Electron Tunneling in Proteins PDF Download
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Author: Jeffrey J. Regan
Publisher:
ISBN:
Category :
Languages : en
Pages : 134
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Author: Jeffrey J. Regan
Publisher:
ISBN:
Category :
Languages : en
Pages : 134
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Author: Dr Derek Bendall
Publisher: Garland Science
ISBN: 1000102262
Category : Cooking
Languages : en
Pages : 317
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Book Description
This book is unique; the factual content and ideas it expounds are only just beginning to be touched upon in standard texts. Protein Electron Transfer is a major collaborative effort by leading experts and explores the molecular basis of the rapidly expan
Author: Crystal Shih
Publisher:
ISBN:
Category : Electronic dissertations
Languages : en
Pages : 254
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Author: Lawrence Flax
Publisher:
ISBN:
Category : Electric conductivity
Languages : en
Pages : 28
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Author: Adrian Ponce
Publisher:
ISBN:
Category : Charge transfer
Languages : en
Pages : 474
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Book Description
The subject of this thesis is electronic coupling in donor-bridge-acceptor systems.
Author: Britton Chance
Publisher: Academic Press
ISBN: 148327134X
Category : Science
Languages : en
Pages : 777
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Book Description
Tunneling in Biological Systems focuses on the low temperature electron transport that reveals a quantum-mechanical effect called "tunneling. This book discusses the tunneling in physical systems; detection of molecular vibrations with electron tunneling; chemical-rate theory of small-polaron hopping; and experimental approaches to electronic coupling in metal ion redox systems. The Faraday rotation and photoconductivity of photosynthetic structures at microwave frequencies; dynamics of electron transport in macromolecules; and electron transfer reactions in cytochrome oxidase are also elaborated. This text likewise covers the kinetic evidence for electron tunneling in solution; specificity and control in biological systems; molecular tunneling in heme proteins; and ligand binding. This publication is valuable to students and researchers interested in the physics of biological and medical problems.
Author: Rudolf K. Allemann
Publisher: Royal Society of Chemistry
ISBN: 0854041222
Category : Science
Languages : en
Pages : 412
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Book Description
In recent years, there has been an explosion in knowledge and research associated with the field of enzyme catalysis and H-tunneling. Rich in its breath and depth, this introduction to modern theories and methods of study is suitable for experienced researchers those new to the subject. Edited by two leading experts, and bringing together the foremost practitioners in the field, this up-to-date account of a rapidly developing field sits at the interface between biology, chemistry and physics. It covers computational, kinetic and structural analysis of tunnelling and the synergy in combining these methods (with a major focus on H-tunneling reactions in enzyme systems). The book starts with a brief overview of proton and electron transfer history by Nobel Laureate, Rudolph A. Marcus. The reader is then guided through chapters covering almost every aspect of reactions in enzyme catalysis ranging from descriptions of the relevant quantum theory and quantum/classical theoretical methodology to the description of experimental results. The theoretical interpretation of these large systems includes both quantum mechanical and statistical mechanical computations, as well as simple more approximate models. Most of the chapters focus on enzymatic catalysis of hydride, proton and H" transfer, an example of the latter being proton coupled electron transfer. There is also a chapter on electron transfer in proteins. This is timely since the theoretical framework developed fifty years ago for treating electron transfers has now been adapted to H-transfers and electron transfers in proteins. Accessible in style, this book is suitable for a wide audience but will be particularly useful to advanced level undergraduates, postgraduates and early postdoctoral workers.
Author: Heather R. Williamson
Publisher:
ISBN:
Category : Biochemical engineering
Languages : en
Pages : 204
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Book Description
Multi-step electron tunneling, or "hopping," has become a fast-developing research field with studies ranging from theoretical modeling systems, inorganic complexes, to biological systems. In particular, the field is exploring hopping mechanisms in new proteins and protein complexes, as well as further understanding the classical biological hopping systems such as ribonuclease reductase, DNA photolyases, and photosystem II. Despite the plethora of natural systems, only a few biologically engineered systems exist. Engineered hopping systems can provide valuable information on key structural and electronic features, just like other kinds of biological model systems. Also, engineered systems can harness common biologic processes and utilize them for alternative reactions. In this thesis, two new hopping systems are engineered and characterized. The protein Pseudomonas aeruginosa azurin is used as a building block to create the two new hopping systems. Besides being well studied and amenable to mutation, azurin already has been used to successfully engineer a hopping system. The two hopping systems presented in this thesis have a histidine-attached high potential rhenium 4,7-dimethyl-1,10-phenanthroline tricarbonyl [Re(dmp)(CO)3]+ label which, when excited, acts as the initial electron acceptor. The metal donor is the type I copper of the azurin protein. The hopping intermediates are all tryptophan, an amino acid mutated into the azurin at select sites between the photoactive metal label and the protein metal site. One system exhibits an inter-molecular hopping through a protein dimer interface; the other system undergoes intra-molecular multi-hopping utilizing a tryptophan "wire." The electron transfer reactions are triggered by excitation of the rhenium label and monitored by UV-Visible transient absorption, luminescence decays measurements, and time-resolved Infrared spectroscopy (TRIR). Both systems were structurally characterized by protein X-ray crystallography.
Author: Kevin Richard Hoke
Publisher:
ISBN:
Category : Copper proteins
Languages : en
Pages : 216
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"The CU_A ̀ˆdomain is the initial point of entry for electrons into cytochrome c oxidase. In order to explain fast rates of intramolecular electron transfer (ET) over long distances, it has been suggested that the ET reorganization energy is less than 0.6 eV. This issue was investigated by attaching a ruthenium(II)-bisbipyridyl-imidazole complex to a single surface histidine of the Thermus thermophilus CU_A domain. Photoexcitation results in rapid ET between the ruthenium complex and the copper site. This was done over a range of driving forces by employing a series of substituted bipyridines. An analysis of the driving force dependence of the ET rate suggests that the total reorganization energy for this CU_A fragment is about 0.7 eV, almost as high as for azurin. The degree of solvent exposure of the active site may be the factor responsible for the higher reorganization energy." In addition, the effect of distance on ET rate was investigated. Two variants of ruthenium-modified CU_A were examined, in which the labeled sites are two positions apart. The observed ET rates only differ by an order of magnitude, drastically less than what theory would predict. It appears that geometric factors other than length influence ET coupled through hydrogen bonds." The role of hydrogen bonds in ET was studied in more detail with ruthenium-modified azurin. Changes in the ET rate were observed for different degrees of deuterium incorporation in the system. For wild-type azurin, the greatest effect (k_H/k_D [almost equal to symbol] 0.7) is seen when the protein is subjected to rigorous exchange under denaturing conditions, then returned to a normal buffer as a control for the solvent isotope effect on the reorganization energy. This is the expected outcome if deuteration of internal, difficult to exchange hydrogen bonds results in improved coupling along the path."
Author: Lawrence Flax
Publisher:
ISBN:
Category : Electric conductivity
Languages : en
Pages : 0
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