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Purpose: To characterize the time structure of K1 kickboxing matches of Glory World Series (Glory) and to determine potential differences between winners and losers., Methods: Seventeen matches of Glory 2019 (17 first rounds, 13 second rounds, and 8 third rounds) were video-analyzed to quantify (1) the time expended in high- and low-intensity activity and pauses, (2) the number and pattern of attacks, and (3) the number of effective attacks. Fighters were professional male athletes (age 27.9 [2.7] y) of the middle-weight category (85 kg). The number and the pattern of attacks and the number of effective attacks were compared between winners and losers., Results: The mean times expended in high- and low-intensity activity and pauses were 234.6 (133.9) seconds, 97.4 (60.1) seconds, and 36.0 (19.9) seconds, respectively, resulting in an effort-to-pause ratio of ∼1.8:1. Compared with losers, winners presented (1) a greater number of attacks in the second round (P = .004) and entire match (P = .009), (2) a greater number of attacks containing 3 attacks in sequence in the second round (P = .001) and attacks containing >3 attacks in the third round (P = .049), and (3) a greater number of effective attacks in the second round (P = .011) and entire match (P = .008)., Conclusions: The findings of the present study indicate that K1 kickboxing in Glory matches presents a ∼1.8:1 effort-to-pause ratio and that winners perform more attacks, effective attacks, and attacks in sequence. These data provide useful insights to improve the training specificity of kickboxing athletes.

Introduction: Introduction: recently there have been several new versions of equipment based on the principles of bioelectrical impedance (BIA). Therefore, it is important to know the agreement between data produced by different commercially available equipment. Objective: to verify the agreement between fat-free mass (FFM), fat mass (FM), and body fat percentage (BF%) estimated using different segmental multi-frequency BIA (Tanita® MC-980U and InBody 770®) and whole-body spectral techniques (Xitron 4200). Methods: the sample consisted of 117 adults of both sexes, aged between 18 and 28 years. Methodological procedures followed specific guidelines for each equipment model. Agreement was analyzed by the t-test for paired data, concordance correlation coefficient (CCC), and Bland-Altman plot. Results: mean estimates of FFM, FM, and BF% produced by the Tanita® MC-980U and InBody 770® devices did not present statistical differences compared to the Xitron 4200® reference device. CCC values for FFM demonstrated magnitudes between 0.904 and 0.931, representing clinically acceptable strength of agreement, while for FM and BF% the strength of agreements was weak (< 0.90). Regarding the FFM, the bias showed underestimates of -0.98 kg to -1.69 kg, with limits of agreement between -7.32 kg and 3.94 kg. In the case of FM and BF%, overestimations were observed that reached values of 1.01 kg and 0.71%, with limits of agreement of -1.91 kg to 3.93 kg and -3.86% to 5.28%, respectively. Conclusion: FFM, FM, and BF% estimated by the Tanita® MC-980U and InBody 770® devices were not individually comparable with estimates produced by the Xitron 4200® reference device; therefore, its replacement for diagnostic purposes and inter- or intra-subject comparisons is not recommended.

The first three-dimensional structure of phenylalanine ammonia lyase (PAL) has been determined at 2.1 A resolution for PAL from Rhodosporidium toruloides. The enzyme is structurally similar to the mechanistically related histidine ammonia lyase (HAL), with PAL having an additional approximately 160 residues extending from the common fold. We propose that catalysis (including lowering the pK(a) of nonacidic C3 of l-phenylalanine for an E1cb mechanism) is potentially governed by dipole moments of seven alpha helices associated with the PAL active site (six positive poles and one negative pole). Cofactor 3,5-dihydro-5-methylidene-4H-imidazol-4-one (MIO) resides atop the positive poles of three helices, for increasing its electrophilicity. The helix dipoles appear fully compatible with a model of phenylalanine docked in the active site of PAL having the first covalent bond formed between the amino group of substrate and the methylidene group of MIO: 12 highly conserved residues (near the N termini of helices for enhancing function) are poised to serve roles in substrate recognition, MIO activation, product separation, proton donation, or polarizing electrons from the phenyl ring of substrate for activation of C3; and a highly conserved His residue (near the C terminus of the one helix that directs its negative pole toward the active site to increase the residue's basicity) is positioned to act as a general base, abstracting the pro-S hydrogen from C3 of substrate. A similar mechanism is proposed for HAL, which has a similar disposition of seven alpha helices and similar active-site residues. The helix dipoles appear incompatible with a proposed mechanism that invokes a carbocation intermediate.

Background: Riboflavin synthase catalyzes the dismutation of two molecules of 6,7-dimethyl-8-(1'-D-ribityl)-lumazine to yield riboflavin and 4-ribitylamino-5-amino-2,6-dihydroxypyrimidine. The homotrimer of 23 kDa subunits has no cofactor requirements for catalysis. The enzyme is nonexistent in humans and is an attractive target for antimicrobial agents of organisms whose pathogenicity depends on their ability to biosynthesize riboflavin., Results: The first three-dimensional structure of the enzyme was determined at 2.0 A resolution using the multiwavelength anomalous diffraction (MAD) method on the Escherichia coli protein containing selenomethionine residues. The homotrimer consists of an asymmetric assembly of monomers, each of which comprises two similar beta barrels and a C-terminal alpha helix. The similar beta barrels within the monomer confirm a prediction of pseudo two-fold symmetry that is inferred from the sequence similarity between the two halves of the protein. The beta barrels closely resemble folds found in phthalate dioxygenase reductase and other flavoproteins., Conclusions: The three active sites of the trimer are proposed to lie between pairs of monomers in which residues conserved among species reside, including two Asp-His-Ser triads and dyads of Cys-Ser and His-Thr. The proposed active sites are located where FMN (an analog of riboflavin) is modeled from an overlay of the beta barrels of phthalate dioxygenase reductase and riboflavin synthase. In the trimer, one active site is formed, and the other two active sites are wide open and exposed to solvent. The nature of the trimer configuration suggests that only one active site can be formed and be catalytically competent at a time.

The reaction of Fe(II)(C5Me5)(C5H5), FeCpCp, with percyano acceptors, A [A = C4(CN)6 (hexacyanobutadiene), TCNQF4 (perfluoro-7,7,8,8-tetracyano-p-quinodimethane), and DDQ (2,3-dichloro-5,6-dicyanobenzoquinone)], results in formation of 1:1 charge-transfer salts of [Fe(III)CpCp]*]*+[A]*- composition. With A = TCNQ (7,7,8,8-tetracyano-p-quinodimethane) a 1:2 electron-transfer salt with FeCpCp forms. With A = TCNE (tetracyanoethylene) a pair of 1:1 salts as well as a pair of 2:3 salts of [FeCpCp]2[TCNE]3.S (S = CH2Cl2, THF) have been isolated and characterized by single-crystal X-ray diffraction. [FeCpCp][TCNE] consists of parallel 1-D.D(*+)A(*-)D(*+)A(*-)D(*+)A(*-). chains, while [FeCpCp][TCNE].MeCN has a herringbone array of D(*+)A2(2-)D(*+) dimers separated by solvent molecules. Although each [TCNE](-) is disordered, the diamagnetic [TCNE]2(2-) dimer is structurally different from those observed earlier with an intradimer separation of 2.79 A. The [TCNE](-) in the 2:3 [FeCpCp]2[TCNE]3.S exists as an eclipsed diamagnetic [TCNE]2(2-) dimer with an intradimer ethylene C.C separation of 2.833 and 2.903 A for the CH2Cl2- and THF-containing materials, respectively. The bond distances and angles for all the cations are essentially equivalent, and the distances are essentially equivalent to those previously reported for [FeCp2](*+) and [FeCp2](*+) cations. The average Fe-C5H5-ring and Fe-C5Me5-ring centroid distances are 1.71 and 1.69 A, respectively, which are 0.05 A longer than reported for Fe(II)CpCp. The one-electron reduction potential for Fe(II)CpCp is 0.11 V (vs SCE). The 5 K EPR of [FeCpCp](*+)[BF4](-) exhibits an axially symmetric powder pattern with g(parallel) = 4.36 and g(perpendicular) = 1.24, and the EPR parameters are essentially identical to those reported for ferrocenium and decamethylferrocenium. The high-temperature magnetic susceptibility for polycrystalline samples of these complexes can be fit by the Curie-Weiss law, chi = C/(T - theta), with low theta values and mu(eff) values from 2.08 to 3.43 mu(B), suggesting that the polycrystalline samples measured had varying degrees of orientation. [FeCpCp][TCNE] exhibits the highest effective moment of 3.43 mu(B)/Fe and weak ferromagnetic coupling, as evidenced from the theta of 3.3 K; however, unexpectedly, it does not magnetically order above 2 K. The formation of the four phases comprising FeCpCp and TCNE emphasizes the diversity of materials that may form and the present inability to predict neither solid-state compositions nor structure types.

Background: 3,4-Dihydroxy-2-butanone-4-phosphate synthase catalyzes a commitment step in the biosynthesis of riboflavin. On the enzyme, ribulose 5-phosphate is converted to 3,4-dihydroxy-2-butanone 4-phosphate and formate in steps involving enolization, ketonization, dehydration, skeleton rearrangement, and formate elimination. The enzyme is absent in humans and an attractive target for the discovery of antimicrobials for pathogens incapable of acquiring sufficient riboflavin from their hosts. The homodimer of 23 kDa subunits requires Mg(2+) for activity., Results: The first three-dimensional structure of the enzyme was determined at 1.4 A resolution using the multiwavelength anomalous diffraction (MAD) method on Escherichia coli protein crystals containing gold. The protein consists of an alpha + beta fold having a complex linkage of beta strands. Intersubunit contacts are mediated by numerous hydrophobic interactions and three hydrogen bond networks., Conclusions: A proposed active site was identified on the basis of amino acid residues that are conserved among the enzyme from 19 species. There are two well-separated active sites per dimer, each of which comprise residues from both subunits. In addition to three arginines and two threonines, which may be used for recognizing the phosphate group of the substrate, the active site consists of three glutamates, two aspartates, two histidines, and a cysteine which may provide the means for general acid and base catalysis and for coordinating the Mg(2+) cofactor within the active site.

Enantioselectivity of Rh(I)-catalyzed asymmetric hydrogenation of dehydroamino acid derivatives and dimethyl itaconate can be enhanced by the appropriate choice of substituents on the aromatic rings of vicinal diarylphosphinites derived from carbohydrates as well as trans-cyclohexane-1,2-diol. For example, the use of phosphinites with electron-donating bis(3,5-dimethylphenyl) groups at phosphorus provide high ee's in these reactions whereas electron-withdrawing aryl substituents decrease the enantioselectivity. In this paper, an attempt is made to clarify the origin of these remarkable electronic effects at two levels. First, crystal structures of a number of precatalysts ([phosphinite](2)Rh(+)[diolefin]X(-)) were determined and their structures were studied in detail to examine the electronic effects, if any, on the ground-state conformations of these molecules. A study of six of these complexes reveals that the gross conformational features of these precatalysts are largely unaffected by electronic effects, which suggests that other explanations have to be sought for the electronic amplification of enantioselectivity. One possibility is a change in the diastereomeric equilibrium between the initially formed [substrate]Rh(+)[phosphinite] complexes as a function of electronic effect of the ligand. In the Rh-catalyzed hydrogenation of dimethyl itaconate, we have examined this equilibrium between the major and minor complexes by (31)P NMR. There is a clear difference in the ratio of these two diastereomers when 3,5-dimethylphenylphosphinite vis-à-vis the unsubstituted diphenylphosphinite is used. Electron-deficient ligands such as 1,2-bis-3,5-diflurophenylphosphinite and 1,2-bis-3,5-bis-trifluromethylphenylphosphinite appear to form these diastereomers more readily at room temperature, even though the exact ratio of the diastereomers could not be established with any certainty.

Comparison of the high-resolution X-ray structures of the native HIV-1 protease and its complexes with the inhibitors suggested that the enzyme flaps are flexible. The movement at the tip of the flaps could be as large as 7 A. On the basis of this observation, cyclic cyanoguanidines have been designed, synthesized, and evaluated as HIV-1 protease (PR) inhibitors. Cyclic cyanoguanidines were found to be very potent inhibitors of HIV-1 protease. The choice of cyclic cyanoguanidines over cyclic guanidines was based on the reduced basicity of the former. X-ray structure studies of the HIV PR complex with cyclic cyanoguanidine demonstrated that in analogy to cyclic urea, cyclic cyanoguanidines also displace the unique structural water molecule. The structure-activity relationship of the cyclic cyanoguanidines is compared with that of the corresponding cyclic urea analogues. The differences in binding constants of the two series of compounds have been rationalized using high-resolution X-ray structure information.

The syntheses, characterizations, and X-ray crystallographic structure determinations are described for adducts of stable nucleophilic carbenes with pnictinidenes. The adducts between 1,3-dimesitylimidazol-2-ylidene and phenylphosphinidene, phenylarsinidene, (trifluoromethyl)phosphinidene, and (pentafluorophenyl)arsinidene are reported. These carbene-pnictinidene adducts are formed by the direct reaction of a stable nucleophilic carbene with the corresponding pnictinidene cyclic oligomers. The synthesis and structure of the adduct between 1,3-dimesitylimidazolin-2-ylidene and phenylphosphinidene from the reaction of 1,3-dimesitylimidazolin-2-ylidene with phenylphosphorus dichloride are also reported. These carbene-pnictinidene adducts possess strongly polarized pnictinidene-carbene bonds. The C-Pn-C angles are all typically small at 97-102 degrees, and there is only a 4% shortening of the nominal Pn=C double bond compared to the Pn-C single bond to the second substituent on the pnictogen. The (31)P NMR shifts of the phosphorus adducts suggest strongly shielded phosphorus centers in accord with the polarized structures.

(meso-Tetrakis(3,5-di-tert-butyl-4-hydroxyphenyl)porphinato)manganese(III) tetracyanoethenide, [MnTP'P][TCNE], has been structurally and magnetically characterized. [MnTP'P][TCNE] (C(96)H(108)MnN(8)O(4)) belongs to the triclinicP&onemacr; (No. 2) space group with a = 8.597(2) Å, b = 14.756(4) Å, c = 17.573(5) Å, alpha = 101.16 (2) degrees, beta = 100.56(2) degrees, gamma = 96.37(2) degrees, and Z = 1. Due to the oxidative instability of the phenoxy groups, [Mn(III)TP'P][TCNE] was prepared from the reaction of [Mn(III)TP'P]OAc with the strong acid H(2)TCNE (pK(a) = 3.6) in the presence of TCNE to form acetic acid and the product. [MnTP'P][TCNE] is a coordination polymer with the Mn(III) sites bridged by trans-&mgr;(2)-bound [TCNE](*)(-) with relatively short (8.587 Å) intrachain and long (>/=14.756 Å) interchain Mn.Mn separations. The magnetic data above 210 K obey the Curie-Weiss expression with an effective &THETAV; value of 90.0 K, the largest yet reported for a soluble molecule-based magnet. In addition to a 15 K T(c) hysteretic behavior with a coercive field of 100 Oe is observed at 5 K. Despite the significant steric bulk leading to the substantially decreased interchain interactions that are crucial for magnetic ordering, the T(c) is unexpectedly high and suggests that other linear chain systems may be expected to exhibit magnetic ordering at higher temperatures.

A novel series of cognition enhancers was designed based on molecular modeling and X-ray structure analysis of EXP-9121 (2). This new series features a spirocyclic ring system that constrains the side chain substituents into the orientation seen in the X-ray crystal structure of 2. MM2 calculations preformed on 2 accurately predicted the solid state conformation. Compounds could be rapidly assembled using a bis-Michael addition reaction. Unfortunately, in vitro testing showed moderate activity at best, suggesting the X-ray structure of 2 does not mimic the bioactive conformation.

Recrystallization of the solid Cd(10)S(4)(SC(6)H(5))(12) from a solution of pyridine and N, N-di-methylformamide (DMF) results in the formation of the cluster Cd(32)S(14)(SC(6)H(5))(36)-DMF(4) as pale yellow cubes. The structure consists of an 82-atom CdS core that is a roughly spherical piece of the cubic sphalerite lattice approximately 12 angstroms in diameter. The four corners of the lattice are capped by hexagonal wurtzite-like CdS units, which results in an overall tetrahedral cluster approximately 15 angstroms in diameter. This cluster dissolves intact in tetrahydrofuran where its absorption spectrum reveals a sharp peak at 358 nanometers at room temperature and its emission spectra show a strong broad band at 500 nanometers.

C(60) and liquid bromine react to form C(60)Br(24), a crystalline compound isolated as a bromine solvate, C(60)Br(24)(Br(2))(x), The x-ray crystal structure defines a new pattern of addition to the carbon skeleton that imparts a rare high symmetry. The parent C(60) framework is recognizable in C(60)Br(24), but sp(3) carbons at sites of bromination distort the surface, affecting conformations of all of the hexagonal and pentagonal rings. Twenty-four bromine atoms envelop the carbon core, shielding the 18 remaining double bonds from addition. At 150 degrees to 200 degrees C there is effectively quantitative reversion of C(60)Br(24) to C(60) and Br(2).

A new class of potent antihypertensives has been discovered that exert their effect through blockade of the angiotensin II (AII) receptor. Most AII antagonists reported so far are peptide mimics of the endogenous vasoconstrictor octapeptide angiotensin II. The compounds of this paper are nonpeptides and therefore constitute a new class of potent AII receptor antagonists. Based on the overlap of a conformation of AII with literature lead 3, a hypothesis was developed suggesting the need for an additional acidic functionality to increase the lead's potency. The substitution of an additional carboxylic acid resulted in a 10-fold increase in binding affinity observed for diacid 4. The binding affinities for subsequent compounds were eventually increased 1000-fold over that of the literature leads through a systematic SAR study. Thus the AII receptor binding affinity [IC50 (microM)] of 15 microM for literature lead 1, for example, was increased to 0.018 and 0.012 microM for compounds 33 and 53. A structure-affinity relationship has been found requiring the presence of four key elements for good activity: (1) an additional phenyl ring at the N-benzyl para position of the benzylimidazole nucleus, (2) an acidic functionality at the ortho position of the terminal aromatic ring, (3) a lipophilic side chain at the imidazole 2-position of three to five carbon atoms in length, and (4) a group at the imidazole 5-position capable of hydrogen bonding. The synthesis as well as the pharmacological activity of the compounds in this new series of AII receptor antagonists are presented.

A new superconductor that displays onset behavior near 120 K has been identified as Bi(2)Sr(3-x)Ca(x)Cu(2)O(8+y), with x ranging from about 0.4 to 0.9. Single crystal x-ray diffraction data were used to determine a pseudo-tetragonal structure based on an A-centered orthorhombic subcell with a = 5.399 A, b= 5.414A, and c = 30.904 A. The structure contains copper-oxygen sheets as in La(2)CuO(4) and YBa(2)Cu(3)O(7), but the copper-oxygen chains present in YBa(2)Cu(3)O(7) do not occur in Bi(2)Sr(3-x)Ca(x)Cu(2)O(8+y). The structure is made up of alternating double copper-oxygen sheets and double bismuth-oxygen sheets. There are Ca(2+) and Sr(2+) cations between the adjacent Cu-O sheets; Sr(2+) cations are also found between the Cu-O and Bi-O sheets. Electron microscopy studies show an incommensurate superstructure along the a axis that can be approximated by an increase of a factor of 5 over the subcell dimension. This superstructure is also observed by x-ray diffraction on single crystals, but twinning can make it appear that the superstructure is along both a and b axes. Flux exclusion begins in our samples at about 116 K and is very strong by 95 K. Electrical measurements on a single crystal of Bi(2)Sr(3-x)Ca(x)Cu(2)O(8+y) show a resistivity drop at about 116 K and apparent zero resistivity at 91 K.

New high-temperature superconductors based on oxides of thallium and copper, but not containing barium, have been prepared. A transition temperature (T(c)) of about 85 K is found for (Tl(0.5)Pb(0.5)) Sr(2)CaCu(2)O(7) whereas (Tl(0.5)Pb(0.5))Sr(2)Ca(2)Cu(3)O(9) has a T(c) of about 120 K. Both materials possess tetragonal symmetry with a = 3.80 A, c = 12.05 A for (Tl(0.5)Pb(0.5))Sr(2)CaCu(2)O(7), and a = 3.81 A, c = 15.23 A for (Tl(0.5)Pb(0.5))Sr(2)Ca(2)Cu(3)O(9). A structure refinement of the latter phase has been carried out with single-crystal x-ray diffraction data.

There is now a new series of high-temperature superconductors that may be represented as (A(III)O)(2)A(2)(II)Can-1CunO2+2n where A(III) is Bi or Tl, A(II) is Ba or Sr, and n is the number of Cu-O sheets stacked consecutively. There is a general trend toward higher transition temperatures as n increases. The highest n value for a bulk phase is three and is found when A(III) is Tl. This compound, Tl(2)Ba(2)Ca(2)Cu(3)O(10), has the highest transition temperature( approximately 125 K) of any presently known bulk superconductor. The structure of Tl(2)Ba(2)Ca(2)Cu(3)O(10) has been determined from single-crystal x-ray diffraction data and is tetragonal, with a = 3.85 A and c = 35.9 A. No superstructure is observed, and the material is essentially twin-free. Electron microscopy in the Tl/Ba/Ca/Cu/O system has revealed intergrowths where n = 5; such regions may well be responsible for the superconducting onset behavior observed in this system at about 140 K.

The structures of hexaazaoctadecahydrocoronene, [HAOC](n) (n = O, + 2), have been determined by single-crystal x-ray diffraction. Although HAOC is aromatic, its dication has a localized structure that is based upon Jahn-Teller-distorted cyanine/p-phenylenediammonium fragments. The structure is consistent with the singlet ground state as determined by magnetic susceptibility and contrasts with the simplest Hückel expectation of a triplet ground state.

Two new ligand systems for complexation with 99mTc were prepared. The two analogs of bisaminoethanethiol (BAT): N,N'-bis(2-methyl-2-mercaptopropyl)-2,2-dimethylpropylenediamin e (PAT-HM) and N,N'-bis[2-(2-ethyl-1-mercaptopropyl)] ethylenediamine (TMR), form neutral and lipid soluble complexes with 99mTc that readily penetrate the blood-brain barrier following i.v. injection into rats. Although the 99mTc chelates do not display the prolonged brain retention required for use in single photon emission computed tomographic imaging studies, the fact that each ligand forms a neutral and lipid-soluble complex of high chemical stability when coordinated with 99mTc warrants further investigation to increase the site- and organ-specificity of these agents.

In developing new brain perfusion imaging agents, we prepared 99mTc complexes of racemic mixtures of bis(aminoethanethiol) (BAT) derivatives containing an N'-benzylpiperazinyl (BPA) side chain. Due to the presence of a chiral center, a mixture of diastereomers (syn and anti) following chelation with the 99mTc (no-carrier-added) was obtained. The neutral and lipid-soluble 99mTc-BPA-BAT (99mTc, T1/2 = 6 h) isomers were separated. The syn and anti isomers of carrier-added 99Tc-BPA-BAT (99Tc, T1/2 = 2 x 10(5) years) were also synthesized, separated, and crystallized. The X-ray crystallography of 99Tc-BPA-BAT showed the syn and anti conformations (in relationship with the central TC(=O)N2S2 core). Despite a similarity in the partition coefficients for the two isomers, the syn isomer showed a higher in vivo brain uptake and longer brain retention in rats (2.77 and 1.08% dose/organ at 2 and 15 min) than that of the corresponding anti isomer (0.57 and 0.27% dose/organ at 2 and 15 min). This information is important and should be taken into consideration when new 99mTc-labeled brain perfusion imaging agents are being designed.