Author: James Malcolm McCormickPublisher:
ISBN:
Category :
Languages : en
Pages : 536
Book Description
Spectroscopic Studies of Mixed-valent Binuclear Non-heme Iron Active Sites
Author: James Malcolm McCormickPublisher:
ISBN:
Category :
Languages : en
Pages : 536
Book Description
Spectroscopic and Reactivity Studies of Binuclear Non-heme Iron Complexes
Author: Subhasish MukerjeeSpectroscopic and Reactivity Studies of Mononuclear and Binuclear Non-heme Iron Complexes
Author: Bala Sundari T. KasibhatlaPublisher:
ISBN:
Category :
Languages : en
Pages : 478
Book Description
Spectroscopic and Theroretical Definition of Binuclear Non-heme Iron Active Sites
Author: Yi-Shan YangSpectroscopic and Theoretical Elucidation of Structural Contributions to Reactivity in Binuclear Non-heme Iron Enzymes
Author: Jennifer Kathleen SchwartzPublisher:
ISBN:
Category :
Languages : en
Pages : 568
Book Description
Spectroscopic and Theoretical Studies of Complexes which Model the Active Sites of Non-heme Iron Proteins
Author: Carl A. BrownSpectroscopic Characterization of Binuclear Non-heme Iron and MN/FE Active Sites
Author: Yeonju KwakPublisher:
ISBN:
Category :
Languages : en
Pages :
Book Description
Binuclear non-heme iron enzymes catalyze various reactions including H-atom abstraction, desaturation, hydroxylation, and electrophilic aromatic substitution through O2 activation. In addition, they protect cells from oxidative stress and regulate iron levels in the cell. These enzymes utilize two irons and have common structural motif of 2-His / 4-carboxylate. Despite the enzymes' structural similarities, subtle changes at their active sites allow these enzymes to have different reactivities. Understanding the active site structures of these enzymes and the key mechanistic features related to these structures can provide a basis for potential applications: they could be drug inhibition targets to treat cancer, diabetes, and pathogenic diseases; they could work as biocatalysts; and they could carry out bioremediation reactions. In this dissertation, studies that examine three binuclear non-heme iron and Mn/Fe enzyme active sites (class Ic ribonucleotide reductase, ferritin variants, and bacterioferritin) and peroxo-bridged biferric model complexes are described. A combined spectroscopic methodology of nuclear resonance vibrational spectroscopy (NRVS), circular dichroism (CD), magnetic circular dichroism (MCD), and variable temperature, variable field (VTVH) MCD is used to probe geometric and electronic structures of Mn and Fe centers in protein active site and in model complexes.
Spectroscopic Studies of the Binuclear Iron Active Site in Hemerythrin
Author: Richard Carroll ReemPublisher:
ISBN:
Category :
Languages : en
Pages : 728
Book Description
High Resolution EPR
Author: Graeme HansonPublisher: Springer Science & Business Media
ISBN: 0387848568
Category : Medical
Languages : en
Pages : 666
Book Description
Metalloproteins comprise approximately 30% of all known proteins, and are involved in a variety of biologically important processes, including oxygen transport, biosynthesis, electron transfer, biodegradation, drug metabolism, proteolysis, and hydrolysis of amides and esters, environmental sulfur and nitrogen cycles, and disease mechanisms. EPR spectroscopy has an important role in not only the geometric structural characterization of the redox cofactors in metalloproteins but also their electronic structure, as this is crucial for their reactivity. The advent of x-ray crystallographic snapshots of the active site redox cofactors in metalloenzymes in conjunction with high-resolution EPR spectroscopy has provided detailed structural insights into their catalytic mechanisms. This volume was conceived in 2005 at the Rocky Mountain Conference on Analytical Chemistry (EPR Symposium) to highlight the importance of high-resolution EPR spectroscopy to the structural (geometric and electronic) characterization of redox active cofactors in metalloproteins. We have been fortunate to have enlisted internationally recognized experts in this joint venture to provide the scientific community with an overview of high-resolution EPR and its application to metals in biology. This volume, High-Resolution EPR: Applications to Metalloenzymes and Metals in Medicine, covers high-resolution EPR methods, iron proteins, nickel and copper enzymes, and metals in medicine. An eloquent synopsis of each chapter is provided by John Pilbrow in the Introduction. A second volume, Metals in Biology: Applications of High-Resolution EPR to Metalloenzymes, will appear later this year covering the complement of other metalloproteins. One of the pioneers in the development of pulsed EPR and its application to metalloproteins was Arthur Schweiger, whose contribution we include in this volume. Unfortunately, he passed away suddenly during the preparation of this volume. The editors and coauthors are extremely honored to dedicate this volume to the memory of Arthur Schweiger in recognition of his technical advances and insights into pulsed EPR and its application to metalloproteins. Arthur was extremely humble and treated everyone with equal respect. He was a gifted educator with an ability to explain complex phenomena in terms of simple intuitive pictures, had a delightful personality, and continues to be sadly missed by the community. It is an honor for the editors to facilitate the dissemination of these excellent contributions to the scientific community. Suggestions for future volumes are always appreciated.
Blood and Tissue Oxygen Carriers
Author: Charlotte P. MangumPublisher: Springer Science & Business Media
ISBN: 3642764185
Category : Medical
Languages : en
Pages : 468
Book Description
Investigations of the oxygen carriers range from the characterization of natural populations to measurements of tenths of nanometer distances between atoms. The scope is so great that few biologists and biochemists can fully comprehend the primary literature in its entirety. In addition, the findings of the past two or three decades have advanced the field so rapidly that a truly current account is not readily accessible to a general audience. In recognition of the problem a symposium was held and its proceedings published in the American Zoologist in 1980. Although it included several research reports, most of the contributions were intended to summarize then state-of-the-art information on molecular structure and respiratory function at a level that could be understood by biologists and biochemists who are not experts on our subject. Judging from the reprint requests with which the authors were inundated, the assessment of need had been accurate. I believe that the need for an update, which is wholly focused on communication to the general audience, is even greater in 1992. I therefore asked the authors of this volume to address individuals who might otherwise turn in vain to an advanced textbook of physiology or biochemistry. I have, of course, requested a more comprehensive coverage than would be possible in a general text, but one that is not more parochial. Just as textbooks differ vastly in the level at which their subject matter is presented, so the level of non-expertise was conceived differently by the contributors to this volume.