Few problems in protein biochemistry have proven to be as challenging and recalcitrant as the molecular description of nitrogenase, the catalyst of one of the most remarkable chemical transformations in biological systems: the nucleotide-dependent reduction of atmospheric dinitrogen to bioavailable ammonia. In "Nitrogen Fixation: Methods and Protocols," recognized experts in the field provide an up-to-date, in-depth overview of the methods that have been applied to studying the nitrogenase at a molecular level, ranging from genetic, biochemical, spectroscopic, and chemical methods to theoretical calculations. In addition, techniques used to study an enzyme system that is homologous to nitrogenase are described in this book. Written in the highly successful "Methods in Molecular Biology " series format, methods chapters include introductions to their respective chapters, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls.

Practical and cutting-edge, "Nitrogen Fixation: Methods and Protocols" will be useful for anyone interested in nitrogenase research and willing to venture further toward addressing the remaining mechanistic and biosynthetic questions of this fascinating enzyme system."

This volume highlights recent progress on the fundamental chemistry and mechanistic understanding of metallocofactors, with an emphasis on the major development in these areas from the perspective of bioinorganic chemistry. Metallocofactors are essential for all forms of life and include a variety of metals, such as iron, molybdenum, vanadium, and nickel. Structurally fascinating metallocofactors featuring these metals are present in many bacteria and mediate remarkable metabolic redox chemistry with small molecule substrates, including N2, CO, H2, and CO2. Current interest in understanding how these metallocofactors function at the atomic level is enormous, especially in the context of sustainably feeding and fueling our planet; if we can understand how these cofactors work, then there is the possibility to design synthetic catalysts that function similarly.

Few problems in protein biochemistry have proven to be as challenging and recalcitrant as the molecular description of nitrogenase, the catalyst of one of the most remarkable chemical transformations in biological systems: the nucleotide-dependent reduction of atmospheric dinitrogen to bioavailable ammonia. In Nitrogen Fixation: Methods and Protocols, recognized experts in the field provide an up-to-date, in-depth overview of the methods that have been applied to studying the nitrogenase at a molecular level, ranging from genetic, biochemical, spectroscopic, and chemical methods to theoretical calculations. In addition, techniques used to study an enzyme system that is homologous to nitrogenase are described in this book. Written in the highly successful Methods in Molecular Biology (TM) series format, methods chapters include introductions to their respective chapters, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and tips on troubleshooting and avoiding known pitfalls. Practical and cutting-edge, Nitrogen Fixation: Methods and Protocols will be useful for anyone interested in nitrogenase research and willing to venture further toward addressing the remaining mechanistic and biosynthetic questions of this fascinating enzyme system.

This volume highlights recent progress on the fundamental chemistry and mechanistic understanding of metallocofactors, with an emphasis on the major development in these areas from the perspective of bioinorganic chemistry. Metallocofactors are essential for all forms of life and include a variety of metals, such as iron, molybdenum, vanadium, and nickel. Structurally fascinating metallocofactors featuring these metals are present in many bacteria and mediate remarkable metabolic redox chemistry with small molecule substrates, including N2, CO, H2, and CO2. Current interest in understanding how these metallocofactors function at the atomic level is enormous, especially in the context of sustainably feeding and fueling our planet; if we can understand how these cofactors work, then there is the possibility to design synthetic catalysts that function similarly.