Direct observation of subpicosecond vibrational dynamics in photoexcited myoglobin

Ferrante, Carino; Pontecorvo, E.; Cerullo, Giulio; Vos, Marten H.; Scopigno, T.

doi:10.1038/nchem.2569

Cited by 44 publications

(58 citation statements)

References 53 publications

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“…Lineshape modifications, such as dispersive or broad profiles, can potentially hamper the spectral interpretation. On the basis of the present observations and on Ferrante et al and Batignani et al, this seems not to be the case in Mb, for which sharply positively peaked SRRS features have been reported. A crucial advantage of the presented SRS experiment is represented by the possibility of continuously tuning the RP wavelength, allowing a fine mapping of the Raman excitation profiles along the sample absorption bands, as recently shown in Batignani et al…”

Section: Discussioncontrasting

confidence: 57%

“…Our results substantiate the potential of this technique as a competitive candidate for the vibrational characterization of complex macromolecules. Moreover, the extension of SRS to the domains of microscopy and time‐resolved studies boosts its significance as a state‐of‐the‐art spectroscopic tool for the biochemical and material sciences.…”

Section: Discussionmentioning

confidence: 99%

“…Down to a few picoseconds, the vibrational evolution can be tracked by single pulse techniques as transient Resonance Raman Scattering and pump‐probe experiments as in time‐resolved resonant Raman . These methods, however, become ineffective in the exploration of subpicosecond temporal realms, due to the fundamental restrictions dictated by the Fourier transform limit.…”

Section: Introductionmentioning

confidence: 99%

“…Beyond assessing the spectral equivalence with RRS, understanding the SRRS response at different electronic and vibrational resonances is of primary importance for both ultrafast and imaging applications.…”

Section: Introductionmentioning

confidence: 99%

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Resonant broadband stimulated Raman scattering in myoglobin

Ferrante

Batignani

Fumero

et al. 2018

J Raman Spectroscopy

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Spontaneous Raman is a well‐established tool to probe molecular vibrations. Under resonant conditions, it is a largely used method for characterizing the structure of heme‐proteins. In recent years, advances in pulsed laser sources allowed to explore vibrational features with complex techniques based on nonlinear optical interactions, among which is stimulated Raman scattering (SRS). Building on its combined spectral–temporal resolutions and high chemical sensitivities, SRS has been largely applied as a probe for ultrafast, time‐resolved studies, as well as an imaging technique in biological systems. By using a frequency tunable, narrowband pump pulse jointly with a femtosecond white light continuum to initiate the SRS process, here we measure the Raman spectrum of a prototypical heme‐protein, namely deoxy myoglobin, under two different electronic resonances. The SRS results are compared with the spontaneous Raman spectra, and the relative advantages, such as the capability of our experimental approach to provide an accurate mapping of Raman excitation profiles, are discussed.

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Section: Discussioncontrasting

confidence: 57%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Resonant broadband stimulated Raman scattering in myoglobin

Ferrante

Batignani

Fumero

et al. 2018

J Raman Spectroscopy

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“…For the reduced forms, a minimum of three exponential phases were required, with time constants of ~0.3 ps, ~1.3 ps and ~5 ps, These should be regarded as mean timescales on which the processes in different hemes take place. The faster phases, corresponding to blue shifting of induced absorption bands, presumably predominantly reflect photophysical relaxation processes, including vibrational cooling 3, 12, 21 . Here, we focus on the spectral characteristics of the slower processes on the time scale of a few picoseconds, leading to recovery of the initial states (Fig.…”

Section: Resultsmentioning

confidence: 99%

Ultrafast photochemistry of the bc₁complex

Vos

Reeder

Daldal

et al. 2017

Phys. Chem. Chem. Phys.

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We present a full investigation of ultrafast light-induced events in the membraneous cytochrome bc1 complex by transient absorption spectroscopy. This energy-transducing complex harbors four redox-active components per monomer: heme c1, two 6-coordinate b-hemes and a [2Fe-2S] cluster. Using excitation of these components in different ratios under various excitation conditions, probing in the full visible range and under three well-defined redox conditions, we demonstrate that for all ferrous hemes of the complex photodissociation of axial ligands takes place and that they rebind in 5–7 ps, as in other 6-coordinate heme proteins, including cytoglobin, which is included as a reference in this study. By contrast, the signals are not consistent with photooxidation of the b hemes. This conclusion contrasts with a recent assessment based on a more limited data set. The binding kinetics of internal and external ligands are indicative of a rigid heme environment, consistent with the electron transfer function. We also report, for the first time, photoactivity of the very weakly absorbing iron-sulfur center. This yields the unexpected perspective of studying photochemistry, initiated by excitation of iron-sulfur clusters, in a range of protein complexes.

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Exciplex Formation in Lipid‐bound Escherichia coli Flavohemoglobin

Marcelli¹,

Patrizi

Bonamore

et al. 2021

ChemPhysChem

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Flavohemoglobins have the particular capability of binding unsaturated and cyclopropanated fatty acids as free acids or phospholipids. Fatty acid binding to the ferric heme results in a weak but direct bonding interaction. Ferrous and ferric protein, in presence or absence of a bound lipid molecule, have been characterized by transient absorption spectroscopy. Measurements have been also carried out both on the ferrous deoxygenated and on the CO bound protein to investigate possible long‐range interaction between the lipid acyl chain moiety and the ferrous heme. After excitation of the deoxygenated derivatives the relaxation process reveals a slow dynamics (350 ps) in lipid‐bound protein but is not observed in the lipid‐free protein. The latter feature and the presence of an extra contribution in the absorption spectrum, indicates that the interaction of iron heme with the acyl chain moiety occurs only in the excited electronic state and not in the ground electronic state. Data analysis highlights the formation of a charge‐transfer complex in which the iron ion of the lipid‐bound protein in the expanded electronic excited state, possibly represented by a high spin Fe III intermediate, is able to bind to the sixth coordination ligand placed at a distance of at 3.5 Å from the iron. A very small nanosecond geminate rebinding is observed for CO adduct in lipid‐free but not in the lipid‐bound protein. The presence of the lipid thus appears to inhibit the mobility of CO in the heme pocket.

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Direct observation of subpicosecond vibrational dynamics in photoexcited myoglobin

Cited by 44 publications

References 53 publications

Resonant broadband stimulated Raman scattering in myoglobin

Resonant broadband stimulated Raman scattering in myoglobin

Ultrafast photochemistry of the bc₁complex

Exciplex Formation in Lipid‐bound Escherichia coli Flavohemoglobin

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Direct observation of subpicosecond vibrational dynamics in photoexcited myoglobin

Cited by 44 publications

References 53 publications

Resonant broadband stimulated Raman scattering in myoglobin

Resonant broadband stimulated Raman scattering in myoglobin

Ultrafast photochemistry of the bc1complex

Exciplex Formation in Lipid‐bound Escherichia coli Flavohemoglobin

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Ultrafast photochemistry of the bc₁complex