Time-Resolved Photoacoustic Calorimetry: Probing the Energetics and Dynamics of Fast Chemical and Biochemical Reactions

Peters, Kevin S.; Snyder, Gary J.

doi:10.1126/science.3045967

Cited by 100 publications

(71 citation statements)

References 36 publications

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“…Experiments conducted at multiple temperatures (10–25°C) were used to determine the heat release and the structural volume change for each transient [33], [74], [75]. The pre-exponential factors φ i – multiplied by the photon energy E λ - were then plotted versus the thermoelastic parameter ratio of the solution.…”

Section: Methodsmentioning

confidence: 99%

Following Ligand Migration Pathways from Picoseconds to Milliseconds in Type II Truncated Hemoglobin from Thermobifida fusca

Marcelli¹,

Abbruzzetti

Bustamante

et al. 2012

PLoS ONE

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CO recombination kinetics has been investigated in the type II truncated hemoglobin from Thermobifida fusca (Tf-trHb) over more than 10 time decades (from 1 ps to ∼100 ms) by combining femtosecond transient absorption, nanosecond laser flash photolysis and optoacoustic spectroscopy. Photolysis is followed by a rapid geminate recombination with a time constant of ∼2 ns representing almost 60% of the overall reaction. An additional, small amplitude geminate recombination was identified at ∼100 ns. Finally, CO pressure dependent measurements brought out the presence of two transient species in the second order rebinding phase, with time constants ranging from ∼3 to ∼100 ms. The available experimental evidence suggests that the two transients are due to the presence of two conformations which do not interconvert within the time frame of the experiment. Computational studies revealed that the plasticity of protein structure is able to define a branched pathway connecting the ligand binding site and the solvent. This allowed to build a kinetic model capable of describing the complete time course of the CO rebinding kinetics to Tf-trHb.

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Section: Methodsmentioning

confidence: 99%

Following Ligand Migration Pathways from Picoseconds to Milliseconds in Type II Truncated Hemoglobin from Thermobifida fusca

Marcelli¹,

Abbruzzetti

Bustamante

et al. 2012

PLoS ONE

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“…the amount of light‐absorbing molecules (visible spectral region) in a single cell is so small that its light absorption and induced thermal phenomena cannot be detected with the techniques mentioned previously. Direct sensing of thermal phenomena may be carried out with laser calorimetric methods (33–40). Their main features are: (1) the registered signal is caused by heat only (no signal without heat release and no influence of scattered or fluorescent light); (2) there is an increase in sensitivity with an increase in radiation energy; and (3) ultimate sensitivity is limited by thermal fluctuations in the sample.…”

Section: Introductionmentioning

confidence: 99%

Photothermal Monitoring of Redox State of Respiratory Chain in Single Live Cells¶

Lapotko

Romanovskaya

Gordiyko

2002

Photochemistry and Photobiology

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A method for monitoring respiratory chain (RC) activity in single live cells is described. It is based on the registration of the photothermal (PT) response after a laser pulse of a live single cell. The dependence of the PT‐response amplitude and shape upon redox state of RC components was studied with a PT microscope for two in vitro models: (1) solutions of the RC component cytochrome c and (2) mice hepatocytes. The parameters of the PT responses differed for oxidized and reduced forms of cytochrome c solutions and for inhibited RC and intact RC. The latter difference may be caused by alteration of the quantum yields of thermal (nonradiative) relaxation for light‐absorbing molecules, i.e. RC components, as they undergo reduction during RC inhibition.

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“…Here a vibrationally excited protein relaxes by dissipating its energy into the solvent through acoustic waves that are generated from the transient expansion and recompression of the protein immediately following excitation that can be detected by a microphone 23 . Likewise, we propose that an enzyme expands, albeit asymmetrically, following the release of the heat of reaction (a process we call ‘chemoacoustic effect’).…”

mentioning

confidence: 99%

The heat released during catalytic turnover enhances the diffusion of an enzyme

Riedel

Gabizon

Wilson

et al. 2014

Nature

217

380

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Recent studies have shown that the diffusivity of enzymes increases in a substrate-dependent manner during catalysis1,2. Although this observation has been reported and characterized for several different systems3–10, the precise origin of this phenomenon is unknown. Calorimetric methods are often used to determine enthalpies from enzyme-catalysed reactions and can therefore provide important insight into their reaction mechanisms11,12. The ensemble averages involved in traditional bulk calorimetry cannot probe the transient effects that the energy exchanged in a reaction may have on the catalyst. Here we obtain single-molecule fluorescence correlation spectroscopy data and analyse them within the framework of a stochastic theory to demonstrate a mechanistic link between the enhanced diffusion of a single enzyme molecule and the heat released in the reaction. We propose that the heat released during catalysis generates an asymmetric pressure wave that results in a differential stress at the protein–solvent interface that transiently displaces the centre-of-mass of the enzyme (chemoacoustic effect). This novel perspective on how enzymes respond to the energy released during catalysis suggests a possible effect of the heat of reaction on the structural integrity and internal degrees of freedom of the enzyme.

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Time-Resolved Photoacoustic Calorimetry: Probing the Energetics and Dynamics of Fast Chemical and Biochemical Reactions

Cited by 100 publications

References 36 publications

Following Ligand Migration Pathways from Picoseconds to Milliseconds in Type II Truncated Hemoglobin from Thermobifida fusca

Following Ligand Migration Pathways from Picoseconds to Milliseconds in Type II Truncated Hemoglobin from Thermobifida fusca

Photothermal Monitoring of Redox State of Respiratory Chain in Single Live Cells¶

The heat released during catalytic turnover enhances the diffusion of an enzyme

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