The 17th International Conference on Cytochrome P450 Biochemistry, Biophysics and Structure (ICCP450) was held in Manchester, UK, from 26 to 30 June 2011. This long running conference series focuses on the various roles of cytochromes P450 (P450s) in biochemistry, physiology and biotechnology, and brings together researchers from all over the globe to review progress in understanding aspects of P450 structure, reaction mechanisms and catalytic properties. This special issue of FEBS J is dedicated to the Manchester ‘P450 2011’ meeting, and features a mixture of invited reviews and primary research papers from delegates that cover a range of topics, from the structural properties of human and microbial P450s and redox partners through to the synthesis of plant toxins and circadian expression of steroidogenic P450s in mammals. This diversity of biochemical form and function is a hallmark of the P450s, which are almost certainly the most versatile class of enzymes in terms of their substrate scope and the range of chemical transformations that they are able to catalyze.
The P450 2011 conference brought the ICCP450 to the UK for the first time since the inception of the series in 1976. P450 2011 followed successful ICCP450 conferences in Bled (Slovenia, 2007) and Okinawa (Japan, 2009), and preceded the return of ICCP450 to the USA with the 2013 conference in Seattle. P450 2011 honoured Professor Klaus Ruckpaul (Berlin) for his major contributions to understanding the P450 structure and mechanism, and also for his efforts in organizing (with Sinisi Maričić) the very first ICCP450 conference in Primosten, Croatia. Klaus’ efforts were not only pivotal in establishing the ICCP450 series, but also served to bring together scientists with common interests from both Eastern Bloc and Western nations. P450 2011 also honoured Professor Eric Johnson (Scripps Institute, La Jolla, CA) as Plenary Speaker for his groundbreaking contributions to the determination of crystal structures of mammalian P450 enzymes, which are all membrane-bound proteins. Also receiving the honours at P450 2011 was Natasha DeVore from Professor Emily Scott’s group at Lawrence, Kansas. Emily herself is a protégé of Eric Johnson and the mentor for Natasha DeVore, who was awarded the FEBS J Klaus Ruckpaul Award for the best poster at P450 2011, which featured her work aiming to determine the crystal structure of human CYP17A1, a key enzyme in the synthesis of androgens and a drug target in prostate cancer treatment. The award was made by Professor Tsuneo Omura, a true pioneer in the field of cytochrome P450, and co-author (with Professor Ryo Sato) of the 1962 paper that gave the P450s the name they still retain today. Of course, every good conference needs the reporting of a major scientific breakthrough in the field. P450 2011 had Mike Green (Penn State University) on stage to report that the hunt for the ‘holy grail’ was over – with his spectroscopic revelation of P450 compound I – the transient iron-oxo species considered to be the highly reactive species that performs the substrate oxidation (oxygen insertion) chemistry for which the P450s are most famous.
For all but an hour of the 5-day P450 2011 conference, Manchester forgot itself and the sun shone down on the great and good of the P450 research community. We look forward to more fine weather and the advances in the field to be reported in Seattle next year, and hope that readers will get a flavour of the high-quality, multidisciplinary science in the P450 area from the papers contained in this issue of FEBS J.
[Andrew Munro is Professor of Molecular Enzymology at the Manchester Interdisciplinary Biocentre (MIB, Faculty of Life Sciences), University of Manchester. He received his PhD from the University of Aberdeen (1991), and then undertook Postdoctoral studies at the University of Glasgow before holding a Royal Society of Edinburgh Research Fellowship at the University of Edinburgh. He held academic positions at the University of Strathclyde (Glasgow) and University of Leicester before moving to Manchester in 2005. His research interests include the structure/function and biotechnology of redox enzymes, with a particular focus on cytochromes P450 and their partner systems.]
[David Leys is Professor of Structural Biology at the Manchester Interdisciplinary Biocentre (MIB), University of Manchester. He received his PhD from the University of Ghent, Belgium (2000), and then undertook Postdoctoral research at the University of Edinburgh before holding a Royal Society University Fellowship at the Universities of Leicester and Manchester (since 2005). His research interests include structure/function relationships in macromolecules, particularly for redox enzyme systems. David and Andrew have collaborated extensively in studies of a range of bacterial cytochromes P450 and their associated redox systems.]