Zobrazeno 1 - 10
of 49
pro vyhledávání: '"Daniel Lavalette"'
Publikováno v:
Biochemical Society Transactions. 34:975-978
Biophysical techniques developed during the last three decades have provided an increasingly detailed description of the internal processes associated with ligand capture and release by haem proteins. Myoglobin has long been the paradigm for these st
Autor:
Catherine Tetreau, Daniel Lavalette
Publikováno v:
Biochimica et Biophysica Acta (BBA) - General Subjects. 1724:411-424
Here, we review the dominant aspects of protein dynamics as revealed by studying hemoproteins using the combination of laser flash photolysis, kinetic spectroscopy and low temperature. The first breakthrough was the finding that geminate ligand rebin
Autor:
Catherine Tetreau, Daniel Lavalette
Publikováno v:
European Journal of Biochemistry. 177:97-108
The recombination kinetics of photo-dissociated oxyhemerythrin (Sipunculus nudus) have been investigated between 298 K and 90 K. Fast geminate recombinations compete with oxygen escape into the solvent, from which a subsequent slower bimolecular rebi
Autor:
Catherine Tetreau, Yves Blouquit, Samuel Murail, Liliane Mouawad, Daniel Lavalette, Patricia Duchambon
Publikováno v:
Biophysical Journal. 88:1250-1263
In this work we show that ligand migration and active site conformational relaxation can occur independently of each other in hemoproteins. The complicated kinetics of carbon monoxide rebinding with cytochrome P450cam display up to five distinct proc
Publikováno v:
Biophysical Journal. 86(1):435-447
Evidence for ligand migration toward the xenon-binding cavities in myoglobin comes from a number of laser photolysis studies of MbO2 including mutants and from cryo- and time-resolved crystallography of MbCO. To explore ligand migration in greater de
Publikováno v:
Biochemistry. 39:14219-14231
Photodissociation of (CO)P-450(cam)(substrate) complexes was found to trigger a conformational relaxation process that interferes with ligand rebinding at temperatures as low as 140 K even though the protein conformational substates (CS(1)) remain fr
Publikováno v:
Biochemistry. 38:7210-7218
The dynamics of CO rebinding with neuronal NO synthase (nNOS) following laser flash photolysis have been investigated from 293 to 77 K in the absence and presence of its substrate L-arginine. The distribution functions of the rate parameters P(k) and
Publikováno v:
Biochemistry. 36:10262-10275
The dynamics of CO rebinding with cytochromes P-450cam, P-450scc, and P-450LM2 after laser flash photolysis have been investigated from 293 to 77 K, and the distribution functions of the rate parameters P(k) and of the activation enthalpy P(H) were d
Publikováno v:
Journal of the American Chemical Society. 117:6041-6047
Publikováno v:
Biophysical Journal. 68(2):665-670
Laser photodissociation of respiratory proteins is followed by fast geminate recombination competing with escape of the oxygen molecule into the solvent. The escape rate from myoglobin or hemerythrin has been shown previously to exhibit a reciprocal