Cu(II)-mediated tautomerization for the pyrazole-nitrile coupling reaction.

This study investigates the mechanism of prototropic tautomerization in metal-bound asymmetric pyrazole (R-PzH) ligands during Cu(II)-mediated PzH-MeCN coupling reactions. Intrinsic prototropic tautomerization of metal-bound ligands has not been previously documented. Various new bis-pyrazolylamidino Cu(II) complexes, [Cu(R-Pz(HNC(Me)))(ClO)], from the coupling reaction, and tetrakis pyrazole Cu(II) complexes, [Cu(R-PzH)(ClO)], with symmetric and asymmetric -monosubstituted R-PzH ligands were synthesized and characterized.

Targeting DNA junction sites by bis-intercalators induces topological changes with potent antitumor effects.

Targeting inter-duplex junctions in catenated DNA with bidirectional bis-intercalators is a potential strategy for enhancing anticancer effects. In this study, we used d(CGTATACG)2, which forms a tetraplex base-pair junction that resembles the DNA-DNA contact structure, as a model target for two alkyl-linked diaminoacridine bis-intercalators, DA4 and DA5. Cross-linking of the junction site by the bis-intercalators induced substantial structural changes in the DNA, transforming it from a B-form helical end-to-end junction to an over-wounded side-by-side inter-duplex conformation with A-DNA characteristics and curvature.

Chloride- and Hydrosulfide-Bound 2Fe Complexes as Models of the Oxygen-Stable State of [FeFe] Hydrogenase.

[FeFe] hydrogenases demonstrate remarkable catalytic efficiency in hydrogen evolution and oxidation processes. However, susceptibility of these enzymes to oxygen-induced degradation impedes their practical deployment in hydrogen-production devices and fuel cells. Recent investigations into the oxygen-stable (H) state of the H-cluster revealed its inherent capacity to resist oxygen degradation.

The effect of anions in the synthesis and structure of pyrazolylamidino copper(II) complexes.

Six new pyrazolylamidino Cu(II) complexes are synthesized directly from the reactions of Cu(X) salts (X = ClO, BF, or Cl) and pyrazole (pzH) in nitrile solution (RCN, R = Me or Et) at 298 K the metal-mediated coupling of RCN with pzH: [Cu(HNC(R)pz)(X)] (X = ClO or BF, R = Me, 1 or 7 and Et, 2 or 8, respectively) and dichloro Cu(II) complexes [CuCl(μ-Cl)(HNC(Me)pz)] (3) and [CuCl(HNC(Et)pz)] (4). Four more new complexes, [Cu(μ-Cl)(HNC(Me)pz)(pzH)][X] (X = ClO, 5 and BF, 9) and [Cu(μ-Cl)(HNC(Et)pz)(pzH)(X)] (X = ClO, 6 and BF, 10), are obtained indirectly from the anion substitution reaction with Cl ions in 1 and 7, and 2 and 8, respectively. All complexes are characterized by EA, FTIR, UV-vis and EPR spectroscopy and X-ray crystallographic analyses.

Catalytic O activation toward oxidative N-S bond formation by a thiolato Fe(III) complex.

Compounds with the benzisothiazol-3-one (BIT) skeleton perform excellently in the pharmaceutical field, although current synthetic methods remain limited in terms of synthetic efficiency. Herein, we report the catalytic intramolecular N-S bond formation for BITs from easily prepared disulfide precursors by an Fe(III) dithiolate through O activation at 298 K. Interestingly, the catalytic performance is enhanced by substituting O with a milder O-donor oxidant, ONMe.

Targeting the ALS/FTD-associated A-DNA kink with anthracene-based metal complex causes DNA backbone straightening and groove contraction.

The use of a small molecule compound to reduce toxic repeat RNA transcripts or their translated aberrant proteins to target repeat-expanded RNA/DNA with a G4C2 motif is a promising strategy to treat C9orf72-linked disorders. In this study, the crystal structures of DNA and RNA-DNA hybrid duplexes with the -GGGCCG- region as a G4C2 repeat motif were solved. Unusual groove widening and sharper bending of the G4C2 DNA duplex A-DNA conformation with B-form characteristics inside was observed.

Dioxygen activation by a dinuclear thiolate-ligated Fe(ii) complex.

Dioxygen activation by FeII thiolate complexes is relatively rare in biological and chemical systems because the sulfur site is at least as vulnerable as the iron site to oxidative modification. O2 activation by FeII-SR complexes with thiolate bound trans to the O2 binding site generally affords the FeIV[double bond, length as m-dash]O intermediate and oxidized thiolate. On the other hand, O2 activation by Fe(ii)-SR complexes with thiolate bound cis to the O2 binding site generates FeIII-O-FeIII or S-oxygenated complexes.

Crystal Structure Analysis of the Repair of Iron Centers Protein YtfE and Its Interaction with NO.

Molecular mechanisms underlying the repair of nitrosylated [Fe-S] clusters by the microbial protein YtfE remain poorly understood. The X-ray crystal structure of YtfE, in combination with EPR, magnetic circular dichroism (MCD), UV, and (17) O-labeling electron spin echo envelope modulation measurements, show that each iron of the oxo-bridged Fe(II) -Fe(III) diiron core is coordinatively unsaturated with each iron bound to two bridging carboxylates and two terminal histidines in addition to an oxo-bridge. Structural analysis reveals that there are two solvent-accessible tunnels, both of which converge to the diiron center and are critical for capturing substrates.

N-[2-(Methyl-sulfan-yl)phen-yl]-2-sulfanylbenzamide.

In the title compound, C(14)H(13)NOS(2), the S atom with the methyl group is involved in an intra-molecular hydrogen bond with the amido H atom. In the crystal, the sulfanyl H atoms form inter-molecular hydrogen bonds with the O atoms, connecting the mol-ecules into zigzag chains along the c axis. The two aromatic rings exhibit a small interplanar angle of 16.

Selective encapsulation of volatile and reactive methyl iodide.

A simple organic molecular container can selectively encapsulate the volatile and highly reactive MeI through hydrogen-bonding interactions in solution. The remarkable encapsulation of MeI without self-methylation of the container appears to be determined by the complementary binding sites and the rigidity of the hydrogen-bonding array constrained by the molecular framework.

N,N'-Bis[(1H-imidazol-1-yl)meth-yl]-2,2'-(disulfanedi-yl)dianiline.

The symmetrical title compound, C(20)H(20)N(6)S(2), contains a disulfide bond of 2.0884 (6) Å. The C-S-S-C torsion angle is -59.

Assembly and disassembly of a Zn10 high-nuclearity circular helicate.

A nano-scale decanuclear Zn(II) circular helicate is synthesized without the aid of counteranions during the assembly process, and can be totally disassembled into its reactants by specific anions.

Selective capture of volatile iodine using amorphous molecular organic solids.

A simple shape-persistent organic molecular container is capable of selective absorption and storage of I(2(g)) over water vapor and NO gas even in its amorphous solid state. In addition, the strongly associated I(2) can be efficiently released from the charged container in organic solvents under ambient conditions.

trans-Diacetonitrile-tetra-kis(1H-pyrazole-κN)nickel(II) dinitrate.

In the title complex, [Ni(CH(3)CN)(2)(C(3)H(4)N(2))(4)](NO(3))(2), the cation lies on an inversion center and adopts an octa-hedral coordination geometry about the Ni atom. The two acetonitrile ligands are in a trans conformation. N-H⋯O hydrogen bonds between cations and anions link the complex mol-ecules into one-dimensional chains running parallel to [100].

Spectroscopic and computational studies of reduction of the metal versus the tetrapyrrole ring of coenzyme F430 from methyl-coenzyme M reductase.

Methyl-coenzyme M reductase (MCR) catalyzes the final step in methane biosynthesis by methanogenic archaea and contains a redox-active nickel tetrahydrocorphin, coenzyme F430, at its active site. Spectroscopic and computational methods have been used to study a novel form of the coenzyme, called F330, which is obtained by reducing F430 with sodium borohydride (NaBH4). F330 exhibits a prominent absorption peak at 330 nm, which is blue shifted by 100 nm relative to F430.

Spectroscopic and kinetic studies of the reaction of bromopropanesulfonate with methyl-coenzyme M reductase.

Methyl-coenzyme M reductase (MCR) catalyzes the final step of methanogenesis in which coenzyme B and methyl-coenzyme M are converted to methane and the heterodisulfide, CoMS-SCoB. MCR also appears to initiate anaerobic methane oxidation (reverse methanogenesis). At the active site of MCR is coenzyme F430, a nickel tetrapyrrole.

The P174L mutation in human Sco1 severely compromises Cox17-dependent metallation but does not impair copper binding.

Sco1 is a metallochaperone that is required for copper delivery to the Cu(A) site in the CoxII subunit of cytochrome c oxidase. The only known missense mutation in human Sco1, a P174L substitution in the copper-binding domain, is associated with a fatal neonatal hepatopathy; however, the molecular basis for dysfunction of the protein is unknown. Immortalized fibroblasts from a SCO1 patient show a severe deficiency in cytochrome c oxidase activity that was partially rescued by overexpression of P174L Sco1.

Human Sco1 and Sco2 function as copper-binding proteins.

The function of human Sco1 and Sco2 is shown to be dependent on copper ion binding. Expression of soluble domains of human Sco1 and Sco2 either in bacteria or the yeast cytoplasm resulted in the recovery of copper-containing proteins. The metallation of human Sco1, but not Sco2, when expressed in the yeast cytoplasm is dependent on the co-expression of human Cox17.

Functional analysis of the domains in Cox11.

Cox11 is an intrinsic mitochondrial membrane protein essential for the assembly of an active cytochrome c oxidase complex. Cox11 is tethered to the mitochondrial inner membrane by a single transmembrane helix. Domain mapping was carried out to determine the functional segments of the Cox11 protein.

Specific copper transfer from the Cox17 metallochaperone to both Sco1 and Cox11 in the assembly of yeast cytochrome C oxidase.

The assembly of the copper sites in cytochrome c oxidase involves a series of accessory proteins, including Cox11, Cox17, and Sco1. The two mitochondrial inner membrane proteins Cox11 and Sco1 are thought to be copper donors to the Cu(B) and Cu(A) sites of cytochrome oxidase, respectively, whereas Cox17 is believed to be the copper donor to Sco1 within the intermembrane space. In this report we show Cox17 is a specific copper donor to both Sco1 and Cox11.

Nickel oxidation states of F(430) cofactor in methyl-coenzyme M reductase.

Magnetic circular dichroism (MCD) spectroscopy and variable-temperature variable-field MCD are used in combination with density functional theory (DFT) and time-dependent DFT (TD-DFT) calculations to characterize the so-called ox1-silent, red1, and ox1 forms of the Ni-containing cofactor F430 in methyl-coenzyme M reductase (MCR). Previous studies concluded that the ox1 state, which is the precursor of the key reactive red1 state of MCR, is a Ni(I) species that derives from one-electron reduction of the Ni(II)-containing ox1-silent state. However, our absorption and MCD data provide compelling evidence that ox1 is actually a Ni(II) species.

Spectroscopic and computational characterization of the nickel-containing F430 cofactor of methyl-coenzyme M reductase.

Methyl-coenzyme M reductase (MCR) catalyzes the terminal reaction in methanogenesis, the formation of methane from methyl-coenzyme M and coenzyme B. The active site of MCR binds the prosthetic group F(430), a unique nickel hydrocorphin cofactor. Here, spectroscopy and computations are employed in developing detailed electronic descriptions of the Ni(II) and Ni(I) forms of the free cofactor.

Rapid ligand exchange in the MCRred1 form of methyl-coenzyme M reductase.

Methyl-coenzyme M reductase (MCR) from Methanothermobacter marburgensis (Mtm), catalyses the final step in methane synthesis in all methanogenic organisms. Methane is produced by coenzyme B-dependent two-electron reduction of methyl-coenzyme M. At the active site of MCR is the corphin cofactor F(430), which provides four-coordination through the pyrrole nitrogens to a central Ni ion in all states of the enzyme.

X-ray absorption and resonance Raman studies of methyl-coenzyme M reductase indicating that ligand exchange and macrocycle reduction accompany reductive activation.

Methyl-coenzyme M reductase (MCR) catalyzes methane formation from methyl-coenzyme M (methyl-SCoM) and N-7-mercaptoheptanoylthreonine phosphate (CoBSH). MCR contains a nickel hydrocorphin cofactor at its active site, called cofactor F(430). Here we present evidence that the macrocyclic ligand participates in the redox chemistry involved in catalysis.