Hostname: page-component-586b7cd67f-rcrh6 Total loading time: 0 Render date: 2024-11-23T19:26:48.522Z Has data issue: false hasContentIssue false
  • English
  • Français

Resonance Raman spectroscopy in biochemistry and biology

Published online by Cambridge University Press:  17 March 2009

P. R. Carey
P. R. Carey
Affiliation:
Division of Biological Sciences National Research Council of Canada Ottawa, Canada KiA 0R6
Get access Rights & Permissions [Opens in a new window]

Extract

Resonance Raman (RR) spectroscopy provides detailed information on the vibrational and electronic properties of biochemical and biological chromophores. The analysis of RR spectra, using for example model compounds or a group frequency approach, enables us to form an accurate structural picture of the chromophore in its natural biological site. Moreover, the insight gained into the electronic states of a biological chromophore can be crucial to our understanding of its function. Thus the RR technique represents a powerful means of eliciting precise structural and electronic data from a coloured species and of focusing upon key aspects of its function. It has even been possible to obtain RR spectra from some natural chromophores in vivo, giving spectra detailed and informative enough to please a spectroscopist from a system complex enough to satisfy a biologist.

Type
Research Article
Information
Quarterly Reviews of Biophysics , Volume 11 , Issue 3 , August 1978 , pp. 309 - 370
Copyright
Copyright © Cambridge University Press 1978

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

REFERENCES

Abeles, R. H. & Dolphin, D. (1976). The vitamin B12 coenzyme. Acc. Chem. Res. 9, 114–120.CrossRefGoogle Scholar
Adar, F. (1977). Resonance Raman spectra of cytochromes c557 and c558. Archs Biochem. Biophys. 181, 5–7.CrossRefGoogle ScholarPubMed
Adar, F. & Ereni–ska, M. (1974). Resonance Raman spectra of the b- and c-type cytochromes of succinate-cytochrome reductase. Archs Biochem. Biophys. 165, 570–580.CrossRefGoogle Scholar
Adar, F., Gouterman, M. & Aronowitz, S. (1976). Fluorescence, resonance Raman, and radiationless decay in several hemoproteins J. phys. Chem. 80, 2184–2191.CrossRefGoogle Scholar
Aisen, P. The transferrins (siderophilins). In Inorganic Biochemistry, vol. I (ed. Eichhorn, G. L.), chap. 9. Amsterdam: Elsevier.Google Scholar
Asher, S. & Sauer, K. (1976). Resonance Raman spectroscopy of Mn(III) etioporphyrin I at the π→ π* and charge transfer bands: the use of charge transfer bands to monitor the complexation state of metalloporphyrins. J. Chem. Phys. 64, 4115–4125.CrossRefGoogle Scholar
Aton, B., Doukas, A. G., Callender, R. H., Becker, B. & (1977). Resonance Raman studies on the purple membrane. Biochemistry. N.Y. 16, 2995–2999.CrossRefGoogle ScholarPubMed
Aylward, & Koenig, J. L. (1970). Raman spectrum of poly (adenylic acid). Macromolecules 3, 590–596.CrossRefGoogle Scholar
Babior, B. M. (1975). Mechanism of cobalamin-dependent rearrangements. Acc. Chem. Res. 8, 376–384.CrossRefGoogle Scholar
Bagshaw, C. R., Eccleston, J. F., Trentham, D. R., Yates, D. W. & Goody, R. S. (1972). Transient kinetic studies of the Mg++-dependent ATPase of myosin and its proteolytic subfragments. Symposium on Quantitative Biology, vol. 37, Cold-Spring Harbor.Google Scholar
Barron, L. D. (1975). Magnetic vibrational optical activity in the resonance Raman spectrum of ferrocytochrome c. Nature. Lond. 257, 372–374.CrossRefGoogle ScholarPubMed
Barron, L. D. (1977). Magnetic resonance Raman optical activity of ferrocytochrome c at different laser wavelengths. Chem. Phys. Letters 46, 579–581.CrossRefGoogle Scholar
Barron, L. D. & Buckingham, A. D. (1975). Rayleigh and Raman optical activity. A. Rev. Phys. Chem. 26, 381–396.CrossRefGoogle Scholar
Blazej, D. C. & Peticolas, W. L. (1977). Ultraviolet resonant Raman spectroscopy of nucleic acid components. Proc. natn. Acad. Sci. U.S.A. 74, 2639–2643.CrossRefGoogle ScholarPubMed
Blum, H., Adar, F., Salerno, J. C. & Leigh, J. S. (1977). Exchange coupling in spinach ferredoxin determined by resonance Raman spectroscopy. Biochem. biophys. Res. Commun. 77, 650–657.CrossRefGoogle ScholarPubMed
Bosworth, Y. M., Clark, R. J. H. & Turtle, P. C. (1975). Resonance Raman excitation profiles of the tetraisothiocyanato-cobaltate(II) ion. J. C. S. Dalton, pp. 2027–2031.CrossRefGoogle Scholar
Bridoux, M., Chapput, A., Delhaye, M., Tourbez, H. & Wallart, F. (1974). Rapid and ultrarapid Raman spectroscopy. In Laser Raman Gas Diagnostics (ed. Lapp, M. and Penney, C. M.), pp. 249–258. New York: Plenum.CrossRefGoogle Scholar
Brown, K. G., Brown, E. B. & Person, W. B. (1977). Near-ultraviolet- excited Raman spectroscopy of lysozyme and the lysozyme-glucose complex. J. Am. chem. Soc. 99, 3128–3133.CrossRefGoogle ScholarPubMed
Brunner, H. (1974) Identification of the iron-ligand vibration of oxyhemoglobin. Naturwissenschaften 61, 129.CrossRefGoogle Scholar
Brunner, H., Mayer, A. & Sussner, H. (1972). Resonance Raman scattering on the haem group of oxy- and deoxyhaemoglobin. J. molec. Biol. 70, 153–156.CrossRefGoogle ScholarPubMed
Brunner, H. & Sussner, H. (1973). Resonance Raman scattering on haemoglobin. Biochim. biophys. Acta 310, 20–31.CrossRefGoogle ScholarPubMed
Callender, R. H., Doukas, A., Crouch, R. & Nakanishi, K. (1976). Molecular flow resonance Raman effect from retinal and rhodopsin. Biochemistry. N.Y. 15, 1621–1629.CrossRefGoogle ScholarPubMed
Callender, R. & Honig, B. (1977). Resonance Raman studies of visual pigments. A. Rev. Biophys. Bioeng. 6, 33–55.CrossRefGoogle ScholarPubMed
Campion, A., El-Sayed, M. A. & Terner, J. (1977 a). Resonance Raman kinetic spectroscopy of bacteriorhodopsin on the microsecond time scale. Biophys. J. 20, 369–375.CrossRefGoogle ScholarPubMed
Campion, A., Terner, J. & El-Sayed, M. A. (1977 b). Time-resolved resonance Raman spectroscopy of bacteriorhodopsin. Nature. Lond. 265, 659–661.CrossRefGoogle ScholarPubMed
Carey, P. R., Carriere, R. G., Lynn, K. R. & Schneider, H. (1976). Resonance Raman evidence for substrate reorganisation in the active site of papain. Biochemistry. N.Y. 15, 2387–2393.CrossRefGoogle Scholar
Carey, P. R., Carriere, R. G., Phelps, D. J. & Schneider, H. (1978). Charge effects in the active site of papain: resonance Raman and absorption evidence for electron polarisation occurring in the acyl group of some acyl papains. Biochemistry. N.Y. 17, 1081–1087.CrossRefGoogle Scholar
Carey, P. R., Froese, A. & Schneider, H. (1973). Resonance Raman spectroscopic studies of 2,4-dinitrophenyl hapten-antibody interactions. Biochemistry. N.Y. 12, 2198–2208.CrossRefGoogle ScholarPubMed
Carey, P. R. & Schneider, H. (1974). Resonance Raman spectra of chymotrypsin acyl enzymes. Biochem. biophys. Res. Commun. 57, 831–837.CrossRefGoogle ScholarPubMed
Carey, P. R. & Schneider, H. (1976). Evidence for a structural change in the substrate preceding hydrolysis of a chymotrypsin acyl enzyme: application of the resonance Raman labelling technique to a dynamic biochemical system. J. molec. Biol. 102, 679–693.CrossRefGoogle ScholarPubMed
Carey, P. R. & Schneider, H. (1978). Resonance Raman labels: a sub- molecular probe for interactions in biochemical and biological systems. Acc. Chem. Res. 11, 122–128.CrossRefGoogle Scholar
Carey, P. R., Schneider, H. & Bernstein, H. J. (1972). Raman spectroscopic studies of ligand-protein interactions: the binding of methyl orange by bovine serum albumin. Biochem. biophys. Res. Commun. 47, 588–595.CrossRefGoogle ScholarPubMed
Carey, P. R. & Young, N. M. (1974). The resonance Raman spectrum of the metalloprotein ovotransferrin. Can. J. Biochem. 52, 273–280.CrossRefGoogle ScholarPubMed
Carriera, L. A., Maguire, T. C. & Malloy, T. B. (1977). Excitation profiles of the coherent anti-Stokes resonance Raman spectrum of βcarotene. J. chem. Phys. 68, 2621–2626.CrossRefGoogle Scholar
Champion, P. M., Collins, D. W. & Fitchen, D. B. (1976a). Resonance Raman spectra of heme proteins at low temperature. J. Am. chem. Soc. 98, 7114–7115.CrossRefGoogle ScholarPubMed
Champion, P. M. & Gunsalus, I. C. (1977). Resonance Raman spectra of cytochrome P450cam. J. Am. chem. Soc. 99, 2000–2002.CrossRefGoogle ScholarPubMed
Champion, P. M., Rembra, R. D., Chiang, R. V., Fitchen, D. B. & Hager, L. P. (1976b). Resonance Raman spectra of chloroperoxidase. Biochim. biophys. Acta 446, 486–492.CrossRefGoogle ScholarPubMed
Chen, J., Li, T.-Y., McFarland, J. T., Petersen, R. L. & Watters, K. L. (1976). The use of resonance Raman spectroscopy to identify enzyme modification sites. Proceedings of the Fifth International Conference on Raman spectroscopy, pp. 206–207. Freiburg: Schulz Verlag.Google Scholar
Chinsky, L., Turpin, P. Y., Duquesne, M. & Brahms, J. (1975). Resonance Raman study of actinomycin D interaction with DNA and its models. Biochem. biophys. Res. Commun. 65, 1440–1446.CrossRefGoogle ScholarPubMed
Chinsky, L., Turpin, P. Y., Duquesne, M. & Brahms, J. (1977). Structural investigation of poly d(BrU-A) by ultraviolet resonance Raman spectroscopy. Biochem. biophys. Res. Commun. 75, 766–771.CrossRefGoogle Scholar
Chottard, G. & Bolard, J. (1976). Raman resonant effect on a cobalt histidine complex, a model of a metalloprotein. Inorganica Chimica Acta 20, L17–L19.CrossRefGoogle Scholar
Chottard, G. & Mansuy, D. (1977). Resonance Raman studies of hemoglobin complexes with nitric oxide, nitrosobenzene and nitrosomethane: observation of the metal-ligand vibrations. Biochem. biophys. Res. Commun. 77, 1333–1338.CrossRefGoogle ScholarPubMed
Colman, P. M., Freeman, H. C., Guss, J. M., Murata, M., Norris, V. A., Ramshaw, J. A. M. & Venkatappa, M. P. (1978). The X-ray crystal structure of plastocyanin, a ‘blue’ copper-protein, at 2·7 Å resolution. Nature. Lond. 272, 319–324.CrossRefGoogle Scholar
Cookingham, R. E., Lewis, A., Collins, D. W. & Marcus, M. A. (1976). Preresonance Raman spectra of crystals of retinal isomers. J. Am. chem. Soc. 98, 2759–2763.CrossRefGoogle ScholarPubMed
Delhaye, M. (1976). Pulsed lasers and imaging techniques in Raman spectroscopy. In Proceedings of the Fifth International Conference on Raman spectroscopy (ed. Schmid, E. D.). Freiburg-im-Breisgau: H. F. Schulz Verlag.Google Scholar
Delhaye, M. & Dhamelincourt, P. (1975). Raman microprobe and microscope with laser excitation. J. Raman Spectrosc. 3, 33–43.CrossRefGoogle Scholar
Douzou, P. (1977). Cryobiochemistry: an Introduction. London: Academic Press.Google Scholar
Dunn, J. B. R., Addison, A. W., Bruce, R. E., Loehr, J. S. & Loehr, T. M. (1977). Comparison of hemerythrins from four species of sipunculids by optical absorption, circular dichroism, fluorescence emission, and resonance Raman spectroscopy. Biochemistry. N.Y. 16, 1743–1749.CrossRefGoogle ScholarPubMed
Dunn, J. B. R., Shriver, D. F. & Klotz, I. M. (1973). Resonance Raman studies of the electronic state of oxygen in hemerythrin. Proc. natn. Acad. Sci. U.S.A. 70, 2582–2584.CrossRefGoogle ScholarPubMed
Dunn, J. B. R., Shriver, D. F. & Klotz, I. M. (1975). Resonance Raman studies of hemerythrin-ligand complexes. Biochemistry. N.Y. 14, 2689–2695.CrossRefGoogle ScholarPubMed
Dupaix, A., Bechet, J.-J., Yon, J., Merlin, J.-C., Delhaye, M. & Hill, M. (1975). Resonance Raman spectroscopic studies of the interaction between trypsin and a competitive inhibitor. Proc. natn. Acad. Sci. U.S.A. 72, 4223–4227.CrossRefGoogle Scholar
Dutta, P. K., Nestor, J. R. & Spiro, T. G. (1977). Resonance coherent anti-Stokes Raman scattering spectra of fluorescent biological chromophores: vibrational evidence for hydrogen bonding of flavin to glucose oxidase and for rapid solvent exchange. Proc. natn. Acad. Sri. U.S.A. 74, 4146–4149.CrossRefGoogle ScholarPubMed
Dwek, R. A., Wain-Hobson, S., Dower, S., Gettins, P., Sutton, B., Perkins, S. J. & Givol, D. (1977). Structure of an antibody combining site by magnetic resonance. Nature. Lond. 266, 31–37.CrossRefGoogle ScholarPubMed
Ebrey, T. G. & Honig, B. (1975). Molecular aspects of photoreceptor function. Q. Rev. Biophys. 8, 129–184.CrossRefGoogle ScholarPubMed
Euler, H. V. & Hellstrom, H. (1932). Raman-spektren von carotinoiden. Z. phys. Chem. 15 B, 342–346.CrossRefGoogle Scholar
Fabian, H., Lau, A., Werncke, W. & Lenz, K. (1977). Fast Raman spectro scopy of cytochrome c using intracavity resonance Raman amplification. Chem. Phys. Letters 48, 607–610.CrossRefGoogle Scholar
Fawcett, V. & Long, D. A. (1976). Biological applications of Raman spectroscopy. In Molecular Spectroscopy, vol. 4, chap. 4 (ed. Barrow, R. V., Lond, D. A. and Millen, D. J.) (Specialist Periodical Reports). London: The Chemical Society.Google Scholar
Felton, R. H., Romans, A. Y., Yu, N.-T. & Schonbaum, G. R. (1976). Laser Raman spectra of oxidised hydroperoxidases. Biochim. biophys. Acta 434, 82–89.CrossRefGoogle ScholarPubMed
Fenna, R. E., TenEyck, L. F. & Matthews, B. W. (1977). Atomic coordinates for the chlorophyll core of a bacteriochlorophyll a-protein from green photosynthetic bacteria. Biochem. biophys. Res. Commun. 75, 751–756.CrossRefGoogle Scholar
Freedman, T. B., Loehr, J. S. & Loehr, T. M. (1976). A resonance Raman study of a copper protein, hemocyanin. New evidence for the structure of the oxygen binding-site. J. Am. chem. Soc. 96, 2809–2815.CrossRefGoogle Scholar
Friedman, J. M., RoussEau, D. L. & Adar, F. (1977). Excited state lifetimes in cytochromes measured from Raman scattering data: evidence for iron-porphyrin interactions. Proc. natn. Acad. Sci. U.S.A. 74, 2607–2611.CrossRefGoogle ScholarPubMed
Funfschilling, J. & Williams, D. F. (1976). CW laser wavelength modulation in Raman and site selection fluorescence spectroscopy. Appl. Spectrosc. 30, 443–446.CrossRefGoogle Scholar
Gaber, B. P., Miskowski, V. & Spiro, T. G. (1974). Resonance Raman scattering from iron(III)- and copper(II)-transferrin and an iron(III) model compound. A spectroscopic interpretation of the transferrin binding site. J. Am. chem. Soc. 96, 6868–6873.CrossRefGoogle Scholar
Galluzzi, F., Gozzo, M. & Ricci, F. F. (1974). Resonance Raman scattering and vibronic coupling in aquo- and cyano-cobalamin. J. Raman Spectrosc. 2, 351–362.CrossRefGoogle Scholar
George, W. O. & Mendelsohn, R. (1973). Resonance RamarL spectrum of cyanocobalamin (vitamin B12). Appl. Spectrosc. 27, 390–391.CrossRefGoogle Scholar
Ghiretti, F. (ed.) (1968). Physiology and Biochemistry of Haemocyanins. New York:Academic Press.Google Scholar
Gill, D., Heyde, M. E. & Rimai, L. (1971). Raman spectrum of the II-cis isomer of retinaldehyde. J. Am. chem. Soc. 93, 6288–6289.CrossRefGoogle Scholar
Gill, D., Kilponen, R. G. & Rimai, L. (1970). Resonance Rarnan scattering of laser radiation by vibrational modes of carotenoid pigment molecules in intact plant tissues. Nature. Lond. 227, 743–744.CrossRefGoogle Scholar
Gutfreund, H. (ed.) (1976). Enzymes: one hundred years. FEBS Lett. 62, E1–E95.Google Scholar
Hacker, H. H. (1968). Ph.D. dissertation, University of Munich.Google Scholar
Harada, I., Sugawara, Y., Matsuura, H. & Shimanouchi, T. (1975). Preresonance Raman spectra of simple amides using ultraviolet lasers. J. Raman Spectrosc. 4, 91–98.CrossRefGoogle Scholar
Haselkorn, D., Friedman, S., Givol, D. & Pecht, I. (1974). Kinetic mapping of the antibody combining site by chemical relaxation spectrometry. Biochemistry, N.Y. 13, 2210–2222.CrossRefGoogle ScholarPubMed
Henderson, R. (1977). The purple membrane from Halobacterium halobium. A. Rev. Biophys. Bioeng. 6, 87–109.CrossRefGoogle ScholarPubMed
Heyde, M. E., Gill, D., Kilponen, R. G. & Rimai, L. (1971). Raman spectra of Schiff bases of retinal (models of visual photoreceptors). J. Am. chem. Soc. 93, 6776–6780.CrossRefGoogle ScholarPubMed
Hillig, K. W. & Morris, M. D. (1976). Pre-resonance Raman spectra of adriamycin. Biochem. biophys. Res. Commun. 71, 1228–1233.CrossRefGoogle ScholarPubMed
Holm, R. H. (1977). Synthetic approaches to the active sites of iron-sulfur proteins. Acc. Chem. Res. 10, 427–434.CrossRefGoogle Scholar
Hoskins, L. C. & Alexander, V. (1977). Determination of carotenoid concentrations in marine phytoplankton by resonance Raman spectroscopy. Analyt. Chem. 49, 695–697.CrossRefGoogle Scholar
Inagaki, F., Tasumi, M. & Miyazawa, T. (1974). Excitation profile of the resonance Raman effect of β-carotene. J. molec. Spectrosc. 50, 286–303.CrossRefGoogle Scholar
Inagaki, F., Tasumi, M. & Miyazawa, T. (1975). Vibrational analysis of polyene chains. J. Raman Spectrosc. 3, 335–343.CrossRefGoogle Scholar
Isler, O. (ed.) (1971). Carotenoids. Basel: Birkhäuser Verlag.CrossRefGoogle Scholar
Jencks, W. P. (1975). Binding energy, specificity, and enzymic catalysis: the circe effect. Advances in Enzymology (ed. Meister, A.), 43, 219–410.Google ScholarPubMed
Johansen, J. T., Klyosov, A. A. & Vallee, B. L. (1976). Circular dichroisminhibitor titrations of arsanilazotyrosine-248 carboxypeptidase A. Biochemistry, N.Y. 15, 296–303 and references therein.CrossRefGoogle ScholarPubMed
Johnson, B. D. & Peticolas, W. L. ( 1976). The resonant Raman effect. A. Rev. phys. Chem. 27, 465–491.CrossRefGoogle Scholar
Jones, T. E., Rorabacher, D. B. & Ochrymowycz, L. A. (1975). Simple models for ‘blue’ copper proteins. The copper-thiaether complex. J. Am. chem. Soc. 97, 7485–7486.CrossRefGoogle Scholar
Katz, J. J. (1973). Chlorophyll. In Inorganic Biochemistry, vol. 2 (ed. Eichhorn, G. L), pp. 1022–1066. Amsterdam: Elsevier.Google Scholar
Kim, B.-K., Kagayama, A., Saito, Y., Machida, K. & Uno, T. (1975). Resonance Raman spectra of methyl orange bound to proteins and cationic surfactants. Bull. chem. Soc. Japan 48, 1394–1396.CrossRefGoogle Scholar
King, R. W. & Burgen, A. S. V. (1976). Kinetic aspects of structure- activity relations: the binding of sulphonamides by carbonic anhydrase. Proc. R. Soc. Lond. B 193, 107–125.Google ScholarPubMed
Kitagawa, T., Abe, M., Kyogoku, Y., Ogoshi, H., Watanabe, E. & Yoshida, Z. (1976 a). Resonance Raman spectra of metallooctaethylporphyrins. Low frequency vibrations of porphyrin and iron-axial ligand stretching modes. J. phys. Chem. 80, 1181–1186.CrossRefGoogle Scholar
Kitagawa, T., Kyogoku, Y., Iizuka, T. & Saito, M. I. (1976b). Nature of the iron-ligand bond in ferrous low spin hemoproteins studied by resonance Raman scattering. J. Am. chem. Soc. 98, 5169–5173.CrossRefGoogle ScholarPubMed
Kitagawa, T., Ozaki, Y., Kyogoku, Y. & Horio, T. (1977a). Resonance Raman study of the pH-dependent and detergent-induced structural alterations in the heme moiety of Rhodospirillum rubrum cytochrome c'. Biochim. biophys. Acta 495, 1–11.CrossRefGoogle ScholarPubMed
Kitagawa, T., Ozaki, Y., Teraoka, J., Kyogoku, Y. & Yamanaka, T. (1977b). The pH dependence of the resonance Raman spectra and structural alterations at heme moieties of various c-type cytochromes. Biochim. biophys. Acta 494, 100–114.CrossRefGoogle Scholar
Klotz, I. M., Klippenstein, G. L. & Hendrickson, W. A. (1976). Hemerythrin: alternative oxygen carrier. Science, N.Y. 192, 335–344.Google Scholar
Krinsky, N. I. (1971). Function. In Carotenoids (ed. Isler, O.), pp. 669–716. Basel: Birkhäuser Verlag.CrossRefGoogle Scholar
Kumar, K. & Carey, P. R. (1975). Resonance Raman spectra and structure of some complex nitroaromatic molecules. J. chem. Phys. 63, 3697–3707.CrossRefGoogle Scholar
Kumar, K. & Carey, P. R. (1977). The resonance Raman spectra and excitation profiles of some 4-sulfamylazObenzenes. Can. J. Chem. 55, 1444–1453.CrossRefGoogle Scholar
Kumar, K., King, R. W. & Carey, P. R. (1974). Carbonic-anhydrase sulfonamide complexes, a resonance Raman study. FEBS Lett. 48, 283–287.CrossRefGoogle ScholarPubMed
Kumar, K., King, R. W. & Carey, P. R. (1976). Resonance Raman studies on some carbonic anhydrase-aromatic sufonamide complexes. Biochemistry, N.Y. 15, 2195–2202.CrossRefGoogle Scholar
Kumar, K., Phelps, D. J. & Carey, P. R. (1978 a). Resonance Raman labels: spectroscopic studies on cis and trans 4-benzylidene-2-phenyl- δ2-oxazolin-5-one and an isotopically substituted analog. Can. J. Chern. 56, 232–239.CrossRefGoogle Scholar
Kumar, K., Phelps, D. J., Carey, P. R. & Young, N. M. (1978b). Resonance Raman studies of the hapten features involved in the binding of 2,4- dinitrophenyl haptens by the murine myeloma proteins, MOPC 315 and MOPC 460. Biochem. J. in Press.CrossRefGoogle Scholar
Kurtz, D. M., Shriver, D. F. & Klotz, I. M. (1976). Resonance Raman spectroscopy with unsymmetrically isotopic ligands. Differentiation of possible structures of hemerythrin complexes. J. Am. chem. Soc. 98, 5033–5035.CrossRefGoogle ScholarPubMed
Larrabee, J. A., Spiro, T. G., Ferris, N. S., Woodruff, W. H., Maltese, W. A. & Kerr, M. S. (1977). Resonance Raman study of mollusc and arthropod hemocyanins using ultravolet excitation: copper environment and subunit inhomogeneity. J. Am. chem. Soc. 99, 1979–1980.CrossRefGoogle Scholar
Larsson, K. & Fjellgren, L. (1977). A study of the combined Raman and fluorescence scattering from human blood plasma. Experientia 30, 481–483.CrossRefGoogle Scholar
Leinhard, G. E. (1973). Enzyme catalysis and transition-state theory. Science, N.Y. 80, 149–154.Google Scholar
Lewis, A., Fager, R. S. & Abrahamson, E. W. (1973). Tunable laser resonance Raman spectroscopy of the visual process I: the spectrum of rhodopsin. J. Raman Spectrosc. I, 465–470.CrossRefGoogle Scholar
Lewis, A., Spoonhower, J., Bogomolni, R. A., Lozier, R. H. & Stoec-Kenius, W. (1974). Tunable laser resonance Raman spectroscopy of bacteriorhodopsin. Proc. natn. Acad. Sci. U.S.A. 71, 4462–4466.CrossRefGoogle ScholarPubMed
Loehr, J. S., Freedman, T. B. & Loehr, T. M. (1974). Oxygen binding to hemocyanin: a resonance Raman spectroscopic study. Biochem. biophys. Res. Commun. 56, 510–515.CrossRefGoogle ScholarPubMed
Long, T. V. & Loehr, T. M. (1970). The possible determination of iron coordination in nonheme iron proteins using laser-Raman spectroscopy. Rubredoxin. J. Am. chem. Soc. 92, 6384–6386.CrossRefGoogle ScholarPubMed
Long, T. V., Loehr, T. M., Allkins, J. R. & Lovenberg, W. (1971). Determination of iron coordination in nonheme iron proteins using laserRaman spectroscopy. II. Clostridium pasteurianium rubredoxin in aqueous solution. J. Am. chem. Soc. 93, 1809–1811.CrossRefGoogle Scholar
Lontie, R. & Witters, R. (1973). Hemocyanin. In Inorganic Biochemistry vol. III, chap. 12 (ed. Eichhorn, G. L.). Amsterdam: Elsevier.Google Scholar
Lovenberg, W. (ed.), (1973), (1977). Iron-sulfur Proteins, vol. I and II, 1973, vol. III, 1977. New York: Academic Press.Google Scholar
Lutz, M. (1972). Spectroscopie Raman de résonance de pigments végéteaux en solution et inclus dans des lamelles chioroplastiques. C. r. hebd. Séanc. Acad. Sci. Paris B 275, 497–500.Google Scholar
Lutz, M. (1974). Resonance Raman spectra of chlorophyll in solution. J. Raman Spectrosc. 2, 497–516.CrossRefGoogle Scholar
Lutz, M. (1977). Antenna chlorophyll in photosynthetic membranes a study by resonance Raman spectroscopy. Biochim. biophys. Acta 460, 408–430.CrossRefGoogle ScholarPubMed
Lutz, M. & Breton, J. (1973). Chlorophyll association in the chloroplast: resonance Raman spectroscopy. Biochem. biophys. Res. Commun. 53, 413–418.CrossRefGoogle ScholarPubMed
Lutz, M. & Kleo, J. (1976). Diffusion Raman de résonance de la chlorophylle d. C. r. hebd. Séanc. Acad. Sci. Paris D 279, 1413–1416.Google Scholar
Lutz, M. & Kleo, J. (1976). Resonance Raman scattering of bacteriochlorophyll, bacteriopheophytin and spheroidene in reaction centers of Rhodoseudomonas spheroides. Biochem. biophys. Res. Commun. 69, 711–717.CrossRefGoogle Scholar
Makinen, M. W. & Fink, A. L. (1977). Reactivity and cyroenzymology of enzymes in the crystalline state. A. Rev. Biophys. Bioeng. 6, 301–343.CrossRefGoogle ScholarPubMed
Malkin, R. (1973). The copper-containing oxidases. In Inorganic Biochemistry, vol. II, chap. 21 (ed. Eichhorn, G. L.). Amsterdam: Elsevier.Google Scholar
Mann, T. & keilin, D. (1940). Suiphanilamide as a specific inhibitor of carbonic anhydrase. Nature. Lond. 146, 164–165.CrossRefGoogle Scholar
Marcus, M. A. & Lewis, A. (1977). Kinetic resonance Raman spectroscopy: dynamics of deprotonation of the Schiff base of bacteriorhodopsin. Science, N.Y. 195, 1328–1330.CrossRefGoogle ScholarPubMed
Markley, J. L., Ulrich, E. L. & Krogmann, D. W. (1977). Spinach plastocyanin: comparison of reduced and oxidised forms by natural abundance carbon-i 3 nuclear magnetic resonance spectroscopy. Biochem. biophys. Res. Commun. 78, 106–114.CrossRefGoogle Scholar
Mathies, R., Freedman, T. B. & Stryer, L. (1977). Resonance Raman studies of the conformation of retinal in rhodopsin and isorhodopsin. J. molec. Biol. 109, 367–372.CrossRefGoogle ScholarPubMed
Mathies, R., Oseroff, A. R. & Stryer, L. (1976). Rapid-flow resonance Raman spectroscopy of photolabile molecules: rhodopsin and isorhodopsin. Proc. natn. Acad. Sci. U.S.A. 73, 1–5.CrossRefGoogle ScholarPubMed
Mayer, E., Gardiner, D. J. & Hester, R. E. (1973 a). Resonance Raman spectra of vitamin B12, and dicyanocobalamin. Biochim. biophys. Acta 297, 568–570.CrossRefGoogle ScholarPubMed
Mayer, E., Gardiner, D. J. & Hester, R. E. (1973 b). The selective enhancement of band intensities in resonance Raman spectra of cobalt corrinoids. Molec. Phys. 26, 783–787.CrossRefGoogle Scholar
Mayer, E., Gaiuiner, D. J. & Hester, R. E. (1973 c). Resonance Raman spectra of vitamin B12, and some cobalt corrinoid derivatives. J. Chem. Soc. Faraday Trans. II, 1350–1358.CrossRefGoogle Scholar
McFarland, J. T., Watrers, K. L. & Peteasen, R. L. (1975). Resonance Raman investigation of an enzyme-inhibitor complex. Biochemistry, N.Y. 14, 624–630.CrossRefGoogle ScholarPubMed
Mendelsohn, R. (1976). Thermal denaturation and photochemistry of bacteriorhodopsin from Halobacterium cutirubrum as monitored by resonance Raman spectroscopy. Biochim. biophys. Acta 427, 295–301.CrossRefGoogle ScholarPubMed
Miskowski, V., Tang, S.-P. W., Spiro, T. G., Sipiro, E. & Moss, T. H. (1975). The copper coordination group in ‘blue’ copper proteins: evidence from resonance Raman spectra. Biochemistry, N. Y. 14, 1244–1250.CrossRefGoogle ScholarPubMed
Nestor, J., Spiro, T. G. & Klauminzer, G. (1976). Coherent anti-Stokes Raman scattering (CARS) spectra, with resonance enhancement, of cytochrome c and vitamin B12, in dilute aqueous solution. Proc. natn. Acad. Sci. U.S.A. 73, 3329–3332.CrossRefGoogle ScholarPubMed
Nishimura, Y., Hirakawa, A. Y., Tsuboj, M. & Nishimura, S. (1976). Raman spectra of transfer RNAs with ultraviolet lasers. Nature Lond. 260, 173–174.CrossRefGoogle ScholarPubMed
Oesterhelt, D. & Stoeckenius, W. (1971). Rhodopsin-like protein from the purple membrane of Halobacterium halobium. Nature (New Biology). Lond. 233, 149–152.CrossRefGoogle ScholarPubMed
Okamura, M. Y. & Klotz, I. M. (1973). Hemerythrin. In Inorganic Biochemistry, vol. I, chap. II (ed. Eichhorn, G. L.). Amsterdam: Elsevier.Google Scholar
Orme-Johnson, W. H. (1973). Iron-sulfur proteins: structure and function. A. Rev. Biochem. 42, 159–204.CrossRefGoogle ScholarPubMed
Oseroff, A. R. & Callender, R. H. (1974). Resonance Raman spectroscopy of rhodopsin in retinal disk membranes. Biochemistry, N.Y. 13, 4243–4248.CrossRefGoogle ScholarPubMed
Ozaki, Y., Kitagawa, T. & Kyogoku, Y. (1976a). Raman study of the acid- base transition of ferric myoglobin; direct evidence for the existence of two molecular species at alkaline pH. FEBS Lett. 62, 369–372.CrossRefGoogle ScholarPubMed
Ozaki, Y., Kitagawa, T., Kyogoku, Y., Shimada, H., Iizuka, T. & Ishimur, Y. (1976b). An anomaly in the resonance Raman spectra of cytochrome P45ocam in the ferrous high-spin state. J. Biochem. 80, 1447–1451.CrossRefGoogle ScholarPubMed
Penner, A. P. & Siebrand, W. (1976). Effect of line broadening mechanisms on resonance Raman excitation profiles: a possible method for measuring short lifetimes. Chem. Phys. Letters 39, 11–13.CrossRefGoogle Scholar
Petersen, R. L, Li, T.-Y., McFarland, J. T. & Watters, K. L. (1977). Determination of ionization state by resonance Raman spectroscopy. Sulfonamide binding to carbonic anhydrase. Biochemistry, N.Y. 16, 726–731.CrossRefGoogle ScholarPubMed
Pézolet, M., Yu, T.-J. & Peticolas, W. L. (1975). Resonance and preresonance Raman spectra of nucleotides using ultraviolet lasers. J. Raman Spectrosc. 3, 55–64.CrossRefGoogle Scholar
Phelps, D. J., Carriere, R. G., Kumar, K. & Carey, P. R. (1978). Preresonance Raman spectra and excitation profiles of some chemically and isotopically substituted trans 4-benzyhdene-oxazolin-5-ones. Can. J. Chem. 56, 240–245.CrossRefGoogle Scholar
Placzek, G. (1934) The Rayleigh and Raman Scattering. UCRL-Translation-526L: from Handbuch der Radiologie (ed. Marx, E.), vol. VI (2), Leipzig: Akamedische Verlagsgesellschaft.Google Scholar
Rakhit, G., Spiro, T. G. & Uyeda, M. (1976). Resonance Raman evidence for Fe(IV) in compound II of horseradish peroxidase. Biochem. biophys. Res. Commun. 71, 803–808.CrossRefGoogle ScholarPubMed
Rein, A. J., Saperstein, D. D., Pines, S. H. & Radlick, P. C. (1976). Blood plasma investigations by resonance Raman spectroscopy: detection of carotenoid pigments. Experientia 32, 1352–1354.CrossRefGoogle ScholarPubMed
Rimai, L., Gill, D. & Parsons, J. L. (1971). Raman spectra of dilute solutions of some stereoisomers of vitamin A type molecules. J. Am. chem. Soc. 93, 1353–1357.CrossRefGoogle Scholar
Rimai, L., Heyde, M. E. & Gill, D. (1973). Vibrational spectra of some carotenoids and related linear polyenes. A Raman spectroscopic study. J. Am. chem. Soc. 95, 4493–4501.CrossRefGoogle ScholarPubMed
Rimai, L., Kilponen, R. G. & Gill, D. (1970a). Excitation profiles of laser Raman spectra in the resonance region of two carotenoid pigments in solution. J. Am. chein. Soc. 92, 3824–3825.CrossRefGoogle Scholar
Rimai, L., Kilponen, R. G. & Gill, D. (1970b). Resonance-enhanced Raman spectra of visual pigments in intact bovine retinas at low temperatures. Biochem. biophys. Res. Commun. 41, 492–497.CrossRefGoogle ScholarPubMed
Salama, S. & Spiro, T. G. (1977). Visible and near-ultraviolet resonance Raman spectra of photolabile vitamin B12 derivatives with a rapid-flow technique. J. Raman Spectrosc. 6, 57–60.CrossRefGoogle Scholar
Salares, V. R., Mendelsohn, R., Carey, P. R. & Bernstein, H. J. (1976). Correlation between the absorption spectra and resonance Raman excitation profiles of astaxanthin. J. phys. Chein. 80, 1137–1141.Google Scholar
Salares, V. R., Young, N. M., Bernstein, H. J. & Carey, P. R. (1977a). Resonance Raman spectra of lobster shell carotenoproteins and a model astaxanthin aggregate. A possible photobiological function for the yellow protein. Biochemistry, N.Y. 16, 4751–4756.CrossRefGoogle Scholar
Salares, V. R., Young, N. M., Carey, P. R. & Bernstein, H. J. (1977b). Excited state (exciton) interactions in polyene aggregates. Resonance Raman and absorption spectroscopic evidence. J. Raman Spectrosc. 6, 282–288.CrossRefGoogle Scholar
Salmeen, I., Rimai, L., Gill, D., Yamamoto, T., Palmer, G., Hartzell, C. R. & Beinert, H. (1973). Resonance Raman spectroscopy of cytochrome c oxidase and electron transport particles with excitation near the Soret band. Biochem. biophys. Res. Commun. 52, 1100–1107.CrossRefGoogle ScholarPubMed
Sauer, K. (1975). Primary events and the trapping of energy. In Bioenergetics of Photosynthesis (ed. Govindjee, ), pp. 115–181. New York: Academic Press.CrossRefGoogle Scholar
Scheule, R. K., Van Wart, H. E., Vallee, B. L. & Scheraga, H. A. (1977). Resonance Raman spectroscopy of arsanilazocarboxypeptidase A: determination of the nature of the azotyrosyl-248 zinc complex. Proc. natn. Acad. Sci. U.S.A. 74, 3273–3277.CrossRefGoogle ScholarPubMed
Scholler, D. M., Hoffman, B. M. & Shriver, D. F. (1976). Resonance Raman spectra of liganded and unliganded carp hemoglobin in both R and T states. J. Am. chem. Soc. 98, 7866–7868.CrossRefGoogle Scholar
Siiman, O., Young, N. M. & Carey, P. R. (1974). Resonance Raman studies of blue’ copper proteins. J. Am. chem. Soc. 96, 5583–5585.CrossRefGoogle ScholarPubMed
Siiman, O., Young, N. M. & Carey, P. R. (1976). Resonance Raman spectra of ‘blue’ copper proteins and the nature of their copper sites. J. Am. chem. Soc. 98, 744–748.CrossRefGoogle ScholarPubMed
Solomon, E. I., Hare, J. W. & Gray, H. B. (1976). Spectroscopic studies and structural model for blue copper centers in proteins. Proc. natn. Acad. Sci. U.S.A. 73, 1389–1393.CrossRefGoogle ScholarPubMed
Spiro, T. G. (1974). Resonance Raman spectroscopy: a new structure probe for biological chromophores. Acc. Chem. Res. 7, 339–344.CrossRefGoogle Scholar
Spiro, T. G. (1975 a). Biological applications of resonance Rainan spectroscopy: haem proteins. Proc. R. Soc. Lond. A 345, 89–105.Google Scholar
Spiro, T. G. (1975 b). Resonance Raman spectroscopic studies of heme proteins. Biochim. biophys. Acta 416, 169–189.CrossRefGoogle ScholarPubMed
Spiro, T. G. & Burke, J. M. (1976). Protein control of porphyrin conformation. Comparison of resonance Raman spectra of heme proteins with mesoporphyrin IX analogues. J. Am. chem. Soc. 98, 5482–5489.CrossRefGoogle ScholarPubMed
Spiro, T. G. & Loehr, T. M. (1975). Resonance Raman spectra of heme proteins and other biological systems. In Advances in infrared and Raman Spectroscopy, vol. I, chap. 3 (ed. Clark, R. J. H. and Hester, R. E.). London: Heyden.Google Scholar
Spiro, T. G. & Stein, P. (1977). Resonance effects in vibrational scattering from complex molecules. Ann. Rev. Phys. Chem. 28, 501–521.CrossRefGoogle Scholar
Spiro, T. G. & Streis, T. C. (1972). Resonance Raman spectra of hemoglobin and cytochrome c: inverse polarization and vibronic scattering. Proc. natn. Acad. Sci. U.S.A. 69, 2622–2626.CrossRefGoogle ScholarPubMed
Stein, P., Burke, J. M. & Spiro, T. G. (1975). Structural interpretation of heme protein resonance Raman frequencies. Preliminary normal coordinate analysis results. J. Am. chem. Soc. 97, 2304–2305.CrossRefGoogle ScholarPubMed
Stenkamp, R. E., Sieker, L. C. & Jensen, L. H. (1976). Structure of the iron complex in methemerythrin. Proc. natn. Acad. Sci. U.S.A. 73, 349–351.CrossRefGoogle ScholarPubMed
Strekas, T. C., Packer, A. J. & Spiro, T. G. (1973). Resonance Raman spectra of fern-hemoglobin fluoride: three scattering regimes. J. Raman Spectrosc. I, 197–206.CrossRefGoogle Scholar
Strekas, T. C. & Spiro, T. G. (1972a). Cytochrome c: resonance Raman spectra. Biochim. biophys. Acta 278, 188–192.CrossRefGoogle ScholarPubMed
Strekas, T. C. & Spiro, T. G. (1972b). Hemoglobin: resonance Raman spectra. Biochim. biophys. Acta 263, 830–833.CrossRefGoogle ScholarPubMed
SufrÀ, S., Dellepiane, G., Masetti, G. & Zerei, G. (1977). Resonance Raman spectrum of β-carotene. J. Raman Spectrosc. 6, 267–272.CrossRefGoogle Scholar
Sulkes, M., Lewis, A., Lemley, A. T. & Cookingham, R. T. (1976). Modeling the resonance Raman spectrum of a metarhodopsin: implications for the color of visual pigments. Proc. natn. Acad. Sd. U.S.A. 73, 4266–4270.CrossRefGoogle ScholarPubMed
Szalontai, B., Bagyinka, Cs. & Horvath, L. I. (1977). Changes in the Raman spectrum of frog sciatic nerve during action potential propagation. Biochein. biophys. Res. Commun. 76, 660–665.CrossRefGoogle ScholarPubMed
Tang, S.-P. W., Spiro, T. G., Antanaitas, C., Moss, T. H., Holm, R. H., Herskovitz, T. & Mortensen, L. E. (1975). Resonance Raman spectroscopic evidence for structural variation among bacterial ferredoxin, HIPIP, and Fe454 (SC2Ph)24. Biochem. biophys. Res. Commun. 62, 1–6.CrossRefGoogle Scholar
Tang, S.-P., Spiro, T. G., Mukai, K. & Kimura, T. (1973). Resonance Raman scattering and optical absorption of adrenodoxin and selenaadrenodoxin. Biochem. biophys. Res. Commun. 53, 869–874.CrossRefGoogle ScholarPubMed
Terner, J., Campion, A. & El-sayed, M. A. (1977). Time-resolved resonance Raman spectroscopy of bacteriorhodopsin on the millisecond time scale. Proc. natn. Acad. Sci. U.S.A. 74, 5212–5216.CrossRefGoogle Scholar
Thamann, T. J., Loehr, J. S. & Loehr, T. M. (1977). Resonance Raman study of oxyhemocyanin with unsymmetrically labelled oxygen. J. Am. chem. Soc. 99, 4187–4189.CrossRefGoogle Scholar
Thomas, G. J. (1977). Raman spectroscopy of biopolymers. In Vibrational Spectra and Structure, vol. 3, chap. 3 (ed. Dung, J. R.). New York: Dekker.Google Scholar
Thompson, J. S., Marks, T. J. & Ibers, J. A. (1977). Blue copper proteins: synthesis, spectra, and structures of CuIN3(SR) and CuIIN3(SR) active site analogues. Proc. natn. Acad. Sci. U.S.A. 74, 3114–3118.CrossRefGoogle Scholar
Tomimatsu, Y., Kint, S. & Scherer, J. R. (1973). Resonance Raman spectroscopy of iron(III)-ovotransferin and iron(III)-human serum transferrin. Biochem. biophys. Res. Commun. 54, 1067–1074.CrossRefGoogle Scholar
Tomimatsu, Y., Kint, S. & Scherer, J. R. (1976). Resonance Raman spectra of iron(III)-, copper(II)-, cobalt(III)-, and manganese(III)-transfernins and of bis(2,4,6-trichlorophenolato) diimidazolecopper(II) monohydrate, a possible model for copper(II) binding to transferrins. Biochemistry, N.Y. 15, 4918–4924.CrossRefGoogle ScholarPubMed
Tosi, L., Garnier, A., Herve, M. & Steinbuch, M. (1975). Ceruloplasminanion interaction, a resonance Raman spectroscopic study. Biochem. biophys. Res. Commun. 65, 100–106.CrossRefGoogle Scholar
Tsuboi, M., Hirakawa, A. Y., Nishimura, Y. & Harada, I. (1974).On the excited-state geometry of the adenine residue as revealed by a preresonance Raman effect. J. Raman Spectrosc. 2, 609–621.CrossRefGoogle Scholar
Van duyne, R. P., Jeanmaire, D. L. & Shriver, D. F. (1974). Mode-locked laser Raman spectroscopy - a new technique for the rejection of interfering background luminescence signals. Analyt. Chem. 46, 213–222.CrossRefGoogle Scholar
Verma, S. P. & Wallach, D. F. H. (1975). Carotenoids as Raman-active probes of erythrocyte membrane sttucture. Biochim. biophys. Acta 401, 168–176.CrossRefGoogle Scholar
Warshel, A. (1977). Interpretation of resonance Raman spectra of biological molecules. A. Rev. Biophys. Bioeng. 6, 273–300.CrossRefGoogle ScholarPubMed
Warshel, A. & Dauber, P. (1977). Calculations of resonance Raman spectra of conjugated molecules. J. chem. Phys. 66, 5477–5488.CrossRefGoogle Scholar
Wilbrandt, R., Pagsberg, P., Hansen, K. B. & Weisberg, C. V. (1975) Fast resonance Raman spectroscopy of a free radical. Chem. Phys. Letters 36, 76–78.CrossRefGoogle Scholar
Williams, J. (1962). A comparison of conalbumin and transferrin in the domestic fowl. Biochein. J. 83, 355–364.CrossRefGoogle ScholarPubMed
Wolfenden, R. (1972). Analog approaches to the structure of the transition state in enzyme reactions. Acc. Chem. Res. 5, 10–18.CrossRefGoogle Scholar
Woodruff, W. H. & Atkinson, G. H. (1976). Vidicon detection of resonance Raman spectra: cytochrome c. Analyt. Chem. 48, 186–189.CrossRefGoogle ScholarPubMed
Wozniak, W. T. & Spiro, T. G. (1973). Resonance Raman spectra of vitamin B12 derivatives. J. Am. diem. Soc. 95, 3402–3404.CrossRefGoogle Scholar
Yamamoto, T., Palmer, G. & Crespi, H. (1976). Resonance Raman studies of a c type algal cytochrome. Biochim. biophys. Acta 349, 232–239.CrossRefGoogle Scholar
Yamamoto, T., Palmer, G., Gill, D., Salmeen, I. T. & Rimai, L. (1973). The valence and spin state of iron in oxyhemoglobin as inferred from resonance Raman spectroscopy. J. biol. Chem. 248, 5211–5213.CrossRefGoogle Scholar
Yoshida, C. M., Fredrvin, T. B. & Loehr, T. M. (1975). Resonance Raman study of cobalt(II)-imidazole complexes as models for metalloproteins. J. Am. chem. Soc. 97, 1028–1032.CrossRefGoogle Scholar
Yoshizawa, T. & Wald, G. (1963). Pre-lumirhodopsin and the bleaching of visual pigments. Nature. Lond. 197, 1279–1286.CrossRefGoogle ScholarPubMed
Yu, N.-T. (1977). Raman spectroscopy: a conformational probe in biochemistry. Critical Reviews In Biochemistry 4, 229–280.CrossRefGoogle ScholarPubMed
Zweier, J. L. & Aisen, P. (1977). Studies of transferrin with the use of Cu2+ as an electron paramagnetic resonance spectroscopic probe. J. biol. Chem. 252, 6090–6096.CrossRefGoogle ScholarPubMed