Kinetics of Histidine Deligation from the Heme in GuHCl-Unfolded Fe(III) Cytochrome <i>c</i> Studied by a Laser-Induced pH-Jump Technique

Abbruzzetti, Stefania; Viappiani, Cristiano; Small, Jeanne Rudzki; Libertini, Louis J.; Small, Enoch W.

doi:10.1021/ja010079n

Cited by 38 publications

(55 citation statements)

References 36 publications

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“…The photoexcitation of an aqueous solution of 2-NBA with a 355 nm nanosecond laser pulse leads to the release of protons in high yield (Φ H + ) 0.45) within a few nanoseconds (25,(27)(28)(29). The concentration of photoreleased protons can reach the range of 10 -4 M with laser pulses of a few tens of mJ (30,31). At low laser pulse energies, the concentration of photoreleased protons is proportional to the laser pulse energy.…”

Section: Methodsmentioning

confidence: 99%

Molten Globule Formation in Apomyoglobin Monitored by the Fluorescent Probe Nile Red

et al. 2006

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The interaction of nile red (NR) with apomyoglobin (ApoMb) in the native (pH 7) and molten globule (pH 4) states was investigated using experimental and computational methods. NR binds to hydrophobic locations in ApoMb with higher affinity (K d ) 25 ( 5 µM) in the native state than in the molten globule state (K d ) 52 ( 5 µM). In the molten globule state, NR is located in a more hydrophobic environment. The dye does not bind to the holoprotein, suggesting that the binding site is located at the heme pocket. In addition to monitoring steady-state properties, the fluorescence emission of NR is capable of tracking submillisecond, time-resolved structural rearrangements of the protein, induced by a nanosecond pH jump. Molecular dynamics simulations were run on ApoMb at neutral pH and at pH 4. The structure obtained for the molten globule state is consistent with the experimentally available structural data.

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Section: Methodsmentioning

confidence: 99%

Molten Globule Formation in Apomyoglobin Monitored by the Fluorescent Probe Nile Red

et al. 2006

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“…This proton releasing reaction was applied to the pH change of a solution containing Mb and Cyt c to monitor the protein unfolding dynamics of Mb and Cyt c by the PA method and transient absorption method, respectively. 3,8 To study the NBA reaction with the presence of a protein, we investigated the TG signal with Mb in NBA aqueous solution. We found that the TG signal changed dramatically by adding the protein as shown in Figure 4.…”

Section: Electrolytementioning

confidence: 99%

“…3,8 Protein folding of apomyoglobin (Mb) 3 and cytochrome c (Cyt c) 8 were studied by the photoactoustic (PA) method and transient absorption method, respectively. However, in their analyses, the photochemical reaction of NBA is assumed to be the same as that in aqueous solution.…”

Section: Introductionmentioning

confidence: 99%

Photochemical Reaction of 2-Nitrobenzaldehyde by Monitoring the Diffusion Coefficient

Choi

Terazima

2003

J. Phys. Chem. B

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The photochemical reaction of 2-nitrobenzaldehyde (NBA) in various electrolyte solutions as well as in a solution with a protein is investigated from the viewpoint of the diffusion coefficient by using the timeresolved transient grating (TG) method. For studying reaction with optically silent materials such as electrolytes, we found that the diffusion coefficient is useful for identifying chemical species involved in the reaction. The TG signal that represents the diffusion process was dramatically changed by adding electrolytes such as Clor Br -, and this result indicates that these electrolytes should participate in the photochemical reaction of NBA. It was found that the time profile of the grating signal also depends on the addition of guanidine-HCl or apomyoglobin. The structural change of the protein associated with the NBA reaction is discussed.

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“…Photoinduced pH jumps use the application of a laser pulse to induce proton transfer to or from a small molecule included in the reaction buffer. The proton transfer kinetics are extremely fast; the time resolution of a few nanoseconds is determined by shape of the pump laser pulse (Abbruzzetti et al ., 2001a; Abbruzzetti et al ., 2001b). As might be expected, pH jumps have been applied primarily to heme binding proteins (e.g.…”

Section: Learning From Simulation and Experimentsmentioning

confidence: 99%

Fast protein folding kinetics

Gelman

Gruebele

2014

Quart. Rev. Biophys.

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Fast folding proteins have been a major focus of computational and experimental study because they are accessible to both techniques: they are small and fast enough to be reasonably simulated with current computational power, but have dynamics slow enough to be observed with specially developed experimental techniques. This coupled study of fast folding proteins has provided insight into the mechanisms which allow some proteins to find their native conformation well less than 1 ms and has uncovered examples of theoretically predicted phenomena such as downhill folding. The study of fast folders also informs our understanding of even “slow” folding processes: fast folders are small, relatively simple protein domains and the principles that govern their folding also govern the folding of more complex systems. This review summarizes the major theoretical and experimental techniques used to study fast folding proteins and provides an overview of the major findings of fast folding research. Finally, we examine the themes that have emerged from studying fast folders and briefly summarize their application to protein folding in general as well as some work that is left to do.

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Kinetics of Histidine Deligation from the Heme in GuHCl-Unfolded Fe(III) Cytochrome c Studied by a Laser-Induced pH-Jump Technique

Cited by 38 publications

References 36 publications

Molten Globule Formation in Apomyoglobin Monitored by the Fluorescent Probe Nile Red

Molten Globule Formation in Apomyoglobin Monitored by the Fluorescent Probe Nile Red

Photochemical Reaction of 2-Nitrobenzaldehyde by Monitoring the Diffusion Coefficient

Fast protein folding kinetics

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