Metal-Carbon Bonds in Enzymes and Cofactors

Astrid Sigel has studied languages and was an editor of the Metal Ions in Biological Systems series (until Volume 44) and also of the Handbooks on Toxicity of Inorganic Compounds (1988), on Metals in Clinical and Analytical Chemistry (1994; both with H. G. Seiler) and on Metalloproteins (2001; with Ivano Bertini). Helmut Sigel is Emeritus Professor (2003) of Inorganic Chemistry at the University of Basel, Switzerland, and a previous editor of the MIBS series until Volume 44. He serves on various editorial and advisory boards, published over 300 articles on metal ion complexes of nucleotides, coenzymes, and other ligands of biological relevance, and lectured worldwide. He was named Protagonist in Chemistry (2002) by ICA (issue 339); among further honors are the P. Ray Award (Indian Chemical Society, of which he is also an Honorary Fellow), the Werner Award (Swiss Chemical Society), a Doctor of Science honoris causa degree (Kalyani University, India), appointments as Visiting Professor (e.g., Austria, China, Japan, UK) and Endowed Lectureships. Roland K. O. Sigel is Associate Professor (2009) of Inorganic Chemistry at the University of Z³rich, Switzerland,; from 2003 to 2008 he was endowed with a F÷rderungsprofessur of the Swiss National Science Foundation. He received his doctoral degree summa cum laude (1999) from the University of Dortmund, Germany, working with Bernhard Lippert. Thereafter he spent nearly three years at Columbia University, New York, USA, with Anna Marie Pyle (now Yale University). During the six years abroad he received several prestigeous fellowships from various sources, and he was awarded the EuroBIC Medal in 2008. His research focuses on the structural and catalytic role of metal ions in ribozymes, especially group II introns, and on related topics. He was also an editor of Volumes 43 and 44 of the MIBS series.

Chapter 1: ORGANOMETALLIC CHEMISTRY OF B12 COENZYMES; Chapter 2: COBALAMIN- AND CORRINOID-DEPENDENT ENZYMES; Chapter 3: NICKEL-ALKYL BOND FORMATION IN THE ACTIVE SITE OF METHYL-COENZYME M REDUCTASE; Chapter 4: NICKEL-CARBON BONDS IN ACETYL-COENZYME A SYNTHASES/CARBON MONOXIDE DEHYDROGENASES; Chapter 5: STRUCTURE AND FUNCTION OF [NiFe]-HYDROGENASES; Chapter 6: CARBON MONOXIDE AND CYANIDE LIGANDS IN THE ACTIVE SITE OF [FeFe]-HYDROGENASES; Chapter 7: CARBON MONOXIDE AS INTRINSIC LIGAND TO IRON IN THE ACTIVE SITE OF [Fe]-HYDROGENASE; Chapter 8: THE DUAL ROLE OF HEME AS COFACTOR AND SUBSTRATE IN THE BIOSYNTHESIS OF CARBON MONOXIDE; Chapter 9: COPPER-CARBON BONDS IN MECHANISTIC AND STRUCTURAL PROBING OF PROTEINS AS WELL AS IN SITUATIONS WHERE COPPER IS A CATALYTIC OR RECEPTOR SITE; Chapter 10: INTERACTION OF CYANIDE WITH ENZYMES CONTAINING VANADIUM, MANGANESE, NON-HEME IRON, AND ZINC; Chapter 11: THE REACTION MECHANISM OF THE MOLYBDENUM HYDROXYLASE XANTHINE OXIDOREDUCTASE: EVIDENCE AGAINST THE FORMATION OF INTERMEDIATES HAVING METAL-CARBON BONDS; Chapter 12: COMPUTATIONAL STUDIES OF BIOORGANOMETALLIC ENZYMES AND COFACTORS