Globins and Other Nitric Oxide-Reactive Proteins, Part B

Edited by

  • Robert K. Poole, University of Sheffield, UK

The critically acclaimed laboratory standard for more than forty years, Methods in Enzymology is one of the most highly respected publications in the field of biochemistry. Since 1955, each volume has been eagerly awaited, frequently consulted, and praised by researchers and reviewers alike. Now with over 400 volumes (all of them still in print), the series contains much material still relevant today—truly an essential publication for researchers in all fields of life sciences. Methods in Enzymology is now available online at ScienceDirect — full-text online of volumes 1 onwards. For more information about the Elsevier Book Series on ScienceDirect Program, please visit: This volume is the second of two planned volumes on the topic of globin and other nitric oxide-reactive proteins.
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Researchers in academics and industry studying biochemistry.


Book information

  • Published: April 2008
  • ISBN: 978-0-12-374278-0

Table of Contents

Section I. Nitric Oxide-Metabolising and Detoxifying EnzymesChapter 1Structural Studies on Flavodiiron Proteins João B. Vicente, Maria Arménia Carrondo, Miguel Teixeira and Carlos FrazãoChapter 2Biochemical, Spectroscopic and Thermodynamic Properties of Flavodiiron ProteinsJoão B. Vicente, Marta C. Justino, Vera L. Gonçalves, Lígia M. Saraiva and Miguel TeixeiraChapter 3Kinetic Characterization of the Escherichia coli Nitric Oxide Reductase Flavorubredoxin João B. Vicente, Francesca M. Scandurra, Elena Forte, Maurizio Brunori, Paolo Sarti, Miguel Teixeira and Alessandro GiuffrèChapter 4Escherichia coli cytochrome c-nitrite reductase NrfAThomas A. Clarke, Paul C. Mills, Susie R. Poock, Julea N. Butt1, Myles R. Cheesman, Jeffrey A. Cole, Jay C. D. Hinton, Andrew M. Hemmings, Gemma Kemp, Christopher Söderberg, Stephen Spiro, Jessica Van Wonderen, David J. RichardsonChapter 5The respiratory NO reductase (NorBC) from Paracoccus denitrificansSarah J. Field, Faye H. Thorndycroft, Andrey D. Matorin, David J. Richardson and Nicholas J. WatmoughChapter 6Redox-controlled dinitrosyl formation at the diiron-oxo center of NorARainer Cramm, Katja StrubeChapter 7Purification and functional analysis of fungal nitric oxide reductase cytochrome P450norLi Zhangand Hirofumi Shoun Chapter 8 A Quantitative approach to nitric oxide inhibition of terminal oxidases of the respiratory chain Maria G. Mason, Rebecca S. Holladay, Peter Nicholls, Mark Shepherd and Chris E. CooperSection II. Sensor ProteinsChapter 9Cloning, Expression, and Purification of the N-terminal Heme Binding Domain of the Globin-Coupled SensorsJennifer A. Saito, Tracey Allen K. Freitas, and Maqsudul AlamChapter 10Oxygen-Sensing Histidine-Protein Kinases: Assays of Ligand-Binding and Turnover of Response-Regulator SubstratesMarie-Alda Gilles-Gonzalez, Gonzalo Gonzalez, Eduardo H. S. Sousa, and Jason TuckermanChapter 11Reactions of nitric oxide and oxygen with FNR (regulator of Fumarate and Nitrate Reduction), a global transcriptional regulator, during anaerobic growth of Escherichia coliJason C. Crack, Nick E. Le Brun, Andrew J. Thomson, Jeffrey Green and Adrian J. JervisChapter 12Genome wide identification of binding sites for the nitric oxide sensitive transcriptional regulator NsrR. Sam Efromovich, David Grainger, Diane Bodenmiller, and Stephen Spiro.Chapter 13Methods in Enzymology: Globins and other NO-reactive proteins. Characterization of the NO-reactive transcriptional activator NorR.Benoît D’Autréaux, Nick Tucker, Stephen Spiro and Ray DixonSection III. Advanced Spectroscopic MethodsChapter 14Hemoglobins from Mycobacterium tuberculosis and Campylobacter jejuni: A Comparative Study with Resonance Raman Spectroscopy Changyuan Lu, Tsuyoshi Egawa, Masahiro Mukai, Robert K. Pooleand Syun-Ru YehChapter 15The power of using continuous-wave and pulsed electron paramagnetic resonance methods for the structure analysis of the ferric forms and NO-ligated ferrous forms of globins.Sabine Van Doorslaer and Filip DesmetChapter 16Oxygen binding to haem proteins in solution, encapsulated in silica gels and in the crystalline stateLuca Ronda, Stefano Bruno, Serena Faggiano, Stefano Bettati and Andrea MozzarelliChapter 17Characterization of ligand migration mechanisms inside haemoglobins from the analysis of geminate rebinding kineticsStefania Abbruzzetti, Stefano Bruno, Serena Faggiano, Luca Ronda, Elena Grandi, Andrea Mozzarelli, Cristiano ViappianiChapter 18Ligand Dynamics in Heme Proteins Observed by Fourier Transform Infrared Spectroscopy at Cryogenic TemperaturesKarin Nienhaus, G. Ulrich NienhausChapter 19Time-resolved x-ray crystallography of heme proteinsVukica Šrajer and William E. Royer, JrChapter 20Structural Dynamics of MyoglobinMaurizio Brunori, Dominque Bourgeois and Beatrice ValloneChapter 21Use of the Conjugate Peak Refinement Algorithm for Identification of Ligand Binding Pathways in GlobinsStephen D. Golden and Kenneth W. OlsenChapter 22Finding gas migration pathways in proteins using implicit ligand samplingJordi Cohen, Kenneth W Olsen, and Klaus SchultenChapter 23Identification of Ligand Binding Pathways in Truncated Hemoglobins Using Locally Enhanced Sampling Molecular DynamicsStephen D. Golden and Kenneth W. Olsen