Bibliografías temáticas / CO geminate recombination

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Literatura académica sobre el tema "CO geminate recombination"

Autor: Grafiati
Publicado: 10 de marzo de 2023

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Artículos de revistas sobre el tema "CO geminate recombination"

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STEVENSON, Thirza H., Aldo F. GUTIERREZ, Wendy K. ALDERTON, Lu-yun LIAN y 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, n.º 1 (8 de agosto de 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 y 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, n.º 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 y V. S. Sharma. "Geminate recombination of CO in rabbit, opossum, and adult hemoglobins." Journal of Biological Chemistry 260, n.º 5 (marzo de 1985): 2752–56. http://dx.doi.org/10.1016/s0021-9258(18)89425-x.

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Tian, Wei Dong, Andrew V. Wells, Paul M. Champion, Carmelo Di Primo, Nancy Gerber y Stephen G. Sligar. "Measurements of CO Geminate Recombination in Cytochromes P450 and P420". Journal of Biological Chemistry 270, n.º 15 (14 de abril de 1995): 8673–79. http://dx.doi.org/10.1074/jbc.270.15.8673.

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5

Maréchal, Amandine, W. John Ingledew y Peter R. Rich. "Time-resolved FTIR study of CO recombination with horseradish peroxidase". Biochemical Society Transactions 36, n.º 6 (19 de noviembre de 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 y Douglas Magde. "Geminate Recombination of Diatomic Ligands CO, O2, and NO with Myoglobin". Biochemistry 33, n.º 8 (marzo de 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 y 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, n.º 1 (marzo de 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 y Paul M. Champion. "Effect of DNA Binding on Geminate CO Recombination Kinetics in CO-sensing Transcription Factor CooA". Journal of Biological Chemistry 287, n.º 26 (28 de abril de 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, n.º 49 (diciembre de 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, n.º 9 (3 de mayo de 1988): 3507–11. http://dx.doi.org/10.1021/bi00409a057.

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Tesis sobre el tema "CO geminate recombination"

1

Barry, Justin. "The Solvent Cage Effect: Using Microviscosity to Predict the Recombination Efficiency of Geminate Radicals Formed by the Photolysis of the Mo-Mo Bond of Cpʹ2Mo2(CO)6". Thesis, University of Oregon, 2018. http://hdl.handle.net/1794/23713.

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Radicals are core reactive species that occur in almost every subfield of chemistry. In particular, solution phase radicals find their way into biochemistry (e.g. vitamin B12), and in polymer chemistry (e.g. radical polymerizations) just to name a few. Yet, given the proliferation of radical chemistry, there are still fundamental aspects of it that are poorly understood. This dissertation probed factors that influence the solvent cage effect. The solvent cage effect is where two radicals are held in close proximity to one another and prevented from easily escaping (to form free radicals) by a cage of solvent molecules. A convenient metric of the solvent cage effect is the radical recombination efficiency (FcP). Typically, FcP correlates with the bulk viscosity of the solution, however, this parameter only produces qualitative assessments. This dissertation outlines a method to quantitatively predict FcP using the microviscosity. This microviscosity dependence holds for non polar, aromatic, polar, and hydrogen-bonding solvents, along with solutions that contain polymers. Microviscosity is a great metric because it addresses an underlying reason for the solvent cage effect, the strength of the cage. Not only does the strength of the solvent cage around the radical pair affect FcP, but so does the identity of the radicals themselves. That is, the strength of the solvent cage is one piece to forming a total predictive model. FcP for the Cp'2Mo2(CO)6 dimer also varies with the wavelength of irradiation. Identifying the mechanism by which this wavelength dependence occurs may also provide another factor to include in an overall model of the solvent cage effect. Also, an attempt at synthesizing an asymmetric molybdenum dimer was performed. This asymmetric dimer would allow the study of solvent caged radical pairs that are different from each other. Predicting the photochemical cage pair recombination efficiency (FcP) is the major topic of this dissertation. However, there is also the collisional cage recombination efficiency (Fcʹ). This is where free radicals come together in what is called a collisional solvent cage pair. A method and values of Fcʹ are detailed later in this dissertation. This dissertation contains previously published and unpublished co-authored material.
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2

PATRIZI, BARBARA. "Dissociation and Geminate Recombination of CO in Truncated Hemoglobins Probed by Ultrafast Infrared Spectroscopy". Doctoral thesis, 2013. http://hdl.handle.net/2158/801471.

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The possibility to follow CO recombination dynamics, in the middle infrared spectral region, after photolysis induced by a short laser pulse provides unique information about the influence of structural and electrostatic properties of the distal heme pocket on the ligand dissociation and rebinding processes occurring in globin proteins. Time-Resolved Infrared Spectroscopy can probe the dynamics of the vibrational bands of the ligand before and after photolysis, thus providing a direct snapshot of the transient state of the photolyzed CO in truncated hemoglobins.
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Actas de conferencias sobre el tema "CO geminate recombination"

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Owrutsky, Jeffrey C. y Andrew P. Baronavski. "Ultrafast Infrared Study of the UV Photodissociation of Mn2(CO)10". En International Conference on Ultrafast Phenomena. Washington, D.C.: Optica Publishing Group, 1996. http://dx.doi.org/10.1364/up.1996.pdp.4.

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The 310 nm photodissociation of Mn2(CO)l0 in cyclohexane has been studied using sub-picosecond IR detection near 5 μm. Photodissociation of Mn2(CO)10 results in two photoproducts, Mn(CO)5 and Mn2(CO)9 The latter undergoes an internal rearrangement to form a semi-bridged CO bond that is suspectible to solvent ligand exchange in electron donating solvents. Photodissociation dynamics have been previously studied using ultrafast UV/vis spectroscopy indicating sub-ps geminate recombination [1] and vibrational relaxation of the products. [2] This study utilizes ultrafast IR detection because it provides band-resolved spectra and is uniquely suited to identify and monitor the bridge bond via the isolated bridge band near 1760 cm−1. This has clearly been demonstrated by flash photolysis studies of Mn2(CO)10 in many environments.[3]
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2

Kholodenko, Yuriy, Martin Volk, Ed Gooding y Robin M. Hochstrasser. "New Features in the Ultrafast Ligand Dynamics and Energy Dissipation in Myoglobin". En International Conference on Ultrafast Phenomena. Washington, D.C.: Optica Publishing Group, 1996. http://dx.doi.org/10.1364/up.1996.tue.23.

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Numerous transformations in heme proteins can be triggered upon photoexcitation, providing perfect model systems for the study of protein dynamics. In particular, the recombination of CO after photodissociation has been investigated in great detail. It was found to occur on the ns time scale. In contrast, the geminate recombination of NO proceeds much faster, within several 100 ps, i.e. on the same time scale as the relaxation of the protein to its unligated structure [1]. Furthermore, the recombination of NO was found to be nonexponential. Several mechanisms have been suggested to explain this behavior: (i) distribution of the barrier to rebinding due to different protein substates (inhomogeneous model), (ii) time dependence of the barrier due to protein/heme relaxation to the unligated structure or (iii) dissociation of the ligand to different intermediate sites in the protein. We are investigating these possibilities by time resolved IR measurements of the NO recombination. Furthermore, the comparison of native heme proteins with specially designed mutants will discriminate between the different mechanisms. We have also investigated the effect of the amount of excess energy in the precursor state on the resulting dynamics. The question is whether a higher excitation energy leads to the release of a ligand with higher kinetic energy, and thereby results in different intermediate protein sites, or whether the excess energy simply leads to hotter heme product which then undergoes vibrational cooling.
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3

Dyer, R. Brian y Timothy P. Causgrove. "Ultrafast Protein Relaxation: Time-Resolved Infrared Studies of Protein Dynamics Triggered by CO Photodissociation from CO Myoglobin". En International Conference on Ultrafast Phenomena. Washington, D.C.: Optica Publishing Group, 1994. http://dx.doi.org/10.1364/up.1994.tub.4.

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A critical feature of the biological function of heme proteins is the direct coupling of protein motion to the process of binding exogenous ligands to the heme. In carbonmonoxymyoglobin (MbCO), a substantial, specific conformational relaxation is associated with the transition from the ligated to the unligated form of the protein. The analogous tertiary structural changes of the monomer heme subunits of hemoglobin ultimately lead to the R→T quaternary structural transition, the allosteric control mechanism of O2 binding efficiency [1]. We have studied these processes on the earliest timescales, using picosecond, time-resolved infrared (TRIR) spectroscopy. It has long been known that infrared spectra in the amide region are sensitive to protein secondary conformation [2]. Recent advances in equipment and techniques have permitted researchers to quantitatively predict secondary structures from infrared spectra [3,4], particularly in the amide I region [4]. Therefore, it is now possible to study protein motion in time-resolved experiments on dynamics and function. The ligation reactions of small molecules such as CO with the heme site of Mb exemplify the mechanisms available to O2. CO is an ideal candidate for initial time-resolved IR experiments in the amide I region because it is easily photolyzed, little geminate recombination [5], and the structure of both MbCO and unligated Mb have been studied by crystallographic methods [6]. TRIR has already been applied to the stretching vibrations of the bound and free CO ligand [7,8]; dynamics of the protein, however, have yet to be probed by TRIR spectroscopy of the protein vibrations. Here we report results on the motions of the protein in response to ligation reactions, probed in the amide I region centered about 1650 cm-1.
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