Download or read book A Study of the Resonance Raman Spectra of Some Heme Proteins and Other Molecules written by Thomas C. Strekas and published by . This book was released on 1974 with total page pages. Available in PDF, EPUB and Kindle. Book excerpt:

Download or read book Resonance Raman Spectra of Heme and Metalloproteins written by Thomas G. Spiro and published by Wiley-Interscience. This book was released on 1988 with total page 584 pages. Available in PDF, EPUB and Kindle. Book excerpt:

Download or read book The Application of Optical Absorption and Resonance Raman Spectroscopy to the Study of Heme Proteins and Model Compounds written by Robert T. Kean and published by . This book was released on 1987 with total page 490 pages. Available in PDF, EPUB and Kindle. Book excerpt:

Download or read book Biochemical Applications of Raman and Resonance Raman Spectroscopes written by P Carey and published by Elsevier. This book was released on 2012-12-02 with total page 277 pages. Available in PDF, EPUB and Kindle. Book excerpt: Biochemical Applications of Raman and Resonance Raman Spectroscopies focuses on the application of Raman and resonance Raman spectroscopies to biochemical problems. The book reviews biological systems and details the application of Raman spectroscopy to biological molecules such as proteins, nucleic acids, and lipids. It also looks at codevelopments of lasers, optics, and electronics that drive advances in experimental Raman spectroscopy, along with the important ramifications of these advances for biochemical applications. This volume is organized into eight chapters and begins with an overview of the theoretical and experimental aspects of Raman spectroscopy, including a very brief explanation of what Raman and resonance Raman spectroscopies are and a discussion of their advantages and disadvantages for biochemical studies. The explanation of the Raman and resonance Raman effects is taken up in more detail in the next chapter, which develops the concept of the vibrational motions of molecules by initially considering mechanical ""ball and spring"" models and goes on to use this concept to formulate a classical model for Raman scattering. The resonance Raman effect is then described by another model which emphasizes the discrete or quantized energy levels available to a molecule. The reader is also introduced to the experimental aspects of Raman spectroscopy and the application of Raman spectroscopy across the entire field of biochemistry. Each chapter contains an outline of the basic chemistry and biochemical nomenclature involved. This book will be of interest to chemists, biochemists, and spectroscopists, as well as graduate students and experienced research workers.

Download or read book Resonance Raman Studies of Isotopically Labeled Heme Proteins written by Freeborn Rwere and published by . This book was released on 2009 with total page pages. Available in PDF, EPUB and Kindle. Book excerpt: One effective approach for exploring structure/function relationships in heme proteins is to study proteins that have been reconstituted with modified hemes so as to systematically perturb the protein-heme interface. However, some reconstituted heme proteins may contain substantial fractions of a "non native" state in which the orientation of the heme in the folded pocket differs from the native conformation by a 180° rotation about the [alph alpha - gamma gamma] meso axis. In fact, this "non native" state has also been shown to exist in some native proteins, including several mammalian globins. In order to define changes in the active site structure associated with this "disorder", we have applied resonance Raman spectroscopy to the metMb derivatives, using selectively deuterated protohemes to associate the observed modes with specific fragments of the heme. Resonance Raman spectroscopy is also employed to characterize heme site structural changes arising from conformational heterogeneity in deoxyMb and ligated derivatives; i.e., the ferrous CO (MbCO) and ferric cyanide (MbCN) complexes. Interestingly, while substantial changes in the disposition of the peripheral vinyl and propionate groups can be inferred from the dramatic spectral shifts, the bonds to the internal histidyl imidazole ligand and those of the Fe-CO and Fe-CN fragments are not significantly affected by the heme rotation, as judged by lack of significant shifts in the [upsilon](Fe-NHis), [upsilon](Fe-C) and [upsilon](C-O) modes. We have synthesized protohemes with selectively labeled vinyl groups and have effectively reconstituted them into apo-myoglobin in order to assign the so-called "vinyl bending" modes of heme group in native and reversed forms of myoglobin to their specific molecular fragments based on their isotopic shift with these vinyl labeled protohemes. In a separate project, these vinyl labeled hemes have been employed to further define structural changes in cytochrome P450cam upon substrate binding. Substrate binding to cytochrome P450cam is known to induce the distortions of the out of plane modes such as [gamma gamma]6 and [gamma gamma]7 modes as well as the heme peripheral substituents. The detection of these low frequency modes is especially important as the disposition of these groups can modify the heme reduction potential.

Download or read book Vibrational Spectroscopy in Life Science written by Friedrich Siebert and published by John Wiley & Sons. This book was released on 2008-07-15 with total page 320 pages. Available in PDF, EPUB and Kindle. Book excerpt: The authors describe basic theoretical concepts of vibrational spectroscopy, address instrumental aspects and experimental procedures, and discuss experimental and theoretical methods for interpreting vibrational spectra. It is shown how vibrational spectroscopy provides information on general aspects of proteins, such as structure, dynamics, and protein folding. In addition, the authors use selected examples to demonstrate the application of Raman and IR spectroscopy to specific biological systems, such as metalloproteins, and photoreceptors. Throughout, references to extensive mathematical and physical aspects, involved biochemical features, and aspects of molecular biology are set in boxes for easier reading. Ideal for undergraduate as well as graduate students of biology, biochemistry, chemistry, and physics looking for a compact introduction to this field.

Download or read book Applications of Infrared Raman and Resonance Raman Spectroscopy in Biochemistry written by Frank S. Parker and published by Springer Science & Business Media. This book was released on 1983-10-01 with total page 582 pages. Available in PDF, EPUB and Kindle. Book excerpt:

Download or read book Vibrational Spectroscopy in Protein Research written by Yukihiro Ozaki and published by Academic Press. This book was released on 2020-05-19 with total page 609 pages. Available in PDF, EPUB and Kindle. Book excerpt: Vibrational Spectroscopy in Protein Research offers a thorough discussion of vibrational spectroscopy in protein research, providing researchers with clear, practical guidance on methods employed, areas of application, and modes of analysis. With chapter contributions from international leaders in the field, the book addresses basic principles of vibrational spectroscopy in protein research, instrumentation and technologies available, sampling methods, quantitative analysis, origin of group frequencies, and qualitative interpretation. In addition to discussing vibrational spectroscopy for the analysis of purified proteins, chapter authors also examine its use in studying complex protein systems, including protein aggregates, fibrous proteins, membrane proteins and protein assemblies. Emphasis throughout the book is placed on applications in human tissue, cell development, and disease analysis, with chapters dedicated to studies of molecular changes that occur during disease progression, as well as identifying changes in tissues and cells in disease studies. Provides thorough guidance in implementing cutting-edge vibrational spectroscopic methods from international leaders in the field Emphasizes in vivo, in situ and non-invasive analysis of proteins in biomedical and life science research more broadly Contains chapters that address vibrational spectroscopy for the study of simple purified proteins and protein aggregates, fibrous proteins, membrane proteins and protein assemblies

Download or read book Resonance Raman Spectra of Some Inorganic Molecules and Ions written by and published by . This book was released on 1976 with total page 390 pages. Available in PDF, EPUB and Kindle. Book excerpt:

Download or read book Raman Spectroscopy in Biology written by Anthony T. Tu and published by John Wiley & Sons. This book was released on 1982 with total page 472 pages. Available in PDF, EPUB and Kindle. Book excerpt:

Download or read book Resonance Raman Spectra of Polyenes and Aromatics written by Thomas G. Spiro and published by Wiley-Interscience. This book was released on 1987 with total page 392 pages. Available in PDF, EPUB and Kindle. Book excerpt:

Download or read book Modern Raman Spectroscopy written by Ewen Smith and published by John Wiley & Sons. This book was released on 2013-03-15 with total page 248 pages. Available in PDF, EPUB and Kindle. Book excerpt: This book reflects the dramatic increase in the number of Raman spectrometers being sold to and used by non-expert practitioners. It contains coverage of Resonance Raman and SERS, two hot areas of Raman, in a form suitable for the non-expert. Builds Raman theory up in stages without overloading the reader with complex theory Includes two chapters on instrumentation and interpretation that shows how Raman spectra can be obtained and interpreted Explains the potential of using Raman spectroscopy in a wide variety of applications Includes detailed, but concise information and worked examples

Download or read book Time resolved Surface Enhanced Resonance Raman Spectro electrochemistry of Heme Proteins written by and published by . This book was released on 2010 with total page pages. Available in PDF, EPUB and Kindle. Book excerpt: The membrane protein Cytochrome c Oxidase (CcO) is one of the most important functional bio-molecules. It appears in almost every eukaryotic cell and many bacteria. Although the different species differ in the number of subunits, the functional differences are merely marginal. CcO is the terminal link in the electron transfer pathway of the mitochondrial respiratory chain. Electrons transferred to the catalytic center of the enzyme conduce to the reduction of molecular oxygen to water. Oxygen reduction is coupled to the pumping of protons into the inter-membrane space and hence generates a difference in electrochemical potential of protons across the inner mitochondrial membrane. This potential difference drives the synthesis of adenosine triphosphate (ATP), which is the universal energy carrier within all biological cells. rnrnThe goal of the present work is to contribute to a better understanding of the functional mechanism of CcO by using time-resolved surface enhanced resonance Raman spectroscopy (TR-SERRS). Despite intensive research effort within the last decades, the functional mechanism of CcO is still subject to controversial discussions. It was the primary goal of this dissertation to initiate electron transfer to the redox centers CuA, heme a, heme a3 and CuB electrochemically and to observe the corresponding redox transitions in-situ with a focus on the two heme structures by using SERRS. A measuring cell was developed, which allowed combination of electrochemical excitation with Raman spectroscopy for the purpose of performing the accordant measurements. Cytochrome c was used as a benchmark system to test the new measuring cell and to prove the feasibility of appropriate Raman measurements. In contrast to CcO the heme protein cc contains only a single heme structure. Nevertheless, characteristic Raman bands of the hemes can be observed for both proteins.rnrnIn order to investigate CcO it was immobilized on top of a silver substrate and embedded into an.

Download or read book Resonance Raman Studies of Heme Proteins written by Guangzhi Yuan and published by . This book was released on 2004 with total page 136 pages. Available in PDF, EPUB and Kindle. Book excerpt:

Download or read book Infrared and Raman Spectroscopy written by Peter Larkin and published by Elsevier. This book was released on 2017-11-13 with total page 288 pages. Available in PDF, EPUB and Kindle. Book excerpt: Infrared and Raman Spectroscopy, Principles and Spectral Interpretation, Second Edition provides a solid introduction to vibrational spectroscopy with an emphasis on developing critical interpretation skills. This book fully integrates the use of both IR and Raman spectroscopy as spectral interpretation tools, enabling the user to utilize the strength of both techniques while also recognizing their weaknesses. This second edition more than doubles the amount of interpreted IR and Raman spectra standards and spectral unknowns. The chapter on characteristic group frequencies is expanded to include increased discussions of sulphur and phosphorus organics, aromatic and heteroaromatics as well as inorganic compounds. New topics include a discussion of crystal lattice vibrations (low frequency/THz), confocal Raman microscopy, spatial resolution in IR and Raman microscopy, as well as criteria for selecting Raman excitation wavelengths. These additions accommodate the growing use of vibrational spectroscopy for process analytical monitoring, nanomaterial investigations, and structural and identity determinations to an increasing user base in both industry and academia. Integrates discussion of IR and Raman spectra Pairs generalized IR and Raman spectra of functional groups with tables and text Includes over 150 fully interpreted, high quality IR and Raman reference spectra Contains fifty-four unknown IR and Raman spectra, with a corresponding answer key

Download or read book Probing the Heme Structure and Environment of Bacterial Heme Nitric Oxide OXygen Binding Domains with Resonance Raman Spectroscopy written by Rosalie Tran and published by . This book was released on 2010 with total page 242 pages. Available in PDF, EPUB and Kindle. Book excerpt: The Heme-Nitric oxide/OXygen binding (H-NOX) domain encompasses a family of proteins closely related (≤ 40% sequence identity) to the heme domain of soluble guanylate cyclase (sGC), the eukaryotic enzyme receptor for NO [1, 2]. sGC discriminates between NO and O2, and exclusively binds NO even in the presence of excess O2. Although some H-NOX domains have ligand binding properties that are identical to sGC, others additionally bind O2, including the atypical sGCs from Drosophila melanogaster and Caenorhabditis elegans [1, 3, 4]. The molecular basis of this ligand selectivity is not fully understood. In order to better understand the H-NOX domain, resonance Raman (RR) spectroscopy was employed in combination with isotopic substitution and site-directed mutagenesis to probe the heme pocket in Thermoanaerobacter tengcongensis (Tt H-NOX) as a model system for this family of heme proteins. Thus, the expression, purification, and RR characterization of Tt H-NOX and selected mutants were performed to elucidate the heme environmental properties that influence ligand binding. A striking feature of the O2-bound WT Tt H-NOX crystal structure is the presence of a distorted heme molecule [5]. RR investigation of Tt H-NOX proteins containing mutations at key conserved residues, Ile-5 and Pro-115, determined that the most dramatic heme conformational changes occurred in the O2-bound forms, and that the single P115A mutation generated a significantly relaxed chromophore. Decreased RR intensities were observed for several out-of-plane modes in the 400-750 cm-1 region known to be sensitive to ruffling and saddling deformations, as well as increased vibrational frequencies for the core heme skeletal modes. These changes demonstrated that the P115A heme conformation was considerably more relaxed than WT, with increased flexibility within the protein pocket that allowed for rapid sampling of alternate conformations. Another remarkable feature of this family is the spectroscopic observation of an unusually high [nu](C-O) frequency. To elucidate the interactions responsible for this property, mutations were made in Tt H-NOX to probe the distal pocket, the conserved Tyr-Ser-Arg (YxSxR) motif, and the heme-linkage site (His-102). RR spectra of these mutants indicated that H-bonding interactions between these residues and the heme significantly affected the CO bond by increasing the back-donation of the FeII d[pi] electrons into the CO [pi]* orbitals. The most significant change occurred upon disruption of the H-bonds between the YxSxR motif and the heme propionate groups, producing two dominant CO-bound heme conformations; one was structurally similar to WT, and the other conformer displayed [nu](C-O) downshifts of up to ̃70 cm-1. Based on these shifts, the most important factor contributing to the C-O stretching mode may be the neutralization of the negative charges on the propionate groups via the strictly conserved YxSxR motif. Finally, the role of the Tt H-NOX binding pocket in stabilizing the O2 complex was investigated. Evidence of H-bonds to the bound O2 was demonstrated in the RR spectra of Trp-9 and Tyr-140 mutants; the disruption of the H-bond network in these mutations increased [nu](Fe-O2) upon returning electron density to the Fe-O2 bond. In contrast, the addition of steric bulk to the H-NOX pocket decreased the [nu](Fe-O2) frequency relative to the WT protein. These shifts suggested that the bulky distal residues forced the H-NOX binding pocket into a more open position that increased the distance between Tyr-140 and the O2, thereby weakening this crucial H-bond. Thus, two distinct factors influence the [nu](Fe-O2) in Tt H-NOX: (i) electrostatic effects from H-bonding with Tyr-140, which increased the [nu](Fe-O2) frequency upon its removal; and (ii) steric effects which decreased [nu](Fe-O2) due to bond lengthening from a more loosely held O2 ligand. In summary, this work presents a comparative analysis of the heme environmental effects in Tt H-NOX. By directly probing the interactions between the heme chromophore and the protein pocket through a combination of RR spectroscopy and site-directed mutagenesis, this study may elucidate the biochemical properties of these H-NOX domains, and bring insight into the relationship between heme structure and protein function in this family.

Download or read book Fifth International Conference on the Spectroscopy of Biological Molecules written by T. Theophanides and published by Springer Science & Business Media. This book was released on 2012-12-06 with total page 410 pages. Available in PDF, EPUB and Kindle. Book excerpt: The series of Conferences on the Spectroscopy of Biological Molecules aims to stimulate research and development in this area of Science. The relationship between the structure and the biological activity of such materials as proteins, lipids, and nucleic acids is fundamental. The 5th European Conference on the Spectroscopy of Biological Molecules (ECSBM) is held at the Hotel Poseidon Club, Loutraki, Greece, on 5-10 September 1993. The scientific contents are remained the same as in the past conferences. Emphasis is given to vibrational spectroscopy, mainly infrared and Raman applied to the study of structure and dynamics of proteins, nucleic acids, porphyrins, carbohydrates, membranes, etc. Most of the contributions describe molecular dynamics and excitation processes, in particular the electronic-vibrational excitations, which are studied by Fr-Raman, Fourier Transform Infrared (Fr-IR) coupled often with microscopy and chromatography. Contributions also include Fr-Raman and FT-IR instrumentation and new developments in this area, and applications in Biology and Medicine. Furthermore, there is a plenary lecture in Mass Spectrometry and its applications in biomedical analysis, and a session devoted to Nuclear Magnetic Resonance (NMR) and its application in the study of biological molecules. Several contributions are devoted to other methods, such as CD, optical absorption, fluorescence and molecular graphics simulations. This volume of ECSBM contains shon articles by the invited and contributed lectures as well as from the Poster presentations from many European and non-European countries.