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Vincent L Pecoraro

Publications and source records attributed to Vincent L Pecoraro.

At least 37 records · Page 2Linked to original sources
PubMed2004

Quantum mechanical models of the resting state of the vanadium-dependent haloperoxidase.

Density functional theory has been used to investigate structural and electronic properties of complexes related to the resting form of the active site of vanadium haloperoxidase as a function of environment and protonation state. Results obtained by studying models of varying size and complexity highlight the influence of environment and protonation state on the structure and stability of the metal cofactor. The study shows that, in the trigonal bipyramidal active site, where one axial position is occupied by a key histidine, the trans position cannot contain a terminal oxo group. Further, a highly negatively charged vanadate unit is not stable. Protonation of at least one equatorial oxo ligand appears necessary to stabilize the metal cofactor. The study also indicates that, while at rest within the protein, the vanadate unit is most likely an anion with an axial hydroxide and an equatorial plane containing two oxos and a hydroxide. For the neutral, protonated state of the vanadate unit, there were two minima found. The first structure is characterized by an axial water with two oxo and one hydroxo group in the equatorial plane. The second structure contains an axial hydroxo group and an equatorial plane composed of one oxo and two hydroxo oxygen atoms. These two species are not significantly different in energy, indicating that either form may be important during the catalytic cycle. These data support the initial crystallographic assignment of an axially bound hydroxide, but an axial water is also a possibility. This study also shows that the protonation state of the vanadate ion is most likely greater than previously proposed.

Binding Sites↗
PubMed2004

XANES evidence against a manganyl species in the S3 state of the oxygen-evolving complex.

Manganyl Mn=O species have been suggested as possible intermediates in photosynthetic water oxidation and as the reactive species in asymmetric olefin epoxidation. The first X-ray absorption spectrum for a MnV=O complex is reported. Comparison of the EXAFS data for Na[MnV=O(HMPAB) with those for lower-valent Mn complexes suggests that EXAFS measurements and edge-energy measurements are unlikely to have sufficient sensitivity to reliably reflect the presence of Mn=O species. In contrast, the preedge transition for Na[MnV=O(HMPAB) is 4-fold more intense than the most intense preedge transition observed for nonmanganyl complexes. This increase in intensity is shown to be sufficiently sensitive to allow detection of a manganyl species if it is formed. These data together with published data for the photosynthetic oxygen-evolving complex provide strong evidence against the presence of manganyl Mn=O species in the oxygen-evolving complex through the S3 state.

Manganese↗
PubMed2004

The first spectroscopic model for the S1 state multiline signal of the OEC.

The parallel-mode electron paramagnetic resonance (EPR) spectrum of the S(1) state of the oxygen-evolving complex (OEC) shows a multiline signal centered around g=12, indicating an integer spin system. The series of [Mn(2)(2-OHsalpn)(2)] complexes were structurally characterized in four oxidation levels (Mn(II)(2), Mn(II)Mn(III), Mn(III)(2), and Mn(III)Mn(IV)). By using bulk electrolysis, the [Mn(III)Mn(IV)(2-OHsalpn)(2)(OH)] is oxidized to a species that contains Mn(IV) oxidation state as detected by X-ray absorption near edge spectroscopy (XANES) and that can be formulated as Mn(IV)(4) tetramer. The parallel-mode EPR spectrum of this multinuclear Mn(IV)(4) complex shows 18 well-resolved hyperfine lines center around g=11 with an average hyperfine splitting of 36 G. This EPR spectrum is very similar to that found in the S(1) state of the OEC. This is the first synthetic manganese model complex that shows an S(1)-like multiline spectrum in parallel-mode EPR.

Electrochemistry↗
PubMed2003

An isocratic separation of underivatized gentamicin components, 1H NMR assignment and protonation pattern.

A simple method for the separation of the major components of commercial gentamicin sulfate (C-1, C-1a, C-2, C-2a) by high-performance liquid chromatography (HPLC) on an analytical and a semipreparative scale was developed. The method utilized ion-pair reversed-phase chromatography, isocratic elution with an aqueous solution containing 9% trifluoroacetic acid and 2.5% acetonitrile as the mobile phase at a flow rate of 2 and 9 mL/min for analytical and semipreparative columns, respectively. Detection was carried out at 213 nm without derivatization. The protonation pattern of the separated gentamicins was determined by potentiometry and 15N and 1H NMR. The full proton NMR assignment for gentamicin C-1 was obtained through the use of 1H 1D and 2D 1H-1H COSY measurements.

Acetonitriles↗
PubMed2003

A cationic 24-MC-8 manganese cluster with ring metals possessing three oxidation states [Mn(II)4Mn(III)6Mn(IV)2(mu4-O)2(mu3-O)4(mu3-OH)4(mu3-OCH3)2(pko)12](OH)(ClO4)3.

Reaction of Mn(ClO4)2 with di-pyridyl ketone oxime, (2-py)2C=NOH, gives the novel cluster [Mn(II)4Mn(III)6Mn(IV)2(mu4-O)2(mu3-O)4(mu3-OH)4(mu3-OCH3)2(pko)12](OH)(ClO4)3 1. It is the only example of a 24-MC-8, and the first metallacrown with ring metal ions in three different oxidation states. Magnetic measurements show antiferromagnetic behavior.

Journal Article↗
PubMed2003

Catalytic oxidation of 3,5-Di-tert-butylcatechol by a series of mononuclear manganese complexes: synthesis, structure, and kinetic investigation.

The manganese compounds [Mn(bpia)(OAc)(OCH(3))](PF(6)) (1), [Mn(bipa)(OAc)(OCH(3))](PF(6)) (2), [Mn(bpia)(Cl)(2)](ClO(4)) (3), [Mn(bipa)(Cl)(2)](ClO(4)) (4), [Mn(Hmimppa)(Cl)(2)] x CH(3)OH (5), and [Mn(mimppa)(TCC)] x 2CHCl(3) (6) (bpia = bis(picolyl)(N-methylimidazole-2-yl)amine; bipa = bis(N-methylimidazole-2-yl)(picolyl)amine; Hmimppa = ((1-methylimidazole-2-yl)methyl)((2-pyridyl)methyl)(2-hydroxyphenyl)amine; TCC = tetrachlorocatechol) were synthesized and characterized by various techniques such as X-ray crystallography, mass spectrometry, IR, EPR, and UV/vis spectroscopy, cyclic voltammetry, and elemental analysis. 1 and 2 crystallize in the triclinic space group Ponemacr; (No. 2), 4 and 6 crystallize in the monoclinic space group P2(1)/n (No. 14), and 5 crystallizes in the orthorhombic space group Pna2(1). Complexes 1-4 are structurally related to the proposed active site of the manganese-dependent extradiol-cleaving catechol dioxygenase exhibiting an N(4)O(2) donor set (1 and 2) or N(4)Cl(2) donor set (3 and 4). Cyclic voltammetric data show that the substitution of oxygen donor atoms with chloride causes a shift of redox potentials to more positive values. These compounds show high catalytic activity regarding the oxidation of 3,5-di-tert-butylcatechol to 3,5-di-tert-butylquinone exhibiting saturation kinetics at high substrate concentrations. The turnover numbers k(cat) = (86 +/- 7) h(-1) (1), k(cat) = (101 +/- 4) h(-1) (2), k(cat) = (230 +/- 4) h(-1) (3), and k(cat) = (130 +/- 4) h(-1) (4) were determined from the double reciprocal Lineweaver-Burk plot. Compounds 5 and 6 can be regarded as structural and electronic Mn analogues for substituted forms of Fe-containing intradiol-cleaving catechol dioxygenases. To our knowledge 5 is the first mononuclear Mn(II) compound featuring an N(3)OCl(2) donor set.

Catalysis↗
PubMed2003

Models for the lower S states of photosystem II: a trinuclear mixed-valent MnII/MnIV/MnII complex.

The trinuclear complex Mn(3)(pko)(4)(CH(3)O)(2)(SCN)(2).CH(3)OH, 1, where Hpko is 2,2'-dipyridylketonoxime, is a rare example of a complex simultaneously containing Mn(II) and Mn(IV). X-ray crystallography and XANES spectroscopy clearly distinguish the Mn(II)(2)Mn(IV) valence isomer from the more commonly observed Mn(III)(2)Mn(II) formulation. Fits to variable-temperature magnetic susceptibility data indicate that the Mn(II) and Mn(IV) are ferromagnetically coupled (J = +6.13 cm(-1)) and that 1 has an S = (13)/(2) ground state.

Crystallography, X-Ray↗
PubMed2003

Isolation of the first ferromagnetically coupled Mn(III/IV) complex.

Binuclear manganese complexes Mn2(III/IV)(dtsalpn)2DCBI, 1, Mn2(III/III)(dtsalpn)2HDCBI, 2, containing the ligand dicarboxyimidazole (DCBI) have been prepared in order to address the issue of imidazole bridged and ferromagnetically coupled Mn sites in high oxidation states of the OEC in Photosystem II (PS II). Temperature dependent magnetic susceptibility studies of 1 indicates that the interaction between the two Mn(III)/Mn(IV) ions is ferromagnetic (J = +1.4 cm(-1)). Variable temperature EPR spectra of 1 shows that a g = 2 multiline is as an excited state signal corresponding to S = 1/2.

Binding Sites↗
PubMed2003

Solution chemistry of copper(II)-gentamicin complexes: relevance to metal-related aminoglycoside toxicity.

The adverse effect to the inner ear of aminoglycosides, drugs widely administered for the treatment of serious infections, appears to result from the interaction of these drugs with Cu(II) or Fe(II)/Fe(III) ions. To understand more completely the metal-induced side effects of one such antibiotic, gentamicin, we studied copper(II) coordination to gentamicin C1a by potentiometry, UV-vis, CD, and EPR spectroscopies, and ESI mass spectrometry. Only monomeric complexes of the CuH(n)L stoichiometry, with n ranging from 3 to -2, were detected over the pH range of 4-12. CuH(3)L and CuH(2)L complexes exhibit the same coordination mode, binding copper(II) through the amino nitrogen atom and a deprotonated alcoholic oxygen atom of the garosamine ring. In the CuHL and CuL complexes a second amino nitrogen atom of the purpurosamine ring participates in central ion coordination. Finally, the additional axial binding of the deprotonated oxygen of the hydroxyl group of the 2-deoxystreptamine moiety occurs in the CuH(-)(1)L and CuH(-)(2)L complexes. Interactions of the Cu(II)-gentamicin-H(2)O(2) system at pH 7.4 with N,N-dimethyl-p-nitrosoaniline, arachidonic acid, and plasmid DNA confirmed that gentamicin complexes facilitate oxidative reactions leading to peroxidation of arachidonic acid and scission of double-stranded DNA mediated by copper-bound reactive oxygen species. However, the stability constants of Cu(II)-gentamicin complexes are inferior to the binding constants of copper(II) complexes with other components of human serum or cells. Computer simulations of copper(II) distribution in the human blood plasma showed that the concentration of gentamicin would have to be at impossible levels (100 M) before a significant fraction of Cu(II) ions would be bound to gentamicin. Further, once introduced into aqueous solution, histidine replaces gentamicin in Cu(II)-gentamicin complexes. Therefore, Cu(II)-gentamicin complexes might not exist under physiological conditions.

Anti-Bacterial Agents↗
PubMed2003

Hg(II) binding to a weakly associated coiled coil nucleates an encoded metalloprotein fold: a kinetic analysis.

A detailed kinetic analysis of metal encapsulation by a de novo-designed protein is described. The kinetic mechanism of Hg(II) encapsulation in the three-stranded coiled coil formed by the peptide CH(3)CO-G LKALEEK CKALEEK LKALEEK G-NH(2) (Baby L9C) is derived by global analysis. The mechanism involves rapid initial collapse of two peptides by Hg(II) forming Hg(Baby L9C(-H))(2) with a linear thiolato Hg(II) bound to the cysteine sulfur atoms. Here, Baby L9C(-H) denotes Baby L9C with the cysteine thiol deprotonated. Addition of the third peptide, forming the three-stranded coiled coil, is the rate-determining step and results in an intermediate state involving two separate species. One of the species, termed the properly folded intermediate, undergoes rapid deprotonation of the third cysteine thiol, yielding the desired three-stranded coiled coil with an encapsulated trigonal thiolato Hg(II). The other species, termed the misfolded intermediate, rearranges in an experimentally distinguishable step to the properly folded intermediate. The order of the reaction involving the addition of the third peptide with respect to the concentration of Baby L9C indicates that addition of the third helix only occurs through reaction of Hg(Baby L9C(-H))(2) and Baby L9C that is unassociated with a coiled coil. Temperature dependence of the reaction afforded activation parameters for both the addition of the third helix (deltaH = 20(2) kcalmol; deltaS= 40(5) calmol K) and the rearrangement of the misfolded intermediate steps (deltaH = 23(2) kcalmol; deltaS= 27(5) calmol K). The mechanism is discussed with regard to metalloprotein folding and metalloprotein design.

Amino Acid Sequence↗
PubMed2002

Oxidation of organic sulfides by vanadium haloperoxidase model complexes.

In addition to halide oxidation, the vanadium haloperoxidases are capable of oxidizing sulfides to sulfoxides. Four vanadium complexes with tripodal amine ligands, K[VO(O(2))(heida)] (1), VO(2)(bpg) (2), K[VO(2)(ada)] (3), and K(2)[VO(O(2))(nta)] (4), previously shown to perform bromide oxidation (Colpas, G. J.; Hamstra, B. J.; Kampf, J. W.; Pecoraro, V. L. J. Am. Chem. Soc. 1996, 118, 3469-3477), have now been shown to oxidize aryl alkyl sulfides to the corresponding sulfoxides. The oxidation was observed by the disappearance of thioanisole's ultraviolet absorption at 290 nm, by the change in the aromatic region of the (1)H NMR spectrum of the sulfides, and by changes in the complexes' (51)V NMR spectra. The amount of methyl phenyl sulfide oxidized in 3 h was 1000 equiv (per metal complex). The oxidation product is almost exclusively sulfoxide, with very little sulfone (less than 3% over a 3 h experiment) formed. This is consistent with an electrophilic oxidation mechanism, as had been proposed for oxidation of bromide by 1-4. The rate was found to be first order in substrate concentration, similar to the rate law observed for bromide oxidation. Unlike the bromide oxidation, the equivalent of acid required for peroxovanadium complex activation is not consumed. The complexes 1-4 are not reactive with styrene or cyclooctene. The relevance of these reactions to the mechanism of the vanadium haloperoxidases and, more generally, peroxovanadium oxygenation of sulfides will be discussed.

Algorithms↗
PubMed2002

Evaluating hydrogen bond interactions in enzymes containing Mn(III)-histidine complexation using manganese-imidazole complexes.

It is often difficult to control hydrogen bond interactions in small molecule compounds that model metalloenzyme active sites. The imidazole-containing ligands 4,5-dicarboxyimidazole (H(3)DCBI) and 4,5-dicarboxy- N-methylimidazole (H(2)MeDCBI) allow examination of the effects of internal hydrogen bonding between carboxylate and imidazole nitrogen atoms. A new series of mononuclear manganese imidazole complexes have been prepared using these ligands: Mn(III)(salpn)(H(2)DCBI)(DMF) (1), Mn(III)(salpn)(HMeDCBI) (2), Mn(III)(dtsalpn)(HMeDCBI) (3), [Mn(IV)(dtsalpn)(HMeDCBI)]PF(6) (4), Mn(III)(salpn)(H(2)DCBI) (5), Mn(III)(dtsalpn)(H(2)DCBI) (6), and Mn(IV)(dtsalpn)(H(2)DCBI)PF(6) (8). Complexes 1, 2, 3, 5, and 6 have been prepared by direct reaction of salpn [salpn=(salicylideneaminato)-1,3-diaminopropane)] or dtsalpn [dtsalpn=(3,5-di- t-butylsalicylideneaminato)-1,3-diaminopropane)] and H(3)DCBI and H(2)MeDCBI with Mn(III) acetate, while complexes 4 and 8 were made by bulk electrolysis of complex 3 or 6 in dichloromethane. Complexes 1, 2, and 6 were characterized by X-ray diffraction. The impact of hydrogen bonding interactions of the complexes has been demonstrated by X-ray diffraction, cyclic voltammetry, and EPR spectroscopy. In all complexes the central metal ion is present in a six-coordinate geometry. Magnetic susceptibility measurements confirm the spin and oxidation states of the complexes. The cyclic voltammograms of 3 and 6 in dichloromethane reveal single, reversible redox waves with E(1/2)=600 mV and 690 mV, respectively. The X-band EPR spectrum of 4 shows a broad signal around g=4.4, and the corresponding complex 8 possesses a broad signal at slightly lower field ( g=5.5) than 4. These studies demonstrate that even small changes in the effective charge of the imidazole ligand can have a profound impact on the structure, spectroscopy, and magnetism of manganese(IV) complexes. We use these observations to present a model that may explain the origin of the g=4.1 signal in the S(2) state of photosystem II.

Electrochemistry↗
PubMed2002

Preparation of highly efficient manganese catalase mimics.

The series of compounds [Mn(bpia)(mu-OAc)](2)(ClO(4))(2) (1), [Mn(2)(bpia)(2)(muO)(mu-OAc)](ClO(4))(3).CH(3)CN (2), [Mn(bpia)(mu-O)](2)(ClO(4))(2)(PF(6)).2CH(3)CN (3), [Mn(bpia)(Cl)(2)](ClO)(4) (4), and [(Mn(bpia)(Cl))(2)(mu-O)](ClO(4))(2).2CH(3)CN (5) (bpia = bis(picolyl)(N-methylimidazol-2-yl)amine) represents a structural, spectroscopic, and functional model system for manganese catalases. Compounds 3 and 5 have been synthesized from 2 via bulk electrolysis and ligand exchange, respectively. All complexes have been structurally characterized by X-ray crystallography and by UV-vis and EPR spectroscopies. The different bridging ligands including the rare mono-mu-oxo and mono-mu-oxo-mono-mu-carboxylato motifs lead to a variation of the Mn-Mn separation across the four binuclear compounds of 1.50 A (Mn(2)(II,II) = 4.128 A, Mn(2)(III,III) = 3.5326 and 3.2533 A, Mn(2)(III,IV) = 2.624 A). Complexes 1, 2, and 3 are mimics for the Mn(2)(II,II), the Mn(2)(III,III), and the Mn(2)(III,IV) oxidation states of the native enzyme. UV-vis spectra of these compounds show similarities to those of the corresponding oxidation states of manganese catalase from Thermus thermophilus and Lactobacillus plantarum. Compound 2 exhibits a rare example of a Jahn-Teller compression. While complexes 1 and 3 are efficient catalysts for the disproportionation of hydrogen peroxide and contain an N(4)O(2) donor set, 4 and 5 show no catalase activity. These complexes have an N(4)Cl(2) and N(4)OCl donor set, respectively, and serve as mimics for halide inhibited manganese catalases. Cyclovoltammetric data show that the substitution of oxygen donor atoms with chloride causes a shift of redox potentials to more positive values. To our knowledge, complex 1 is the most efficient binuclear functional manganese catalase mimic exhibiting saturation kinetics to date.

Algorithms↗
PubMed2002

Comparison of the binding of cadmium(II), mercury(II), and arsenic(III) to the de novo designed peptides TRI L12C and TRI L16C.

Designed alpha-helical peptides of the TRI family with a general sequence Ac-G(LKALEEK)(4)G-CONH(2) were used as model systems for the study of metal-protein interactions. Variants containing cysteine residues in positions 12 (TRI L12C) and 16 (TRI L16C) were used for the metal binding studies. Cd(II) binding was investigated, and the results were compared with previous and current work on Hg(II) and As(III) binding. The metal peptide assemblies were studied with the use of UV, CD, EXAFS, (113)Cd NMR, and (111m)Cd perturbed angular correlation spectroscopy. The metalated peptide aggregates exhibited pH-dependent behavior. At high pH values, Cd(II) was bound to the three sulfurs of the three-stranded alpha-helical coiled coils. A mixture of two species was observed, including Cd(II) in a trigonal planar geometry. The complexes have UV bands at 231 nm (20 600 M(-1) cm(-1)) for TRI L12C and 232 nm (22 600 M(-1) cm(-1)) for TRI L16C, an average Cd-S bond length of 2.49 A for both cases, and a (113)Cd NMR chemical shift at 619 ppm (Cd(II)(TRI L12C)(3)(-)) or 625 ppm (Cd(II)(TRI-L16C)(3)(-)). Nuclear quadrupole interactions show that two different Cd species are present for both peptides. One species with omega(0) = 0.45 rad/ns and low eta is attributed to a trigonal planar Cd-(Cys)(3) site. The other, with a smaller omega(0), is attributed to a four-coordinate Cd(Cys)(3)(H(2)O) species. At low pH, no metal binding was observed. Hg(II) binding to TRI L12C was also found to be pH dependent, and a 3:1 sulfur-to-mercury(II) species was observed at pH 9.4. These metal peptide complexes provide insight into heavy metal binding and metalloregulatory proteins such as MerR or CadC.

Amino Acid Sequence↗