Experiments with proteins at low temperature: What do we learn on properties in their functional state?

Ponkratov, Vladimir V.; Wiedersich, J.; Friedrich, J.; Vanderkooi, J. M.

doi:10.1063/1.2723731

Cited by 3 publications

(1 citation statement)

References 34 publications

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“…Absorption spectra and MCD of unstable high-valent intermediates in heme enzymes have been described by Gasyna, Stillman and coworkers (76,89-91). Application of cryogenic optical spectroscopy to biophysical chemistry of proteins, including heme enzymes, has been described by Vanderkooi, Friedrich and colleagues (11,34,92-98). Frauenfelder and colleagues systematically applied various spectroscopic methods at cryogenic temperatures to study fundamental aspects of protein structure and dynamics (12,99-101).…”

Section: Additional Readingmentioning

confidence: 99%

Cryoradiolysis and Cryospectroscopy for Studies of Heme-Oxygen Intermediates in Cytochromes P450

Denisov

Grinkova

Sligar

2012

Methods in Molecular Biology

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Cryogenic radiolytic reduction is one of the most simple and convenient methods of generation and stabilization of reactive iron-oxygen intermediates for mechanistic studies in chemistry and biochemistry. The method is based on one-electron reduction of the precursor complex in frozen solution via exposure to the ionizing radiation at cryogenic temperatures. Such approach allows for accumulation of the fleeting reactive complexes which otherwise could not be generated at sufficient amount for structural and mechanistic studies. Application of this method allowed for characterizing of peroxoferric and hydroperoxo-ferric intermediates, which are common for the oxygen activation mechanism in cytochromes P450, heme oxygenases and nitric oxide synthases, as well as for the peroxide metabolism by peroxidases and catalases.

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Section: Additional Readingmentioning

confidence: 99%

Cryoradiolysis and Cryospectroscopy for Studies of Heme-Oxygen Intermediates in Cytochromes P450

Denisov

Grinkova

Sligar

2012

Methods in Molecular Biology

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Protein elasticity determined by pressure tuning of the tyrosine residue of ubiquitin

Somoza

Wiedersich

Friedrich

2007

The Journal of Chemical Physics

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We determined the isotropic, isothermal compressibility of ubiquitin by pressure tuning spectral holes burnt into the red edge of the absorption spectrum of the single tyrosine residue. The pressure shift is perfectly linear with burn frequency. From these data, a compressibility of 0.086 GPa(-1) in the local environment of the tyrosine residue could be determined. This value fits nicely into the range known for proteins. Although the elastic behavior at low temperatures does not show any unusual features, the pressure tuning behavior at room temperature is quite surprising: the pressure-induced spectral shift is close to zero, even up to very high pressure levels of 0.88 GPa, well beyond the denaturation point. The reason for this behavior is attributed to equally strong blue as well as red spectral pressure shifts resulting in an average pressure-induced solvent shift that is close to zero.

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Protein elasticity probed with two synchrotron-based techniques

Leu

Alataş

Sinn

et al. 2010

The Journal of Chemical Physics

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Compressibility characterizes three interconnecting properties of a protein: dynamics, structure, and function. The compressibility values for the electron-carrying protein cytochrome c and for other proteins, as well, available in the literature vary considerably. Here, we apply two synchrotron-based techniques--nuclear resonance vibrational spectroscopy and inelastic x-ray scattering--to measure the adiabatic compressibility of this protein. This is the first report of the compressibility of any material measured with this method. Unlike the methods previously used, this novel approach probes the protein globally, at ambient pressure, does not require the separation of protein and solvent contributions to the total compressibility, and uses samples that contain the heme iron, as in the native state. We show, by comparing our results with molecular dynamics predictions, that the compressibility is almost independent of temperature. We discuss potential applications of this method to other materials beyond proteins.

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Experiments with proteins at low temperature: What do we learn on properties in their functional state?

Cited by 3 publications

References 34 publications

Cryoradiolysis and Cryospectroscopy for Studies of Heme-Oxygen Intermediates in Cytochromes P450

Cryoradiolysis and Cryospectroscopy for Studies of Heme-Oxygen Intermediates in Cytochromes P450

Protein elasticity determined by pressure tuning of the tyrosine residue of ubiquitin

Protein elasticity probed with two synchrotron-based techniques

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