Vibrational Spectroscopy in Life Science [Kõva köide]

Preface		ix
Introduction		1	(10)
Aims of Vibrational Spectroscopy in Life Sciences		2	(1)
Vibrational Spectroscopy - An Atomic-scale Analytical Tool		3	(1)
Biological Systems		4	(3)
Scope of the Book		7	(2)
Further Reading		9	(2)
References		10	(1)
Theory of Infrared Absorption and Raman Spectroscopy		11	(52)
Molecular Vibrations		12	(13)
Normal Modes		15	(3)
Internal Coordinates		18	(1)
The FG-Matrix		19	(4)
Quantum Chemical Calculations of the FG-Matrix		23	(2)
Intensities of Vibrational Bands		25	(13)
Infrared Absorption		25	(3)
Raman Scattering		28	(4)
Resonance Raman Effect		32	(6)
Surface Enhanced Vibrational Spectroscopy		38	(25)
Surface Enhanced Raman Effect		39	(4)
Surface Enhanced Infrared Absorption		43	(17)
References		60	(3)
Instrumentation		63	(36)
Infrared Spectroscopy		63	(16)
Fourier Transform Spectroscopy		64	(3)
Interferometer		67	(2)
Infrared Detectors		69	(1)
Advantages of Fourier Transform Infrared Spectroscopy		70	(1)
Optical Devices: Mirrors or Lenses?		71	(1)
Instrumentation for Time-resolved Infrared Studies		72	(1)
Time-resolved Rapid-scan Fourier Transform Infrared Spectroscopy		72	(2)
Time-resolved Studies Using Tunable Monochromatic Infrared Sources		74	(1)
Time-resolved Fourier Transform Infrared Spectroscopy Using the Step-scan Method		74	(2)
Time-resolved Pump-probe Studies with Sub-nanosecond Time-resolution		76	(3)
Raman Spectroscopy		79	(20)
Laser		80	(1)
Laser Beam Properties		81	(2)
Optical Set-up		83	(1)
Spectrometer and Detection Systems		84	(1)
Monochromators		84	(2)
Spectrographs		86	(1)
Confocal Spectrometers		87	(2)
Fourier Transform Raman Interferometers		89	(8)
References		97	(2)
Experimental Techniques		99	(56)
Inherent Problems of Infrared and Raman Spectroscopy in Life Sciences		99	(6)
The ``Water'' Problem in Infrared Spectroscopy		99	(2)
Unwanted Photophysical and Photochemical Processes in Raman Spectroscopy		101	(1)
Fluorescence and Raman Scattering		102	(2)
Photoinduced Processes		104	(1)
Sample Arrangements		105	(13)
Infrared Spectroscopy		106	(1)
Sandwich Cuvettes for Solution Studies		106	(2)
The Attenuated Total Reflection (ATR) Method		108	(5)
Electrochemical Cell for Infrared Spectroscopy		113	(3)
Raman and Resonance Raman Spectroscopy		116	(1)
Measurements in Solutions		116	(1)
Solid State and Low-temperature Measurements		117	(1)
Surface Enhanced Vibrational Spectroscopy		118	(13)
Colloidal Suspensions		119	(1)
Massive Electrodes in Electrochemical Cells		120	(2)
Metal Films Deposited on ATR Elements		122	(1)
Metal/Electrolyte Interfaces		123	(4)
Adsorption-induced Structural Changes of Biopolymers		127	(1)
Biocompatible Surface Coatings		128	(2)
Tip-enhanced Raman Scattering		130	(1)
Time-resolved Vibrational Spectroscopic Techniques		131	(18)
Pump-Probe Resonance Raman Experiments		132	(1)
Continuous-wave Excitation		133	(5)
Pulsed-laser Excitation		138	(3)
Photoinduced Processes with Caged Compounds		141	(1)
Rapid Mixing Techniques		141	(3)
Rapid Flow		144	(1)
Rapid Freeze-Quench		145	(1)
Relaxation Methods		146	(2)
Spatially Resolved Vibrational Spectroscopy		148	(1)
Analysis of Spectra		149	(6)
References		151	(4)
Structural Studies		155	(26)
Basic Considerations		155	(3)
Practical Approaches		158	(3)
Studies on the Origin of the Sensitivity of Amide I Bands to Secondary Structure		161	(6)
Direct Measurement of the Interaction of the Amide I Oscillators		167	(2)
UV-resonance Raman Studies Using the Amide III Mode		169	(2)
Protein Folding and Unfolding Studies Using Vibrational Spectroscopy		171	(10)
References		178	(3)
Retinal Proteins and Photoinduced Processes		181	(46)
Rhodopsin		183	(23)
Resonance Raman Studies of Rhodopsin		185	(3)
Resonance Raman Spectra of Bathorhodopsin		188	(7)
Fourier Transform Infrared Studies of the Activation Mechanism of Rhodopsin		195	(2)
Low-temperature Photoproducts		197	(4)
The Active State Metarhodopsin II (MII)		201	(5)
Infrared Studies of the Light-driven Proton Pump Bacteriorhodopsin		206	(8)
Study of the Anion Uptake by the Retinal Protein Halorhodopsin Using ATR Infrared Spectroscopy		214	(3)
Infrared Studies Using Caged Compounds as the Trigger Source		217	(10)
References		222	(5)
Heme Proteins		227	(56)
Vibrational Spectroscopy of Metalloporphyrins		228	(8)
Metalloporphyrins Under D4h Symmetry		228	(3)
Symmetry Lowering		231	(1)
Axial Ligation		232	(1)
Normal Mode Analyses		233	(1)
Empirical Structure-Spectra Relationships		234	(2)
Hemoglobin and Myoglobin		236	(8)
Vibrational Analysis of the Heme Cofactor		237	(2)
Iron-Ligand and Internal Ligand Modes		239	(1)
Probing Quaternary Structure Changes		240	(4)
Cytochrome c - a Soluble Electron-transferring Protein		244	(24)
Vibrational Assignments		245	(1)
Redox Equilibria in Solution		246	(2)
Conformational Equilibria and Dynamics		248	(5)
Redox and Conformational Equilibria in the Immobilised State		253	(7)
Electron Transfer Dynamics and Mechanism		260	(7)
The Relevance of Surface-enhanced Vibrational Spectroscopic Studies for Elucidating Biological Functions		267	(1)
Cytochrome c Oxidase		268	(15)
Resonance Raman Spectroscopy		268	(3)
Redox Transitions		271	(3)
Catalytic Cycle		274	(3)
Oxidases from Extremophiles and Archaea		277	(1)
References		278	(5)
Non-heme Metalloproteins		283	(22)
Copper Proteins		284	(6)
Iron-Sulfur Proteins		290	(6)
Di-iron Proteins		296	(4)
Hydrogenases		300	(5)
References		302	(3)
Index		305

Friedrich Siebert is Professor for Biophysics at the University of Freiburg. He studied physics in Freiburg and Hamburg, receiving his PhD in solid-state physics. Since his diploma thesis he is working with different methods of vibrational spectroscopy. In 1972 he changed to biophysics, establishing the method of static and time-resolved infrared difference spectroscopy. Current research interests are photo-biological systems, membrane proteins and receptors, surface-enhanced techniques, time-resolved IR techniques. Peter Hildebrandt received his PhD in chemistry from the Universität Göttingen in 1985. After a post-doc stay in Princeton, he worked in research institutes in Göttingen, Mülheim, and Lisboa. Since 2003 he is Professor for Physical Chemistry and Biophysical Chemistry at the Technische Universität Berlin. His research is dedicated to vibrational spectroscopy of biological systems, focussing on Raman spectroscopic techniques applied to redox proteins and photoreceptors.