The Smallest Biomolecules: Diatomics and their Interactions with Heme Proteins book cover

The Smallest Biomolecules: Diatomics and their Interactions with Heme Proteins

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.

Audience
Libraries Professors and group leaders Students, postdocs

Hardbound, 614 Pages

Published: December 2007

Imprint: Elsevier

ISBN: 978-0-444-52839-1

Contents

  • Introductory overviewsChapter 1. Mammalian myoglobin as a model for ligand understanding affinities and discrimination in heme proteinsJohn S. Olson and Abhik GhoshChapter 2. A surfeit of biological heme-based sensorsMarie-Alda Gilles-Gonzales and Gonzalo GonzalesChapter 3. NO and NOx interactions with hemesPeter C. Ford, Susmita Bandyopadhyay, Mark D. Lim, Ivan M. LorkovicElectronic structure and spectroscopyChapter 4. CO, NO, and O2 as vbrational probes of heme protein active sitesThomas G. Spiro, Mohammed Ibrahim and Ingar WasbottenChapter 5. Nuclear resonance vibrational spectroscopyW. Robert Scheidt and Tim Sage Chapter 6. EPR and low-temperature MCD spectroscopy of ferrous heme nitrosyls Nicolai LehnertAspects of hemoglobins (except heme-NOx interactions)Chapter 7. Protoglobin and globin-coupled sensorsMaqsudul Alam, Tracey Allen Keawe Freitas, Jennifer Saito, Xuehua(Ivy) Wan and Shaobin HouChapter 8. Neuroglobin and cytoglobinThorsten Burmester and Tom HankelnChapter 9. Extreme pH sensitivity in the binding of oxygen to some fish hemoglobins: the Root effectTom BrittainChapter 10. Microbial hemoglobins: Structure, function and foldingTsuyoshi Egawa, Changyuan Lu, Dipanwita Batabyal, Masahiro Mukai and Syun-Ru YehHeme-NOx interactionsChapter 11. The reaction between nitrite and hemoglobin: The role of nitrite in hemoglobin-mediated hypoxic vasodilationDaniel B. Kim-Shapiro, Mark T. Gladwin, Rakesh P. Patel and Neil HoggChapter 12. Nitric oxide dioxygenase: An ancient enzymic function of hemoglobin Paul R. Gardner and Anne M. GardnerChapter 13. Respiratory nitric oxide reductases, NorB and NorZ, of the hemeƒ{copper oxidase typeWalter G. ZumftChapter 14. Nitric oxide reductase (P450nor) from Fusarium oxysporumAndreas Daiber, Hirofumi Shoun and Volker UllrichChapter 15. Nitric oxide interaction with insect nitrophorins and possibilities for the Electron configuration of the {FeNO}6 complexF. Ann WalkerChapter 16. Bioinorganic chemistry of the HNO lgandFilip Sulc and Patrick J. Farmer Selected enzymes and sensorsChapter 17. Protein-ligand interactions in mammalian nitric oxide synthaseDenis L. Rousseau, David Li, Eric Y. Hayden, Haiteng Deng and Syun-Ru YehChapter 18. CooA, a paradigm for gas-sensing regulatory proteinsGary P. Roberts, Robert L. Kerby, Hwan Youn and Mary ConradChapter 19. Soluble guanylate cyclase and its evolutionary relativesEduardo Henrique Silva Sousa, Gonzalo Gonzalez and Marie-Alda Gilles-GonzalezChapter 20. Resonance Raman studies of the activation mechanism of soluble guanylate cyclaseBiswajit Pal and Teizo KitagawaChapter 21. Insights into heme-based O2 sensing from structure-function relationships in the FixL proteinsKenton R. Rodgers, Graeme R. A. Wyllie and Gudrun S Lukat-Rodgers

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