Marcela Ayala received her BSc (1997) in chemical engineering from the National Autonomous University of Mexico (UNAM). She obtained her PhD (Biochemical Science Program, 2002) under the guidance of Rafael Vazquez-Duhalt from UNAM. From 2002–2005, she worked as a scientist researcher at the Mexican Institute of Petroleum in the area of petroleum biotechnology. In 2005, she joined the Institute of Biotechnology (UNAM) where she is currently the head of the Redox Biocatalysis group. Her research interests revolve around understanding the catalytic mechanisms of oxidoreductases (peroxidases, laccases, halogenases, etc.), finding strategies to improve their operational stability as well as studying biotechnological applications in the environmental and material synthesis field.
Tim Bugg is Professor of Biological Chemistry at the University of Warwick. His academic career started at the University of Southampton in 1991, where his group studied enzymes involved in the bacterial degradation of aromatic compounds and enzymes involved in bacterial peptidoglycan assembly. Since moving to Warwick in 1999, his group has more recently studied enzymes involved in bacterial degradation of lignin, and the application of biocatalysis to convert lignin into renewable aromatic chemicals. He is the author of the undergraduate textbook Introduction to Enzyme and Coenzyme Chemistry.
H. Brian Dunford was born in Oyen, Alberta in 1927. He obtained his BSc (Alberta) in 1950 and his PhD (McGill) in 1954. His career in enzyme kinetics began with a sabbatical leave in the laboratory of Robert Alberty at the University of Wisconsin in 1965. He is Emeritus Professor of Biophysical Chemistry in the Department of Chemistry at the University of Alberta, Edmonton. He has worked with scientists from 26 countries, directed the research of 20 successful PhD candidates, and has ∼250 publications, mostly in peer-reviewed journals. He is the author of two earlier books on peroxidases, both published by John Wiley & Sons (1999 and 2010). He has held the positions of Associate Dean (Research) in the Faculty of Science and Associate V. P. (Research), both at the University of Alberta. He continues to pursue studies of the symbiotic relationship between electronic charge rearrangement and enzyme kinetics.
Oliver Einsle (b. 1970) studied biology in Konstanz, Germany, and then moved to the Max-Planck-Institute for Biochemistry in Martinsried, Germany, to work with Robert Huber and Peter Kroneck on cytochrome c nitrite reductase. In 2001, he joined the laboratory of Doug Rees at Caltech, USA, to study nitrogenase, and in 2003, he took on a position as junior professor for protein crystallography in Göttingen, Germany. Since 2008, he has been full professor of biochemistry in Freiburg, Germany, and director of the Institute of Biochemistry in the faculty of chemistry and pharmacy. His group has made seminal contributions to the structural and functional characterization of various metalloproteins, including nitrogenase and nitrous oxide reductase, but also multiheme cytochromes c. A second line of research is centered on the study of integral membrane proteins, in particular bacterial transporters and channels.
Dr Franzen is a professor of chemistry at North Carolina State University in Raleigh, North Carolina. He has broad research interests in physical chemistry, including multi-functional enzymes, drug delivery using plant virus vectors, nucleic acid photochemistry and mid-infrared plasmonic materials. He has collaborated with co-author Dr Ghiladi on dehaloperoxidase for 8 years, which has led to many of the insights published in this chapter. Dr Franzen acknowledges material assistance and collegial discussions with Drs Dawson and Lebioda who have kept the field of dehaloperoxidase active and vibrant with their contributions.
Hiroshi Fujii was born in Gifu, Japan, in 1962 and received a B. E. (1985) in industrial chemistry from Kanazawa University, and M. E. (1987) and PhD (1990) degrees from Kyoto University. He then became a research associate at Hokkaido University. In 1992, he moved to the University of Minnesota to carry out postdoctoral work with Prof. L. Que, Jr. He then returned to the Institute for Life Support Technology (Yamagata, Japan) as a chief scientist in 1994 before moving to the Institute for Molecular Science (Okazaki, Japan) as an associate professor in 1998. He has been at Nara Women's University (Nara, Japan) as a professor since 2014. His research interests focus on the molecular mechanism of metalloenzymes and metal catalysts that catalyze various oxidation reactions with oxygen activation.
Professor Tony Kettle is director of the Centre for Free Radical Research (CFRR) at the University of Otago, Christchurch, New Zealand. He gained his PhD in 1989 investigating how superoxide affects oxidant production by myeloperoxidase. His research is still largely focused on the enzymology of myeloperoxidase and its impact on host defense and inflammatory tissue damage. His research team in the CFRR has advanced the understanding of how the enzyme contributes to bacterial killing by neutrophils. They have also demonstrated how hypohalous acids and free radicals are produced during inflammation and cause tissue damage. In clinical investigations, they showed that chlorine bleach damages tissue during inflammation in rheumatoid arthritis, cystic fibrosis, asthma and cardiovascular disease. In collaboration with AstraZeneca, they identified potent inhibitors of myeloperoxidase that have potential as anti-inflammatory drugs. Professor Kettle has published more than 100 scientific papers. He is a fellow of the Royal Society of New Zealand and has received the Society for Free Radical Research (Australasia) Distinguished Service Award as well as the infamous “Iron Bolt award” from the Gordon Conference for Oxygen Radicals.
Peter Loewen was educated in the Department of Chemistry at the University of Alberta in Canada (1969) and completed postdoctoral training first at the University of Geneva, Switzerland, and subsequently at the Massachusetts Institute of Technology under the supervision of Nobel Laureate Gobind Khorana (1973). The remainder of his career has been in the Department of Microbiology at the University of Manitoba, Canada. He currently holds a Canada Research Chair in protein chemistry.
Lawrence J. Marnett, PhD, is a university professor, the director of the A. B. Hancock Jr. Memorial Laboratory for Cancer Research, Mary Geddes Stahlman Professor of Cancer Research, and professor of biochemistry, chemistry, and pharmacology. Marnett received his PhD in chemistry from Duke University in 1973 and did postdoctoral work at the Karolinska Institute and Wayne State University. He began his academic career at Wayne State University where he rose through the ranks to professor of chemistry. In 1989, he moved to Vanderbilt.
As a postdoctoral fellow, Marnett discovered the peroxidase activity of prostaglandin endoperoxide synthase (COX) and his laboratory has provided insights into the mechanism of action of this peroxidase. His current research program focuses on the role of the enzyme COX-2 in cancer and inflammation as well as on the role of lipid oxidation products in DNA damage and mutation. His group has used structure-based approaches in conjunction with medicinal chemistry to design selective cyclooxygenase-2 inhibitors as potential anti-inflammatory, cancer preventive, and imaging agents. He is the author of over 480 research publications and 14 patents. Included in the awards Marnett has received are the American Cancer Society Faculty Research Award, the Sigma Xi Research Award, an Outstanding Investigator Award and a MERIT Award from the National Cancer Institute, the Founders Award from the American Chemical Society Division of Chemical Toxicology, and the George and Christine Sosnovsky Award for Cancer Research from the American Chemical Society. He is a fellow of the American Association for the Advancement of Science and a fellow of the American Chemical Society.
Paul R. Ortiz de Montellano, whose full name is even longer, was awarded a BS degree by MIT and MS and PhD degrees by Harvard University. His doctoral work with E. J. Corey and Konrad Bloch, followed by postdoctoral work with Duilio Arigoni in Zürich at the ETH, provided the foundation for a career at the interface of chemistry and biology, with a particular focus on the mechanisms and inhibition of heme proteins. He is currently a professor at the University of California, San Francisco. Outside of chemistry, his current interests lie in the direction of Dante, Puccini, Piero della Francesca, and Primitivo.
Christian Obinger studied chemistry and biochemistry and performed his doctoral thesis (cyanobacterial cytochrome c oxidase) at the Institute of Physical Chemistry of the University of Vienna (Austria). In 1992 he switched to BOKU – University of Natural Resources and Life Sciences in Vienna. Here in 1999 he was promoted to Associate Professor (habilitation) for Biochemistry and in 2011 to Full Professor for Protein Biochemistry. He is interested in the structure–function relationships of heme-containing oxidoreductases including peroxidases, peroxidasins, catalases, chlorite dismutases and related systems. His research focuses on the impact of the protein matrix and post-translational modifications on catalytically relevant redox intermediates and electron-transfer reactions. He has published more than 170 SCI publications in this field.
Thomas L. Poulos received a PhD in Biology in 1972 at the University of California at San Diego (UCSD). He then moved to the chemistry department at UCSD for postdoctoral work in the protein crystallography lab of Joe Kraut. While at UCSD he solved the first heme enzyme crystal structure, cytochrome c peroxidase, and initiated work on P450s. In 1983, he was recruited to Genex Corp. in Gaithersburg MD where he held the position of Principal Research Scientist and then Director of Protein Engineering. It was during this time that he solved the first cytochrome P450 structure. In 1987, he moved to the University of Maryland where he was a professor of chemistry and director of the Center for Advanced Research in Biotechnology. In 1992, he moved to the Department of Molecular Biology and Biochemistry at UCI where he now holds the title of Chancellor's Professor and joint appointments in the departments of chemistry and pharmaceutical sciences. In 1991, he won the Presidential Meritorious Service Award from the University of Maryland, the Brodie Award from the American Society of Experimental Pharmacology and Therapeutics in 2004, the American Chemical Society Biochemistry Gordon Hammes Lectureship in 2014, and was elected a AAAS fellow in 2005. His primary research interests are in heme enzyme structure and function and structure-based drug design.
Emma Raven was born in Northamptonshire and obtained a BSc in chemistry from the University of Leicester. Her interest in metalloproteins originated during PhD studies at Newcastle University with the late Geoff Sykes. She subsequently moved to the University of British Columbia (Vancouver) to Grant Mauk's laboratory, where she worked on a number of heme-containing proteins. In 1994, to her everlasting surprise, she was offered a lectureship at the University of Leicester where she is currently Professor of Biological Chemistry.
Giulietta Smulevich was born in Florence, Italy. She graduated in pharmaceutical chemistry cum laude at the University of Florence in 1979 where she is currently Professor of Physical Chemistry. She has been a postdoctoral fellow and visiting scientist at Princeton University (1983–1992), a visiting professor at Rutgers University (USA) (1988), Concordia University (Canada) (1990), and external professor at the Department of Biotechnology, Aalborg University (DK) (2003–2008). Her research is in the area of biophysical chemistry and is mainly focused on understanding the interplay between structure, dynamics and functional properties of heme proteins, one of the most important classes of biomolecules. In particular, her research goal is to understand the role played by the key residues in the proximity of the heme cavity in order to decipher the structure–function relationship by using electronic and vibrational spectroscopic techniques (Raman and resonance Raman, SERS, and FTIR, UV-Vis). She is the author of more than 170 publications in international journals.
Professor Christine Winterbourn is an Auckland University chemistry graduate who received her PhD in biochemistry from Massey University and has a personal chair in the Pathology Department, University of Otago, Christchurch. She is a principal investigator in the Centre for Free Radical Research and leads a group investigating the biochemistry of free radical reactions and the involvement of oxidants and antioxidants in health and disease. Her work encompasses mechanisms of antioxidant defence, understanding how white blood cells kill bacteria, and free radical involvement in cardiovascular and respiratory diseases. Professor Winterbourn has published more than 300 scientific papers. As well as receiving the 2011 Royal Society of New Zealand Rutherford Medal, she has received the NZ Association of Scientists' Marsden Medal, Massey University 75th Anniversary Medal, Society for Free Radical Research (Australasia) Distinguished Service Award, University of Otago Distinguished Research Medal and Society for Free Radical Research (International) Lifetime Achievement Award. She is a fellow of the Royal Society of New Zealand and a companion of the NZ Order of Merit.