Journal ArticleDOI
Assignment of Protoheme Resonance Raman Spectrum by Heme Labeling in Myoglobin
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In this paper, the Resonance Raman (RR) spectra are reported for myoglobin reconstituted with seven heme isotopomers which are labeled with 15N and meso-D4 in the porphyrin skeleton or at the propionate substituents.Abstract:
Resonance Raman (RR) spectra are reported for myoglobin reconstituted with seven heme isotopomers which are labeled with 15N and meso-D4 in the porphyrin skeleton or at the vinyl and propionate substituents. The RR bands are assigned to the porphyrin in-plane and out-of-plane modes as well as to the internal vibrations of substituents on the basis of the observed isotope shifts. The issue of vinyl substituent effects is revisited, and bands are assigned to the 2- or 4-vinyl group from selective deuteration shifts. Contributions of the aliphatic propionate groups are also revealed in the RR spectrum. The protein influence on the heme structure is reflected in the activation of several out-of-plane modes in the low-frequency region.read more
Citations
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Resonance Raman spectroscopy of red blood cells using near-infrared laser excitation.
TL;DR: New insights are provided into the vibrational dynamics, electronic structure and resonant enhancement of heme moieties within functional erythrocytes at near-IR excitation wavelengths and non-totally symmetric B1g modes in oxygenated cells.
Journal ArticleDOI
Surface-enhanced Raman scattering of whole human blood, blood plasma, and red blood cells: cellular processes and bioanalytical sensing.
TL;DR: SERS spectra of whole human blood, blood plasma, and red blood cells on Au nanoparticle SiO(2) substrates excited at 785 nm have been observed and can have significant impact in the area of clinical diagnostics, blood supply management, and forensics.
Journal ArticleDOI
Raman Spectroscopy of Blood and Blood Components
TL;DR: The literature in the field is reviewed, the published Raman spectroscopy studies of erythrocytes, leucocytes, platelets, plasma, and whole blood are collated, and general conclusions on the state of the field are drawn.
Journal ArticleDOI
Micro-Raman characterisation of the R to T state transition of haemoglobin within a single living erythrocyte.
TL;DR: The first recorded Raman spectra of haemoglobin in both the R and T states from within a single living erythrocyte are presented using 632.8 nm excitation, and the oxidation state marker band appeared invariant within this domain in all single cells and conditions investigated.
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Spectroscopic studies on the interaction between human hemoglobin and CdS quantum dots.
TL;DR: Results indicated that the sulfur atoms of the cysteine residues form direct chemical bonds on the surface of the CdS QDs, which does not significantly affect the spin state of the heme iron, and deoxidation is not expected to take place on the coated oxyhemoglobin.
References
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Journal ArticleDOI
Conformation change of cytochrome c. I. Ferrocytochrome c structure refined at 1.5 A resolution.
TL;DR: Tuna ferrocytochrome c has been crystallographically refined at a resolution of 1.5 A using the Diamond real-space method followed by Jack-Levitt restrained energy and reciprocal space refinement, monitoring progress continuously with superimposed Fourier and difference Fourier maps.
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High-resolution refinement of yeast iso-1-cytochrome c and comparisons with other eukaryotic cytochromes c
Gordon V. Louie,Gary D. Brayer +1 more
TL;DR: Comparison of the structure of yeast iso-1-cytochrome c with those of tuna and rice cytochromes c shows that these three molecules have very high structural similarity, with the atomic packing in the heme crevice region being particularly highly conserved.
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Oxidation state-dependent conformational changes in cytochrome c
TL;DR: High-resolution three-dimensional structural analyses of yeast iso-1-cytochrome c have now been completed in both oxidation states using isomorphous crystalline material and similar structure determination methodologies, showing that oxidation state-dependent changes are expressed for the most part in terms of adjustments to heme structure, movement of internally bound water molecules and segmental thermal parameter changes along the polypeptide chain.
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Resonance Raman Spectra of Hemoglobin and Cytochrome c: Inverse Polarization and Vibronic Scattering
TL;DR: The dependence of the resonance Raman spectra on the wavelength of the exciting radiation, as well as their polarization properties, demonstrates that the prominent bands correspond to vibronically active modes of the first electronic transition of the heme proteins, and provide confirmation of Albrecht's vibronic theory of Raman intensities.