A photoacoustic calorimetry study of horse carboxymyoglobin on the 10-nanosecond time scale

Norris, Christopher L.; Peters, Kevin S.

doi:10.1016/s0006-3495(93)81223-2

Cited by 34 publications

(34 citation statements)

References 26 publications

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“…blood oxygen saturation level estimation) and visualization (e.g. imaging of melanin in tissue) of bio-medical samples, as also in calorimetric studies [18]. It can probe deep tissue regions because pressure waves are detected in the receiving end whose scattering is two to three orders of magnitude less than that of light and thus, can travel longer distance in tissue.…”

Section: Introductionmentioning

confidence: 99%

Computational Investigation on the Photoacoustics of Malaria Infected Red Blood Cells

Saha

Karmakar²,

Roy³

2012

PLoS ONE

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A computer simulation study on the possibility of using photoacoustic (PA) technique to differentiate intraerythrocytic stages of malarial parasite is reported. This parasite during its development substantially converts hemoglobin into hemozoin. This conversion is expected to alter the cellular absorption leading to changes in the PA emission of a red blood cell (RBC) at certain incident optical wavelengths. The PA signals from blood samples corresponding to ring, trophozoite and schizont stages were computed and compared with that of normal blood. A Monte Carlo algorithm was implemented generating random locations of RBCs in 3D to simulate blood samples. The average PA amplitude for wide bandwidth signals decreases for 434 nm incident radiation, but increases for 700 nm as the parasite matures. The spectral power at 7.5 MHz for the blood sample at the schizont stage compared to the normal blood is nearly reduced by 6 dB and enhanced by 22 dB at those incident wavelengths, respectively. Bandlimited signals for transducers of 15 and 50 MHz center frequencies were studied and found to exhibit similar characteristics. The presence of hemozoin inside the cells was examined and an excellent estimation was made. The simulation results suggest that intraerythrocytic stages of malarial parasite may be assessed using the PA technique.

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Section: Introductionmentioning

confidence: 99%

Computational Investigation on the Photoacoustics of Malaria Infected Red Blood Cells

Saha

Karmakar²,

Roy³

2012

PLoS ONE

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“…Essentially, the method is based on the fact that, after pulse excitation, a volume change takes place in the medium. This volume change may be composed of two terms: 1) the expansion or contraction due to the release of heat by radiationless processes from the excited molecules and 2) the pos-Thus, both contributions can be separated by temperaturedependent measurements (Callis et al, 1972;Norris and Peters, 1993; Peters et al, 1992). The volume change may be detected by a rapid pressure transducer and in this case we called the method laser-induced optoacoustic spectroscopy (LIOAS) (Braslavsky and Heibel, 1992).…”

Section: Introductionmentioning

confidence: 99%

Photoinduced volume change and energy storage associated with the early transformations of the photoactive yellow protein from Ectothiorhodospira halophila

Brederode¹,

Gensch²,

Hoff³

et al. 1995

Biophysical Journal

102

103

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The photocycle of the photoactive yellow protein (PYP) isolated from Ectothiorhodospira halophila was analyzed by flash photolysis with absorption detection at low excitation photon densities and by temperature-dependent laser-induced optoacoustic spectroscopy (LIOAS). The quantum yield for the bleaching recovery of PYP, assumed to be identical to that for the phototransformation of PYP (pG), to the red-shifted intermediate, pR, was phi R = 0.35 +/- 0.05, much lower than the value of 0.64 reported in the literature. With this value and the LIOAS data, an energy content for pR of 120 kJ/mol was obtained, approximately 50% lower than for excited pG. Concomitant with the photochemical process, a volume contraction of 14 ml/photoconverted mol was observed, comparable with the contraction (11 ml/mol) determined for the bacteriorhodopsin monomer. The contraction in both cases is interpreted to arise from a protein reorganization around a phototransformed chromophore with a dipole moment different from that of the initial state. The deviations from linearity of the LIOAS data at photon densities > 0.3 photons per molecule are explained by absorption by pG and pR during the laser pulse duration (i.e., a four-level system, pG, pR, and their respective excited states). The data can be fitted either by a simple saturation process or by a photochromic equilibrium between pG and pR, similar to that established between the parent chromoprotein and the first intermediate(s) in other biological photoreceptors. This nonlinearity has important consequences for the interpretation of the data obtained from in vitro studies with powerful lasers.

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“…Photoacoustics (PA) has been used to monitor CO photodetachment from related systems including heme proteins myoglobin (Mb) [37][38][39], cytochrome P450 cam (P450) [40][41][42] and horseradish peroxidase (HRP) [43]. Larsen and coworkers have applied photothermal techniques to study CO photodetachment from heme-copper oxidases [44][45][46], model compounds [47][48][49], and smaller heme proteins [50][51][52].…”

Section: Introductionmentioning

confidence: 99%

Photoacoustic characterization of protein dynamics following CO photodetachment from fully reduced bovine cytochrome c oxidase

Oertling

Cornellison

Treff

et al. 2007

Journal of Inorganic Biochemistry

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A photoacoustic calorimetry study of horse carboxymyoglobin on the 10-nanosecond time scale

Cited by 34 publications

References 26 publications

Computational Investigation on the Photoacoustics of Malaria Infected Red Blood Cells

Computational Investigation on the Photoacoustics of Malaria Infected Red Blood Cells

Photoinduced volume change and energy storage associated with the early transformations of the photoactive yellow protein from Ectothiorhodospira halophila

Photoacoustic characterization of protein dynamics following CO photodetachment from fully reduced bovine cytochrome c oxidase

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