)H(3)OPO(3)H(2), were synthesized, including one with a zigzag-chain, [Ca(II)[O(3)POC(6)H(3)-2,6-(NHCOPh)(2)](H(2)O)(4)(EtOH)](n), a cyclic-octanuclear form, [Ca(II)(8)[O(3)POC(6)H(3)-2,6-(NHCOPh)(2)](8)(O=CHNMe(2))(8)(H(2)O)(12)], and a hexanuclear complex, (NHEt(3))[Na(3)[O(3)POC(6)H(3)-2,6-(NHCOPh)(2)](2)(H(2)O)(MeOH)(7)]. X-ray crystallography revealed that all ha

Abstract The formation of the NH···O hydrogen bonds of carboxylic acids, 2,6-(t-BuCONH)2C6H3COOH (1) and 2-t-BuCONH-6-MeC6H3COOH (2), carboxylate, [NEt4][2,6-(t-BuCONH)2C6H3COO] (3), and a mixed complex, [N(n-Pr)4][H{2,6-(t-BuCONH)2C6H3(COO)}2] (4), were determined by X-ray structure analysis, 1H NMR, and IR spectroscopy, both in the solid state and in solution. The amide NH group forms weak intramolecular hydrogen bond between the NH and O=C group, and no NH···OH hydrogen bond is formed in the

Site-specific modification of peptides and proteins is an important method for introducing an artificial function to the protein surface. Recently, we found that new bioconjugation reagents, 6-(azidomethyl)-2-pyridinecarbaldehyde (6AMPC) derivatives, allow specific N-terminal modification and enhance the reaction rate of the subsequent bioconjugation in a chelation-assisted CuAAC reaction. The N-terminal specific azide-labeling of bioactive peptides and proteins occurs under mild reaction condit