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Journal articles on the topic 'CO geminate recombination'

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Author: Grafiati

Published: 10 March 2023

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1

STEVENSON, Thirza H., Aldo F. GUTIERREZ, Wendy K. ALDERTON, Lu-yun LIAN, and Nigel S. SCRUTTON. "Kinetics of CO binding to the haem domain of murine inducible nitric oxide synthase: differential effects of haem domain ligands." Biochemical Journal 358, no. 1 (August 8, 2001): 201–8. http://dx.doi.org/10.1042/bj3580201.

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The binding of CO to the murine inducible nitric oxide synthase (iNOS) oxygenase domain has been studied by laser flash photolysis. The effect of the (6R)-5,6,7,8-tetrahydro-l-biopterin (BH4) cofactor l-arginine and several Type I l-arginine analogues/ligands on the rates of CO rebinding has been evaluated. The presence of BH4 in the iNOS active site has little effect on the rebinding of protein-caged haem–CO pairs (geminate recombination), but decreases the bimolecular association rates 2-fold. Addition of l-arginine to the BH4-bound complex completely abolishes geminate recombination and results in a further 80-fold decrease in the overall rate of bimolecular association. Three of the Type I ligands, S-ethylisothiourea, l-canavanine and 2,5-lutidine, displaced the CO from the haem iron upon addition to the iNOS oxygenase domain. The Type I ligands significantly decreased the rate of bimolecular binding of CO to the haem iron after photolysis. Most of these ligands also completely abolished geminate recombination. These results are consistent with a relatively open distal pocket that allows CO to bind unhindered in the active site of murine iNOS in the absence of l-arginine or BH4. In the presence of BH4 and l-arginine, however, the enzyme adopts a more closed structure that can greatly reduce ligand access to the haem iron. These observations are discussed in terms of the known structure of iNOS haem domain and solution studies of ligand binding in iNOS and neuronal NOS isoenzymes.

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2

Ghosh, Arghya Pratim, Abdullah Al Mamun, and Pawel M. Kozlowski. "How does the mutation in the cap domain of methylcobalamin-dependent methionine synthase influence the photoactivation of the Co–C bond?" Physical Chemistry Chemical Physics 21, no. 37 (2019): 20628–40. http://dx.doi.org/10.1039/c9cp01849b.

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The topology of the S₁ PES is modulated by introducing a mutation at the F708 position. The mutation influences the photoactivation of the Co–C bond by decreasing the rate of geminate recombination and altering the rate of radical pair formation.

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3

Campbell, B. F., D. Magde, and V. S. Sharma. "Geminate recombination of CO in rabbit, opossum, and adult hemoglobins." Journal of Biological Chemistry 260, no. 5 (March 1985): 2752–56. http://dx.doi.org/10.1016/s0021-9258(18)89425-x.

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4

Tian, Wei Dong, Andrew V. Wells, Paul M. Champion, Carmelo Di Primo, Nancy Gerber, and Stephen G. Sligar. "Measurements of CO Geminate Recombination in Cytochromes P450 and P420." Journal of Biological Chemistry 270, no. 15 (April 14, 1995): 8673–79. http://dx.doi.org/10.1074/jbc.270.15.8673.

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5

Maréchal, Amandine, W. John Ingledew, and Peter R. Rich. "Time-resolved FTIR study of CO recombination with horseradish peroxidase." Biochemical Society Transactions 36, no. 6 (November 19, 2008): 1165–68. http://dx.doi.org/10.1042/bst0361165.

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Vibrational changes associated with CO recombination to ferrous horseradish peroxidase were investigated by rapid-scan FTIR (Fourier-transform IR) spectroscopy in the 1200–2200 cm−1 range. At pH 6.0, two conformers of bound CO are present that appear as negative bands at 1905 and 1934 cm−1 in photolysis spectra. Their recombination rate constants are identical, confirming that they arise from two substates of bound CO that are in rapid thermal equilibrium, rather than from heterogeneous protein sites. A smaller positive band at 2134 cm−1 also appears on photolysis and decays with the same rate constant, indicative of an intraprotein geminate site involved in recombination or, possibly, a weak-affinity surface CO-binding site. Other signals arising from protein and haem in the 1700–1200 cm−1 range can also be time-resolved with similar kinetics.

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6

Walda, Kevin N., X. Y. Liu, Vijay S. Sharma, and Douglas Magde. "Geminate Recombination of Diatomic Ligands CO, O2, and NO with Myoglobin." Biochemistry 33, no. 8 (March 1994): 2198–209. http://dx.doi.org/10.1021/bi00174a029.

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7

Leclerc-L'Hostis, Estelle, Stefan Franzen, Jean-Christophe Lambry, Jean-Louis Martin, Liliane Leclerc, Claude Poyart, and Michael C. Marden. "Picosecond geminate recombination of CO to the complexes calmodulin∗ heme-CO and calmodulin∗ heme-CO∗ melittin." Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology 1293, no. 1 (March 1996): 140–46. http://dx.doi.org/10.1016/0167-4838(95)00237-5.

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8

Benabbas, Abdelkrim, Venugopal Karunakaran, Hwan Youn, Thomas L. Poulos, and Paul M. Champion. "Effect of DNA Binding on Geminate CO Recombination Kinetics in CO-sensing Transcription Factor CooA." Journal of Biological Chemistry 287, no. 26 (April 28, 2012): 21729–40. http://dx.doi.org/10.1074/jbc.m112.345090.

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9

Harvey, Jeremy N. "DFT Computation of the Intrinsic Barrier to CO Geminate Recombination with Heme Compounds." Journal of the American Chemical Society 122, no. 49 (December 2000): 12401–2. http://dx.doi.org/10.1021/ja005543n.

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10

Agmon, Noam. "Reactive line-shape narrowing in low-temperature inhomogeneous geminate recombination of CO to myoglobin." Biochemistry 27, no. 9 (May 3, 1988): 3507–11. http://dx.doi.org/10.1021/bi00409a057.

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11

Grogan, Tammy G., Nilkamal Bag, Teddy G. Traylor, and Douglas Magde. "Picosecond Reaction of Picket Fence Heme with O2 and CO: Geminate Recombination in the Solvent Cage." Journal of Physical Chemistry 98, no. 51 (December 1994): 13791–96. http://dx.doi.org/10.1021/j100102a053.

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12

Su, Xiaojun, Rong Hu, Guanzhao Wen, Xianshao Zou, Mengyao Qing, Jun Peng, Xiaochuan He, and Wei Zhang. "Understanding of Photophysical Processes in DIO Additive-Treated PTB7:PC71BM Solar Cells." Crystals 11, no. 9 (September 18, 2021): 1139. http://dx.doi.org/10.3390/cryst11091139.

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1,8-diiodooctane (DIO) additive is an important method for optimizing the morphology and device performance of polythieno[3,4-b]-thiophene-co-benzodithiophene (PTB7)-based polymer solar cells. However, the effect of DIO additive on charge photogeneration dynamics of PTB7-based polymer solar cells is still poorly understood. In this work, the effect of DIO additive on the carrier photogeneration dynamics, as well as device performance of PTB7: [6,6]-phenyl-C71-butyric acid methyl ester (PC71BM) solar cells was studied. Bias-dependent photoluminescence (PL) experiments of a neat PTB7 device show that the exciton cannot be dissociated by the electric field in the device within the operating voltage range, but it can be effectively dissociated by the high electric field. PL and time-resolved PL studies show that DIO additive reduces the phase size of PTB7 in the blend film, resulting in an increased exciton dissociation efficiency. The carrier recombination processes were studied by transient absorption, which shows geminate carrier recombination was suppressed in the DIO-treated PTB7:PC71BM device in ultrafast time scale. The increased exciton dissociation efficiency and suppressed carrier recombination in ultrafast time scale play an important role for DIO-treated PTB7:PC71BM solar cells to attain a higher power conversion efficiency.

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13

De Simone, Giovanna, Alessandra di Masi, Alessandra Pesce, Martino Bolognesi, Chiara Ciaccio, Lorenzo Tognaccini, Giulietta Smulevich, et al. "Mycobacterial and Human Ferrous Nitrobindins: Spectroscopic and Reactivity Properties." International Journal of Molecular Sciences 22, no. 4 (February 7, 2021): 1674. http://dx.doi.org/10.3390/ijms22041674.

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Structural and functional properties of ferrous Mycobacterium tuberculosis (Mt-Nb) and human (Hs-Nb) nitrobindins (Nbs) were investigated. At pH 7.0 and 25.0 °C, the unliganded Fe(II) species is penta-coordinated and unlike most other hemoproteins no pH-dependence of its coordination was detected over the pH range between 2.2 and 7.0. Further, despite a very open distal side of the heme pocket (as also indicated by the vanishingly small geminate recombination of CO for both Nbs), which exposes the heme pocket to the bulk solvent, their reactivity toward ligands, such as CO and NO, is significantly slower than in most hemoproteins, envisaging either a proximal barrier for ligand binding and/or crowding of H2O molecules in the distal side of the heme pocket which impairs ligand binding to the heme Fe-atom. On the other hand, liganded species display already at pH 7.0 and 25 °C a severe weakening (in the case of CO) and a cleavage (in the case of NO) of the proximal Fe-His bond, suggesting that the ligand-linked movement of the Fe(II) atom onto the heme plane brings about a marked lengthening of the proximal Fe-imidazole bond, eventually leading to its rupture. This structural evidence is accompanied by a marked enhancement of both ligands dissociation rate constants. As a whole, these data clearly indicate that structural–functional relationships in Nbs strongly differ from what observed in mammalian and truncated hemoproteins, suggesting that Nbs play a functional role clearly distinct from other eukaryotic and prokaryotic hemoproteins.

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14

Kubo, Minoru, Takeshi Uchida, Satoru Nakashima, and Teizo Kitagawa. "Construction of a Subnanosecond Time-Resolved, High-Resolution Ultraviolet Resonance Raman Measurement System and its Application to Reveal the Dynamic Structures of Proteins." Applied Spectroscopy 62, no. 1 (January 2008): 30–37. http://dx.doi.org/10.1366/000370208783412573.

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A subnanosecond time-resolved ultraviolet (UV) resonance Raman system has been developed to study protein structural dynamics. The system is based on a 1 kHz Nd:YLF-pumped Ti: Sapphire regenerative amplifier with harmonic generation that can deliver visible (412, 440, 458, and 488 nm) and UV (206, 220, 229, and 244 nm) pulses. A subnanosecond (0.2 ns) tunable near-infrared pulse from a custom-made Ti: Sapphire oscillator is used to seed the regenerative amplifier. A narrow linewidth of the subnanosecond pulse offers the advantage of high resolution of UV resonance Raman spectra, which is critical to obtain site-specific information on protein structures. By combination with a 1 m single spectrograph equipped with a 3600 grooves/mm holographic grating and a custom-made prism prefilter, the present system achieves excellent spectral (<10 cm−1) and frequency (∼1 cm−1) resolutions with a relatively high temporal resolution (<0.5 ns). We also report the application of this system to two heme proteins, hemoglobin A and CooA, with the 440 nm pump and 220 nm probe wavelengths. For hemoglobin A, a structural change during the transition to the earliest intermediate upon CO photodissociation is successfully observed, specifically, nanosecond cleavage of the A–E interhelical hydrogen bonds within each subunit at Trpα14 and Trpβ15 residues. For CooA, on the other hand, rapid structural distortion (<0.5 ns) by CO photodissociation and nanosecond structural relaxation following CO geminate recombination are observed through the Raman bands of Phe and Trp residues located near the heme. These results demonstrate the high potential of this instrument to detect local protein motions subsequent to photoreactions in their active sites.

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15

Cardenas-Conejo, Y., G. Arguello-Astorga, A. Poghosyan, J. Hernandez-Gonzalez, V. Lebsky, J. Holguin-Peña, D. Medina-Hernandez, and S. Vega-Peña. "First Report of Tomato yellow leaf curl virus Co-infecting Pepper with Tomato chino La Paz virus in Baja California Sur, Mexico." Plant Disease 94, no. 10 (October 2010): 1266. http://dx.doi.org/10.1094/pdis-06-10-0444.

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Chile peppers are among the most common and important crops in the State of Baja California Sur, Mexico, where diverse varieties of this crop are annually cultivated. The “chile ancho” (Capsicum annuum L. var. ancho poblano) is one of the most popular hot peppers that is exported fresh to the United States. During a survey in December of 2007 in an experimental field of the CIBNOR in El Carrizal, one of the principal farm districts in the state, a high incidence of yellowing, stunted growth with shortened internodes, foliage discoloration, malformation and crinkle, abortion of flowers, and reduction in size and quantity of fruit were noted in chile ancho. Symptoms and the presence of large populations of whiteflies in the field suggested a possible viral etiology of disease. The symptoms of disease were successfully transmitted by grafting from field plants to tomato and pepper test plants. Samples from both field and test plants were analyzed by scanning electron microscopy (SEM) and molecular techniques. SEM study revealed groups of geminate particles characteristic of begomoviruses (Geminiviridae) in phloem tissue of randomly selected symptomatic plants (four field and two test plants). Total DNA from 12 symptomatic plants (eight naturally infected and four test plants) was obtained by a modified Dellaporta method and analyzed by PCR using the begomovirus universal primers prRepDGR (2) and prC889 (3). Amplicons of ~1.4 kb were obtained from all plant samples and PCR products from four of them were cloned into pGEM-T Easy vector (Promega, Madison, WI) and subsequently analyzed by restriction fragment length polymorphism (RFLP) using EcoRI and HinfI. Two distinct restriction fragment patterns were observed among the cloned PCR products, indicating the occurrence of at least two viruses in the infected plant tissues. The four examined samples contained the same two begomoviruses according to the RFLP analysis data. The complete sequence of the genomic component A of those viruses was determined by PCR amplification of viral DNA with universal, degenerate primers previously described (2), the subsequent cloning of overlapped PCR products, and sequencing. The full-length DNA-A sequence was assembled and compared with viral sequences available at the GenBank database using BlastN and the ClustalV alignment method (MegAlign; DNASTAR, Madison, WI). The 2,781-bp complete genome sequence of one co-infecting monopartite begomovirus (Accession No. HM459851) displayed the highest identity (99%) with Tomato yellow leaf curl virus (TYLCV), isolate Guasave, Sinaloa (Accession No. FJ609655). The 2,609-bp DNA-A sequence of the second begomovirus exhibited the highest nucleotide identity (96%) with Tomato chino La Paz virus (ToChLPV)-[Baja California Sur] (Accession No. AY339619). The presence of TYLCV in this region of Mexico had not been previously reported nor was ToChLPV detected in pepper until now. To our knowledge, this is the first report of a mixed infection of pepper plants with TYLCV and a bipartite begomovirus in Baja California Peninsula. Since the high frequency of recombination events observed in begomovirus mixed infections involving TYLCV (1), it would be important to monitor the possible emergence of ToChLPV-TYLCV recombinants with higher potential virulence. References: (1) S. García-Andrés et al. Virology 365:210, 2007. (2) A. Mauricio-Castillo et al. Plant Dis. 91:1513, 2007. (3) S. D. Wyatt and J. K. Brown. Phytopathology 86:1288, 1996.

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