Determination of Soluble and Membrane Protein Structure by Fourier Transform Infrared Spectroscopy

Goormaghtigh, Erik; Cabiaux, Véronique; Ruysschaert, Jean Marie

doi:10.1007/978-1-4615-1863-1_8

Cited by 397 publications

(452 citation statements)

References 106 publications

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“…Assignment of the IR band at 1620 cm À1 to n as CO 2 À seems obvious, but contrary to some reports [23,24,27,40], the peak cannot be attributed to n as CO 2 À solely, since a band at this position is also observed in the IR spectrum of the fully protonated form H 4 His 2+ at pH 0. A plausible explanation is, that n as CO 2 À coincides with d as NH 3 + , a vibration which is also expected to exhibit strong IR, but weak Raman activity around 1620 cm À1 . Comparison of the IR spectrum at pH 0 with those recorded at higher pH values reveals the appearance at pH 2 of a shoulder at the low frequency side of the 1620 cm À1 band that further increases in intensity with the pH.…”

Section: Resultsmentioning

confidence: 99%

“…The drop in the vibrational frequency can be explained by a further decrease of the bond C=C strength, while the increased symmetry of the imidizole ring explains the strong Raman activity. It should be noted, that the imidazole C=C vibration might exhibit some minor IR activity as well, but a contribution to the IR bands of n as CO 2 À and d as NH 3 + in the region 1620-1570 cm À1 is not observed.…”

Section: Imidazole C=c and C=n Vibrationsmentioning

confidence: 93%

“…Finally, IR and Raman are complementary techniques, which implies that an almost complete vibrational analysis is possible, particularly when combined with theoretical calculations. As a result, many vibrational spectroscopic studies on histidine and related imidazole-type compounds have been carried out, providing a considerable amount of data in the literature, occasionally summarized in reviews [2][3][4][5][6][7][8] and books [9,10]. To our knowledge, normal coordinate analysis (NCA) on histidine has not been carried out thus far and the first ab initio and density functional theory (DFT) study on the molecule was published only very recently [11].…”

Section: Introductionmentioning

confidence: 99%

“…The majority of this research has been focussed on IR or Raman bands that can be used as a marker to determine the state of protonation of the imidazole nitrogen atoms [15,16,[20][21][22][23][24][25][26][27] or the type of metal ion binding [24,29,32,34,37,39,40] and thus, measurements have been performed mainly at physiological conditions or at specific pH values close to the pK a values of the different active sites. Besides, samples have often been measured in D 2 O or after crystallization to circumvent interference from water bands. As a consequence, there are large gaps in the availability of experimental vibrational data and assignments in H 2 O, while an integrated IR and Raman study on aqueous solutions of histidine has to, our knowledge, not been published so far.…”

Section: Introductionmentioning

confidence: 99%

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Infrared and Raman spectroscopic study of pH-induced structural changes of l-histidine in aqueous environment

Mesu

Visser

Soulimani

et al. 2005

Vibrational Spectroscopy

131

102

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Aqueous solutions of L-histidine have been analysed in parallel by infrared (IR) and Raman spectroscopy over the pH range 0-14 with increments of one pH unit. The vibrational spectra in the region 2000-500 cm À1 have been interpreted and band positions have been assigned tentatively, taking into account assignments from literature after critical evaluation. As a result, a complete and complementary set of vibrational data has been obtained that can be used to determine all possible states of protonation of histidine, i.e. H 4 His 2+ , H 3 His + , H 2 His 0 , HHis À and His 2À . In addition, IR and Raman bands have been proposed as markers for the presence of the imidazole N p -or N t -protonated tautomeric forms of H 2 His 0 and HHis À .

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Section: Resultsmentioning

confidence: 99%

Section: Imidazole C=c and C=n Vibrationsmentioning

confidence: 93%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Infrared and Raman spectroscopic study of pH-induced structural changes of l-histidine in aqueous environment

Mesu

Visser

Soulimani

et al. 2005

Vibrational Spectroscopy

131

102

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“…The putative assignment of the pair of bands to -sheet structures is consistent with the observed band shape of the infrared spectrum (Figure 3). Other vibrational modes belonging to amino acid side-chain groups can also absorb in this region of the infrared spectrum (43). The 1515 and 1583 cm -1 bands were associated respectively with the ring stretching of Tyr residues and the vibrational stretching of carboxylate of either Asp or Glu residues (44).…”

Section: Resultsmentioning

confidence: 99%

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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Role of metal ions on the secondary and quaternary structure of alkaline phosphatase from bovine intestinal mucosa

1999

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Alkaline phosphatase (EC 3.1.3.1) from bovine intestinal mucosa (BIAP) is an homodimeric metalloenzyme, containing one Mg2+ and two Zn2+ ions in each active site. ApoBIAP, prepared using ion-chelating agents, exhibited a dramatic decrease of its hydrolase activity, concomittant to conformational changes in its quaternary structure. By rate-zonal centrifugation and electrophoresis, we demonstrated, for the first time, that the loss of divalent ions leads to some monomerization process for a metal-depleted alkaline phosphatase. Divalent ions are also involved in the secondary and tertiary structures. Metal-depletion induced more exposure of some Trp residues and hydrophobic regions to the solvent (as proved by intrinsic and ANS fluorescences). These changes might correspond to the disappearance of alpha-helices and/or turns with a concomittant appearance of unordered structures and beta-sheets (as probed by FTIR spectroscopy). For BIAP, three steps of temperature-induced changes were exhibited, while for apoBIAP, only one step was exhibited at 55 degrees C. Our work on BIAP showed two main differences with alkaline phosphatase from Escherichia coli. The loss of the divalent ions induces protein monomerization and the total recovery of enzyme activity by divalent ion addition to apoBIAP was not obtained.

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Determination of Soluble and Membrane Protein Structure by Fourier Transform Infrared Spectroscopy

Cited by 397 publications

References 106 publications

Infrared and Raman spectroscopic study of pH-induced structural changes of l-histidine in aqueous environment

Infrared and Raman spectroscopic study of pH-induced structural changes of l-histidine in aqueous environment

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

Role of metal ions on the secondary and quaternary structure of alkaline phosphatase from bovine intestinal mucosa

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