New Approaches for Flavin Catalysis

<p>1. Methods for determining the reduction potentials of flavin enzymes<br>Shelbi L. Christgen, Sophia M. Becker and Donald F. Becker<br>2. Anaerobic methods for the transient-state study of flavoproteins: The use of specialized glassware to define the concentration of dioxygen<br>Graham R. Moran<br>3. Performing anaerobic stopped-flow spectrophotometry inside of an anaerobic chamber<br>Hannah Valentino and Pablo Sobrado<br>4. Chemical quenching and identification of intermediates in flavoenzyme-catalyzed reactions<br>Kalani Karunaratne and Tatiana V. Mishanina<br>5. On the use of noncompetitive kinetic isotope effects to investigate flavoenzyme mechanism<br>Kevin Francis and Giovanni Gadda<br>6. Isotopically labeled flavoenzymes and their uses in probing reaction mechanisms<br>Andreea I. Iorgu, Matthew J. Cliff, Jonathan P. Waltho, Nigel S. Scrutton and Sam Hay<br>7. Unraveling flavoenzyme reaction mechanisms using flavin analogues and linear free energy relationships<br>Christopher J. Thibodeaux, Wei-chen Chang and Hung-wen Liu<br>8. Vibrational spectroscopy of flavoproteins<br>James N. Iuliano, Jarrod B. French and Peter J. Tonge<br>9. Measuring electronic structure properties of flavins and flavoproteins by electronic stark spectroscopy<br>Robert J. Stanley and Cornelius van Galen<br>10. EPR spectroscopy on flavin radicals in flavoproteins<br>Daniel Nohr, Stefan Weber and Erik Schleicher<br>11. Applications of molecular modeling to flavoproteins: Insights and challenges<br>Emil Sjulstok, Ilia A. Solov'yov and Peter L. Freddolino<br>12. Exploring the sequence, function, and evolutionary space of protein superfamilies using sequence similarity networks and phylogenetic reconstructions<br>Janine N. Copp, Dave W. Anderson, Eyal Akiva, Patricia C. Babbitt and Nobuhiko Tokuriki<br>13. Structural methods for probing the interaction of flavoenzymes with oxygen and its surrogates<br>Raspudin Saleem-Batcha and Robin Teufel<br>14. Reduction midpoint potentials of bifurcating electron transfer flavoproteins<br>Anne-Frances Miller, H. Diessel Duan, Taylor A. Varner and Nishya M. Raseek<br>15. Investigations of two-component flavin-dependent monooxygenase systems<br>John M. Robbins and Holly R. Ellis<br>16. The styrene monooxygenase system<br>George T. Gassner<br>17. Flavin-N5-oxide intermediates in dibenzothiophene, uracil, and hexachlorobenzene catabolism<br>Sanjoy Adak and Tadhg P. Begley<br>18. Prenylated FMN: Biosynthesis, purification, and Fdc1 activation<br>Anna N. Khusnutdinova, Johnny Xiao, Po-Hsiang Wang, Khorcheska A. Batyrova, Robert Flick, Elizabeth A. Edwards and Alexander F. Yakunin<br>19. Heterologous production, reconstitution and EPR spectroscopic analysis of prFMN dependent enzymes<br>Stephen Marshall, Karl A.P. Payne, Karl Fisher, Deepankar Gahloth, Samuel S. Bailey, Arune Balaikaite, Annica Saaret, Irina Gostimskaya, Godwin Aleku, Huanming Huang, Stephen E.J. Rigby, David Procter and David Leys<br>20. Physical methods for studying flavoprotein photoreceptors<br>Estella F. Yee, Siddarth Chandrasekaran, Changfan Lin and Brian R. Crane</p>