Ghosh | The Smallest Biomolecules: Diatomics and Their Interactions with Heme Proteins | Buch | 978-0-444-52839-1 | sack.de

Buch, Englisch, 614 Seiten, Format (B × H): 168 mm x 239 mm, Gewicht: 1270 g

Ghosh

The Smallest Biomolecules: Diatomics and Their Interactions with Heme Proteins

Buch, Englisch, 614 Seiten, Format (B × H): 168 mm x 239 mm, Gewicht: 1270 g

ISBN: 978-0-444-52839-1
Verlag: Elsevier Science


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.
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Weitere Infos & Material


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 hemef{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


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