Ultrafast relaxation in picosecond photolysis of nitrosylhemoglobin

Cornelius, P. A.; Hochstrasser, Robin M.; Steele, A W

doi:10.1016/0022-2836(83)90032-3

Cited by 106 publications

(84 citation statements)

References 17 publications

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“…The results show that the fitted 2 A PES has two welldefined minima, which correspond to the Fe-NO and Fe-ON states. These two states have already been found in earlier work 48,56 but are absent in other investigations.…”

Section: A the Fitted Pesmentioning

confidence: 80%

“…The root mean square error for the validation set as determined from the fitted PES was 1.0 kcal/mol and 1.1 kcal/mol for the 2 A and 4 A PESs, respectively. This is close to chemical accuracy except for errors in the quantum chemical methods used.…”

Section: A Intermolecular Interactionsmentioning

confidence: 97%

“…The calculations were carried out for the 2 A and 4 A states using a 3-dimensional grid resulting in 1210 and 1452 reference points for the two states, respectively. In addition, 100 validation points for both 2 A and 4 A states were computed at off-grid points for different values of r and θ = 30…”

Section: A Intermolecular Interactionsmentioning

confidence: 99%

“…1 The rebinding kinetics of NO to Mb has been studied intensively over the past three decades using experimental and computational methods. [2][3][4][5][6][7][8][9][10][11][12][13][14] Compared to rebinding of CO, no substantial rebinding barrier has been found for geminate recombination of NO to the heme Fe 3 and ab initio calculations have even suggested that the recombination reaction may be barrierless for NO in specific conformations. 15 Because of the short time scale involved (picoseconds), this process is ideally suited to be investigated computationally at an atomistic level.…”

Section: Introductionmentioning

confidence: 99%

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Reproducing kernel potential energy surfaces in biomolecular simulations: Nitric oxide binding to myoglobin

Soloviov

Meuwly

2015

The Journal of Chemical Physics

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A line integral reaction path approximation for large systems via nonlinear constrained optimization: Application to alanine dipeptide and the β hairpin of protein G J. Chem. Phys. 124, 194903 (2006) Multidimensional potential energy surfaces based on reproducing kernel-interpolation are employed to explore the energetics and dynamics of free and bound nitric oxide in myoglobin (Mb). Combining a force field description for the majority of degrees of freedom and the higher-accuracy representation for the NO ligand and the Fe out-of-plane motion allows for a simulation approach akin to a mixed quantum mechanics/molecular mechanics treatment. However, the kernel-representation can be evaluated at conventional force-field speed. With the explicit inclusion of the Fe-out-of-plane (Fe-oop) coordinate, the dynamics and structural equilibrium after photodissociation of the ligand are correctly described compared to experiment. Experimentally, the Fe-oop coordinate plays an important role for the ligand dynamics. This is also found here where the isomerization dynamics between the Fe-ON and Fe-NO state is significantly affected whether or not this co-ordinate is explicitly included.

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Section: A the Fitted Pesmentioning

confidence: 80%

Section: A Intermolecular Interactionsmentioning

confidence: 97%

Section: A Intermolecular Interactionsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Reproducing kernel potential energy surfaces in biomolecular simulations: Nitric oxide binding to myoglobin

Soloviov

Meuwly

2015

The Journal of Chemical Physics

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“…Because the binding of ligand proceeds on the picosecond or nanosecond time scale, time-resolved spectroscopy has been used to probe the binding dynamics and structural changes induced by ligand binding after photodeligation of the ligand-bound proteins. [2][3][4][5][6][7][8][9][10][11] The quantum yield (QY) of photodeligation for these ligands in the ligated ferrous heme proteins by Soret or Q-band excitation in the visible region is significant, 2,12 and the photodeligation occurs on a subpicosecond time scale;…”

Section: Introductionmentioning

confidence: 99%