Interpretation of the doublet at 850 and 830 cm<sup>-1</sup> in the Raman spectra of tyrosyl residues in proteins and certain model compounds

Siamwiza, Mwindaace N.; Lord, R. C.; Chen, Michael C.; Takamatsu, Tadahisa; Harada, Issei; Matsuura, Hiroatsu; Shimanouchi, Takehiko

doi:10.1021/bi00693a014

Cited by 589 publications

(552 citation statements)

References 34 publications

(12 reference statements)

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“…Siamwiza et al (1975) have shown that this doublet is due to the Fermi resonance between the ring symmetric stretching vibration and the overtone of the C-C and C-O stretching vibrations. It is well-known that the Raman intensity ratio I 850 /I 830 is an indicator of the tyrosine environment (Siamwiza et al, 1975). For a high ratio (I 850 /I 830 ) 2.5), the hydroxyl group of the tyrosine acts like an acceptor of strong hydrogen bonds.…”

Section: Infraredmentioning

confidence: 97%

Determination of the Secondary Structure and Conformation of Puroindolines by Infrared and Raman Spectroscopy

Bihan

Désormeaux

et al. 1996

Biochemistry

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The conformation of puroindoline-a and -b, two basic lipid-binding proteins isolated from wheat seedlings, has been studied for the first time by infrared and Raman spectroscopy. The infrared results show that puroindoline-a and -b have similar secondary structure composed of approximately 30% R-helices, 30% -sheets, and 40% unordered structure at pH 7. The conformation of both puroindolines is significantly pH-dependent. The reduction of the disulfide bridges leads to a decrease of the solubility of puroindolines in water and to an increase of the -sheet content by about 15% at the expense of the R-helix content. Raman spectroscopy confirms the structure similarity between the two puroindolines with little differences in the side chains' environment. All the disulfide bridges are in a gauche-gauchegauche conformation, and the unique tyrosine residue present in both puroindolines is hydrogen-bonded to water. Raman spectra have been recorded in both H 2 O and D 2 O media, thus providing additional information concerning the accessibility of certain residues to water. We have also observed that puroindoline-a tends to form some aggregates under acidic and high ionic strength conditions. Nearultraviolet circular dichroism measurements suggest that the tryptophan-rich domain is involved in this aggregate formation. Finally, on the basis of a combined infrared and sequence conformational analysis, we propose a secondary structure assignment for both puroindolines. The results show that puroindolines exhibit a similar folding pattern with plant nonspecific lipid-transfer protein and some amylase-protease inhibitors. These proteins could form a homogeneous structural family of plant proteins involved in the defense against pathogens that are probably derived from a common "helicoidal" protein ancestor.

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Section: Infraredmentioning

confidence: 97%

Determination of the Secondary Structure and Conformation of Puroindolines by Infrared and Raman Spectroscopy

Bihan

Désormeaux

et al. 1996

Biochemistry

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“…23 Since this doublet has been observed for a large number of parasubstituted benzenes with C 2v local symmetry, we carefully analysed this region for the thyroid hormones, especially T2 and T4.…”

Section: Vibrational Assignmentmentioning

confidence: 99%

Comparative vibrational analysis of thyronine hormones using infrared and Raman spectroscopy and density functional theory calculations

Alvarez

Farı́as

Hildebrandt

2004

J Raman Spectroscopy

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The molecular structures of L-thyroxine (T4), 3,5,3 -triiodo-L-thyronine (T3) and 3,5-diiodo-L-thyronine (T2) were investigated by means of vibrational spectroscopy and density functional theory calculations using the B3LYP hybrid functional and the SDD effective core potential basis set, suitable for heavy atoms. The experimental data were obtained from FT-IR and Raman spectra of the thyroid hormones in the crystalline state. The combined experimental and theoretical approach allows a consistent assignment for most of the fundamental modes in the range between 100 and 1650 cm −1 . It was found that, in general, the modes are largely localized in the individual rings and in the linkage connecting both rings. Hence it was possible to identify bands that are dominated by the internal coordinates of the ether bridge and the C-I stretchings. These bands are considered to be sensitive spectral markers for monitoring conformational changes of the hormones after insertion into phospholipid bilayers.

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“…The Raman spectrum of native CK in buffer (10 mM Tris-HCl, pH 7.8, and 10 mM MgCl 2 ) is shown in Figure 1. Line fitting of the Tyr doublet at 852 and 828 cm -1 yields an intensity ratio (peak height) I(852)/I(828) of 1.25, suggesting that Tyr acts as weak H-bond donor/acceptor (34). The Raman spectra around 900 cm -1 show basically two bands at ca.…”

Section: Resultsmentioning

confidence: 98%

Magnesium−Adenosine Diphosphate Binding Sites in Wild-type Creatine Kinase and in Mutants: Role of Aromatic Residues Probed by Raman and Infrared Spectroscopies

Hagemann¹,

Marcillat²,

Buchet³

et al. 2000

Biochemistry

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Two distinct methods were used to investigate the role of Trp residues during Mg-ADP binding to cytosolic creatine kinase (CK) from rabbit muscle: (1) Raman spectroscopy, which is very sensitive to the environment of aromatic side-chain residues, and (2) reaction-induced infrared difference spectroscopy (RIDS) and photolabile substrate (ADP[Et(PhNO 2 )]), combined with site-directed mutagenesis on the four Trp residues of CK. Our Raman results indicated that the environment of Trp and of Tyr were not affected during Mg-ADP binding to CK. Analysis of RIDS of wild-type CK, inactive W227Y, and active W210,217,272Y mutants suggested that Trp227 was not involved in the stacking interactions. Results are consistent with Trp227 being essential to prevent water molecules from entering in the active site [as suggested by Gross, M., Furter-Graves, E. M., Wallimann, T., Eppenberger, H. M., and Furter, R. (1994) Protein Sci. 3, 1058-1068 and that another Trp could in addition help to steer the nucleotide in the binding site, although it is not essential for the activity of CK. Raman and infrared spectra indicated that Mg-ADP binding does not involve large secondary structure changes. Only 3-4 residues absorbing in the amide I region are directly implicated in the Mg-ADP binding (corresponding to secondary structure changes less than 1%), suggesting that movement of protein domains due to Mg-nucleotide binding do not promote large secondary structure changes.Creatine kinase (CK) 1 isoenzymes participate in the regulation of ATP supply during contraction of muscle or other high-energy metabolic process (1-3). The different localization of isoenzymes and substrates in the cells suggested distinct roles for the mitochondrial CK and the cytosolic CK (4). The mitochondrial CK, in the vicinity of ATP production site, converts creatine into phosphocreatine, while cytosolic CK (MM isoenzyme of creatine kinase), found in myofibrils, functions as a fast energy supplier by converting phosphocreatine and ADP into creatine and ATP. This regulation mechanism, the so-called creatine-phosphocreatine energy shuttle (4), explains that during muscle contraction, ATP levels are only minimally decreased while creatine phosphate is depleted. Despite their different functional roles in ATP regulation, octameric mitochondrial

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Interpretation of the doublet at 850 and 830 cm^-1 in the Raman spectra of tyrosyl residues in proteins and certain model compounds

Cited by 589 publications

References 34 publications

Determination of the Secondary Structure and Conformation of Puroindolines by Infrared and Raman Spectroscopy

Determination of the Secondary Structure and Conformation of Puroindolines by Infrared and Raman Spectroscopy

Comparative vibrational analysis of thyronine hormones using infrared and Raman spectroscopy and density functional theory calculations

Magnesium−Adenosine Diphosphate Binding Sites in Wild-type Creatine Kinase and in Mutants: Role of Aromatic Residues Probed by Raman and Infrared Spectroscopies

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Interpretation of the doublet at 850 and 830 cm-1 in the Raman spectra of tyrosyl residues in proteins and certain model compounds

Cited by 589 publications

References 34 publications

Determination of the Secondary Structure and Conformation of Puroindolines by Infrared and Raman Spectroscopy

Determination of the Secondary Structure and Conformation of Puroindolines by Infrared and Raman Spectroscopy

Comparative vibrational analysis of thyronine hormones using infrared and Raman spectroscopy and density functional theory calculations

Magnesium−Adenosine Diphosphate Binding Sites in Wild-type Creatine Kinase and in Mutants: Role of Aromatic Residues Probed by Raman and Infrared Spectroscopies

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Interpretation of the doublet at 850 and 830 cm^-1 in the Raman spectra of tyrosyl residues in proteins and certain model compounds