Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0162473 (Frey)
 2,599 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Three groups that absorb in the 2100-1800-cm-1 infrared spectral region have recently been detected in Ni-hydrogenase from Chromatium vinosum [Bagley, K.A., Duin, E.C., Roseboom, W., Albracht, S. P.J. & Woodruff, W.H. (1995) Biochemistry 34, 5527-5535]. To assess the significance and generality of this observation, we have carried out an infrared-spectroscopic study of eight hydrogenases of three different types (nickel, iron and metal-free) and of 11 other iron-sulfur and/or nickel proteins. Infrared bands in the 2100-1800-cm-1 spectral region were found in spectra of all Ni-hydrogenases and Fe-hydrogenases and were absent from spectra of any of the other proteins, including a metal-free hydrogenase. The positions of these bands are dependent on the redox state of the hydrogenase. The three groups in Ni-hydrogenases that are detected by infrared spectroscopy are assigned to the three unidentified small non-protein ligands that coordinate iron in the dinuclear Ni/Fe active site as observed in the X-ray structure of the enzyme from Desulfovibrio gigas [Volbeda, A., Charon, M.-H., Piras, C., Hatchikian, E.C., Frey, M. & Fontecilla-Camps, J.C. (1995) Nature 373, 580-587]. It is concluded that these groups occur exclusively in metal-containing H2-activating enzymes. It is proposed that the active sites of Ni-hydrogenases and of Fe-hydrogenases have a similar architecture, that is required for the activation of molecular hydrogen.
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PMID:Similarities in the architecture of the active sites of Ni-hydrogenases and Fe-hydrogenases detected by means of infrared spectroscopy. 864 6

The selenium-containing F420-nonreducing hydrogenase from Methanococcus voltae was prepared in the Nia(I) middle dotCO state. The effect of illumination on this light-sensitive species was studied. EPR studies were carried out with enzyme containing natural selenium or with enzyme enriched in 77Se. Samples were prepared with either CO or 13CO. In the Nia(I) middle dotCO state, the nuclear spins of both 77Se (I = 1/2) and 13C (I = 1/2) interacted with the nickel-based unpaired electron, suggesting that they are positioned on opposite sites of the nickel ion. In the light-induced signal, the interaction with 13CO was lost. The 77Se nuclear spin introduced an anisotropic hyperfine splitting in both the dark and light-induced EPR signals. The data on the active enzyme of M. voltae are difficult to reconcile with the crystal structure of the inactive hydrogenase of Desulfovibrio gigas (Volbeda, A., Charon, M. H., Piras, C., Hatchikian, E. C., Frey, M., and Fontecilla Camps, J. C. (1995) Nature 373, 580-587) and suggest a structural change in the active site upon activation of the enzyme.
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PMID:Interactions of 77Se and 13CO with nickel in the active site of active F420-nonreducing hydrogenase from Methanococcus voltae. 879 8

The role of amino acid residues in the H(2)-activating subunit (HoxH) of the NAD-reducing hydrogenase (SH) from Alcaligenes eutrophus has been investigated by site-directed mutagenesis. Conserved residues in the N-terminal L1 (RGxE) and L2 (RxCGxCx(3)H) and the C-terminal L5 (DPCx(2)Cx(2)H/R) motifs of the active site-harboring subunit were chosen as targets. Crystal structure analysis of the [NiFe] hydrogenase from Desulfovibrio gigas uncovered two pairs of cysteines (motifs L2 and L5) as coordinating ligands of Ni and Fe. Glutamate (L1) and histidine residues (L2 and L5) were proposed as being involved in proton transfer [Volbeda, A., Charon, M.-H., Piras, C., Hatchikian, E. C., Frey, M., and Fontecilla Camps, J. C. (1995) Nature 373, 580-587]. The A. eutrophus mutant proteins fell into three classes. (i) Replacement of the putative four metal-binding cysteines with serine led to the loss of H(2) reactivity and blocked the assembly of the holoenzyme. Exchange of Cys62, Cys65, or Cys458 was accompanied by the failure of the HoxH subunit to incorporate nickel, supporting the essential function of these residues in the formation of the active site. Although the fourth mutant of this class (HoxH[C461S]) exhibited nickel binding, the modified protein was catalytically inactive and unable to oligomerize. (ii) Mutations in residues possibly involved in proton transfer (HoxH[E43V], HoxH[H69L], and HoxH[H464L]) yielded Ni-containing proteins with residual low levels of hydrogenase activity. (iii) The most promising mutant protein (HoxH[R40L]), which was identified as a metal-containing tetrametric enzyme, was completely devoid of H(2)-dependent oxidoreductase activity but exhibited a remarkably high level of D(2)-H(+) exchange activity. These characteristics are compatible with the interpretation of a functional proton transfer uncoupled from the flow of electrons.
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PMID:Amino acid replacements at the H2-activating site of the NAD-reducing hydrogenase from Alcaligenes eutrophus. 1057 8

Using an in vitro model, we investigated the chronological effects of orthodontic force on the response properties of periodontal mechanoreceptors (PMRs) in the rat mandibular first molar (M1). Experimental tooth movement was obtained by attaching a super-elastic titanium-nickel (Ti-Ni) alloy closed coil spring from the mandibular incisors to the right M1. On 1, 2, 3, 4, 7 and 14 days after the appliances were set, three right mandibular molars were extracted and direct stimulation with von Frey hairs was applied to the PMRs remaining in the tooth sockets of right M1. Single unit discharges were recorded from the inferior alveolar nerve. Following results were obtained; (1) in the 1-, 2- and 3-day groups, the mechanical thresholds were significantly lower than those in the control group. In the 4-day group, the mechanical threshold was significantly higher than that of the 3-day group. (2) In the 3-, 4-, 7- and 14-day groups, the conduction velocities of A(beta) units were lower than those in the control group. These results imply that orthodontic force applied to M1 induced functional changes in the PMRs within a few days, suggesting that the PMR seems to respond to orthodontic force at early stage of tooth movement.
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PMID:Changes in response properties of periodontal mechanoreceptors during tooth movement in rats. 1262 15

Using an in vitro preparation, we investigated chronological changes in response properties of periodontal mechanoreceptors (PMRs) in the rat right mandibular first molar (M1) after experimental orthodontic tooth movement. Orthodontic force was applied to M1 for 14 days by activating 24.5 mN superelastic titanium-nickel alloy closed coil springs anchored to the mandibular incisors. Experiments were performed on days 3, 7, 10, and 14 during application of orthodontic force and on days 7, 14, 21, and 28 after removal of orthodontic force. The rats without application of orthodontic force were used as control group. In each group, direct mechanical stimulation using von Frey hairs and electrical stimulation was applied to the distal root of M1. Results showed that compared with controls (1) the mechanical thresholds were significantly lower during application of orthodontic force; however, no significant difference was found after removal of force application and (2) conduction velocities were significantly lower from day 7 during application of orthodontic force to day 14 after removal of orthodontic force; however, no significant difference was found on days 21 and 28 after removal of orthodontic force. These results suggest that the PMRs, although having some of their response properties altered during orthodontic force application, were able to recover and adapt to the newly acquired intraoral condition after removal of the orthodontic force.
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PMID:Changes in response properties of periodontal mechanoreceptors after experimental orthodontic tooth movement in rats. 1503 96

Published assays for mechanical nociception in Drosophila have led to variable assessments of behavior. Here, we fabricated, for use with Drosophila larvae, customized metal nickel-titanium alloy (nitinol) filaments. These mechanical probes are similar to the von Frey filaments used in vertebrates to measure mechanical nociception. Here, we demonstrate how to make and calibrate these mechanical probes and how to generate a full behavioral dose-response from subthreshold (innocuous or non-noxious range) to suprathreshold (low to high noxious range) stimuli. To demonstrate the utility of the probes, we investigated tissue damage-induced hypersensitivity in Drosophila larvae. Mechanical allodynia (hypersensitivity to a normally innocuous mechanical stimulus) and hyperalgesia (exaggerated responsiveness to a noxious mechanical stimulus) have not yet been established in Drosophila larvae. Using mechanical probes that are normally innocuous or probes that typically elicit an aversive behavior, we found that Drosophila larvae develop mechanical hypersensitization (both allodynia and hyperalgesia) after tissue damage. Thus, the mechanical probes and assay that we illustrate here will likely be important tools to dissect the fundamental molecular/genetic mechanisms of mechanical hypersensitivity.
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PMID:An Improved Assay and Tools for Measuring Mechanical Nociception in Drosophila Larvae. 3319 34