Please use this identifier to cite or link to this item: https://ktisis.cut.ac.cy/handle/10488/11060
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dc.contributor.authorVarotsis, Constantinos-
dc.contributor.authorBabcock, Gerald-
dc.contributor.otherΒαρότσης, Κωνσταντίνος-
dc.date.accessioned2018-05-16T14:47:33Z-
dc.date.available2018-05-16T14:47:33Z-
dc.date.issued1993-01-
dc.identifier.citationNanosecond Time-Resolved Resonance Raman Spectroscopy. In Metallobiochemistry Part C: Spectroscopic and Physical Methods for Probing Metal Ion Environments in Metalloenzymes and Metalloproteins, 1993, pp. 409-431en_US
dc.description.abstractResonance Raman (RR) spectroscopy is a powerful technique to probe molecular vibrations that are coupled to electronic transitions. Monochromatic light, now universally obtained from continuous wave (CW) or pulsed lasers, is used to illuminate a sample, and the spectrum of scattered radiation is analyzed to determine vibrational information on molecular species within the sample. By bringing the laser frequency into resonance with an electronic transition of a species of interest, dramatic enhancements in scattered intensity result. The individual vibrational frequencies observed in a Raman spectrum arise from normal modes in the ground electronic state. The intensities of the Raman lines, however, reflect the character of the electronic excited states. Owing to the high selectivity and sensitivity in the enhancement of vibrational modes, resonance Raman spectroscopy offers the opportunity to probe chemical species such as reaction intermediates, excited electronic states, and chromophoric site(s) of biological systems. Biological chromophores such as heroes, flavins, chlorophylls, and a number of different types of metal-containing proteins are investigated by resonance Raman spectroscopy. The static resonance Raman effect and biological applications of Raman spectroscopy has been the subject of numerous reports and reviews. Time-resolved resonance Raman (TR3) spectroscopy is a technique that can be used to probe structural and conformational as well as kinetic properties of transient species. The two-pulse, pump-probe, time-resolved Raman approach, in conjunction with a single monochromator and a CCD detector, provides the most reliable configuration to record the time evolution of transient species.en_US
dc.formatpdfen_US
dc.language.isoenen_US
dc.relation.ispartofseriesMethods in Enzymology-
dc.rights© Elsevieren_US
dc.subjectCytochrome c oxidaseen_US
dc.subjectHemoglobinen_US
dc.subjectMetalloproteinen_US
dc.subjectMyoglobinen_US
dc.titleNanosecond Time-Resolved Resonance Raman Spectroscopyen_US
dc.typeBook Chapteren_US
dc.collaborationMichigan State Universityen_US
dc.subject.categoryBiological Sciencesen_US
dc.countryU.S.A.en_US
dc.subject.fieldNatural Sciencesen_US
dc.identifier.doi10.1016/0076-6879(93)26019-6en_US
cut.common.academicyear1995-1996en_US
dc.identifier.spage409en_US
dc.identifier.epage431en_US
item.languageiso639-1en-
item.grantfulltextnone-
item.openairetypebookPart-
item.fulltextNo Fulltext-
item.cerifentitytypePublications-
item.openairecristypehttp://purl.org/coar/resource_type/c_3248-
crisitem.author.deptDepartment of Chemical Engineering-
crisitem.author.facultyFaculty of Geotechnical Sciences and Environmental Management-
crisitem.author.orcid0000-0003-2771-8891-
crisitem.author.parentorgFaculty of Geotechnical Sciences and Environmental Management-
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