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The Smallest Biomolecules: Diatomics and their Interactions with Heme Proteins
Critical and authoritative evaluation of advances in heme-diatomic interactions
Abhik Ghosh (Edited by)
9780444528391, Elsevier Science
Hardback, published 12 December 2007
614 pages, Approx. 210 illustrations
24 x 16.5 x 3.4 cm, 1.29 kg
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 Who’s 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.
Introductory Overviews
Chapter 1. Mammalian myoglobin as a model for ligand affinities and discrimination in heme Proteins.
John S. Olson and Abhik Ghosh
Chapter 2. A surfeit of biological heme-based sensors.
Marie-Alda Gilles-Gonzales and Gonzalo Gonzales
Chapter 3. NO and NOx interactions with hemes.
Peter C. Ford, Susmita Bandyopadhyay, Mark D. Lim, Ivan M. Lorkovic
Electronic structure and spectroscopy
Chapter 4. CO, NO, and O2 as vbrational probes of heme protein active sites.
Thomas G. Spiro, Mohammed Ibrahim, and Ingar Wasbotten
Chapter 5. Nuclear resonance vibrational spectroscopy.
W. Robert Scheidt and Tim Sage
Chapter 6. EPR and low-temperature MCD spectroscopy of ferrous heme nitrosyls.
Nicolai Lehnert
Aspects of hemoglobins (Except heme-NOx interactions)
Chapter 7. Protoglobin and globin-coupled sensors.
Maqsudul Alam
Chapter 8. Neuroglobin and cytoglobin.
Thorsten Burmester and Tom Hankeln
Chapter 9. Root effect hemoglobins.
Tom Brittain
Chapter 10. Resonance Raman studies of hemoglobins from unicellular organisms.
Syun-Ru Yeh
Heme-NOx interactions
Chapter 11. The reaction between nitrite and hemoglobin: The role of nitrite in hemoglobin-mediated hypoxic vasodilation.
Daniel B. Kim-Shapiro, Mark T. Gladwin, Rakesh P. Patel and Neil Hogg
Chapter 12. Nitric oxide dioxygenase: An ancient enzymic function of hemoglobin.
Paul R. Gardner and Anne M. Gardner
Chapter 13. Respiratory nitric oxide reductases, NorB and NorZ, of the hemeƒ{copper oxidase type.
Walter G. Zumft
Chapter 14. Nitric oxide reductase (P450nor) from Fusarium oxysporum.
Andreas Daiber, Hirofumi Shoun, and Volker Ullrich
Chapter 15. Interaction of NO with insect nitrophorins.
F. Ann Walker
Chapter 16. Bioinorganic chemistry of the HNO Ligand.
Filip Sulc and Patrick Farmer
Selected enzymes and sensors
Chapter 17. Protein-ligand interactions in mammalian nitric oxide synthase.
Denis L. Rousseau, David Li, Eric Y. Hayden, Haiteng Deng and Syun-Ru Yeh
Chapter 18. CooA, a paradigm for gas-sensing regulatory proteins.
Gary P. Roberts, Robert L. Kerby, Hwan Youn, and Mary Conrad
Chapter 19. Soluble guanylate cyclase and its evolutionary relatives.
Eduardo Henrique Silva Sousa, Gonzalo Gonzalez, and Marie-Alda Gilles-Gonzalez
Chapter 20. Resonance Raman studies of the activation mechanism of soluble guanylate cyclase.
Biswajit Pal and Teizo Kitagawa
Chapter 21. FixL
Kenton R. Rodgers and Gudrun S Lukat-Rodgers
