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|a 0080556329 (electronic bk)
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|a (OCoLC)671532866
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|a Elsevierocn228148392
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|a ocn228148392
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|a (OCoLC)228148392
|z (OCoLC)190824942
|z (OCoLC)441816567
|z (OCoLC)505139278
|z (OCoLC)647691311
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|e AFNOR
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|a eng
|2 639-2
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|a Ghosh, Abhik.
|4 aut.
|e Auteur
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|a The Smallest Biomolecules :
|b Diatomics and their Interactions with Heme Proteins
|c Abhik Ghosh.
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|a Données textuelles.
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|a San Diego, CA :
|b Elsevier Science,
|c 2008.
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|b txt
|2 rdacontent
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|2 rdamedia
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|a Contient un index.
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|a Titre provenant de la page de titre du document numérique.
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|a Numérisation de l'édition de Amsterdam : Elsevier Science & Technology Books, 2008.
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|a La pagination de l'édition imprimée correspondante est de 626 p.
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|a L'accès complet à la ressource est réservé aux usagers des établissements qui en ont fait l'acquisition
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|a Fichier PDF.
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|a This is not a book on NO biology, nor about hemoglobin, nor about heme-based sensors per se. Of course, it covers all these topics and more, but above all, it aims at providing a truly multidisciplinary perspective of heme-diatomic interactions. The overarching goal is to build bridges among disciplines, to bring about a meeting of minds. The contributors to this book hail from diverse university departments and disciplines chemistry, biochemistry, molecular biology, microbiology, zoology, physics, medicine and surgery, bringing with them very different views of heme-diatomic interactions. The hope is that the juxtaposition of this diversity will lead to increased exchanges of ideas, approaches, and techniques across traditional disciplinary boundaries. The authors represent a veritable Whos Who of heme protein research and include John Olson, Tom Spiro, Walter Zumft, F. Ann Walker, Teizo Kitagawa, W. Robert Scheidt, Pat Farmer, Marie-Alda Gilles-Gonzalez, and many other equally distinguished scientists. Extremely distinguished list of authors Multidisciplinary character equally suitable for chemists and biochemists Covers the hottest topics in heme protein research: sensors, NO biology, new roles of hemoglobin, etc
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|a Configuration requise : navigateur internet.
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|b Editor: Abhik Ghosh
|b Table of Contents
|b Introductory Overviews
|b Chapter 1. Mammalian myoglobin as a model for ligand affinities and discrimination in heme Proteins.
|b John S. Olson and Abhik Ghosh
|b Chapter 2. A surfeit of biological heme-based sensors.
|b Marie-Alda Gilles-Gonzales and Gonzalo Gonzales
|b Chapter 3. NO and NOx interactions with hemes.
|b Peter C. Ford, Susmita Bandyopadhyay, Mark D. Lim, Ivan M. Lorkovic
|b Electronic structure and spectroscopy
|b Chapter 4. CO, NO, and O2 as vbrational probes of heme protein active sites.
|b Thomas G. Spiro, Mohammed Ibrahim, and Ingar Wasbotten
|b Chapter 5. Nuclear resonance vibrational spectroscopy.
|b W. Robert Scheidt and Tim Sage
|b Chapter 6. EPR and low-temperature MCD spectroscopy of ferrous heme nitrosyls.
|b Nicolai Lehnert
|b Aspects of hemoglobins (Except heme-NOx interactions)
|b Chapter 7. Protoglobin and globin-coupled sensors.
|b Maqsudul Alam
|b Chapter 8. Neuroglobin and cytoglobin.
|b Thorsten Burmester and Tom Hankeln
|b Chapter 9. Root effect hemoglobins.
|b Tom Brittain
|b Chapter 10. Resonance Raman studies of hemoglobins from unicellular organisms.
|b Syun-Ru Yeh
|b Heme-NOx interactions
|b Chapter 11. The reaction between nitrite and hemoglobin: The role of nitrite in hemoglobin-mediated hypoxic vasodilation.
|b Daniel B. Kim-Shapiro, Mark T. Gladwin, Rakesh P. Patel and Neil Hogg
|b Chapter 12. Nitric oxide dioxygenase: An ancient enzymic function of hemoglobin.
|b Paul R. Gardner and Anne M. Gardner
|b Chapter 13. Respiratory nitric oxide reductases, NorB and NorZ, of the heme{copper oxidase type.
|b Walter G. Zumft
|b Chapter 14. Nitric oxide reductase (P450nor) from Fusarium oxysporum.
|b Andreas Daiber, Hirofumi Shoun, and Volker Ullrich
|b Chapter 15. Interaction of NO with insect nitrophorins.
|b F. Ann Walker
|b Chapter 16. Bioinorganic chemistry of the HNO Ligand.
|b Filip Sulc and Patrick Farmer
|b -- Selected enzymes and sensors
|b Chapter 17. Protein-ligand interactions in mammalian nitric oxide synthase.
|b Denis L. Rousseau, David Li, Eric Y. Hayden, Haiteng Deng and Syun-Ru Yeh
|b Chapter 18. CooA, a paradigm for gas-sensing regulatory proteins.
|b Gary P. Roberts, Robert L. Kerby, Hwan Youn, and Mary Conrad
|b Chapter 19. Soluble guanylate cyclase and its evolutionary relatives.
|b Eduardo Henrique Silva Sousa, Gonzalo Gonzalez, and Marie-Alda Gilles-Gonzalez
|b Chapter 20. Resonance Raman studies of the activation mechanism of soluble guanylate cyclase.
|b Biswajit Pal and Teizo Kitagawa
|b Chapter 21. FixL
|b Kenton R. Rodgers and Gudrun S Lukat-Rodgers
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|a Diatomic molecules.
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|a Hemoproteins.
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|u https://srvext.uco.fr/login?url=https://univ.scholarvox.com/book/45006553
|w Données éditeur
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