Journal of Organometallic Chemistry 628 (2001) 131– 132 www.elsevier.nl/locate/jorganchem
Book Review Advances in Inorganic Chemistry Heme –Fe Proteins, Vol. 51; A.G. Sykes, A.G. Mauk (Eds.); Academic Press, San Diego, 2001, xv+455 pages, ISBN 0-120-23651-6, US$ 130.00 Ad6ances in Inorganic Chemistry has been an indispensable reference for inorganic chemists for nearly half a century. There cannot be many inorganic chemists working today who have not consulted it at one time or another. Each volume contains about 10 specialist, but often diverse reviews covering the broad spectrum of inorganic chemistry. Occasionally the volume is devoted to a single specialist topic and in recent years this has followed the editor’s interest in bioinorganic chemistry. For instance, Vol. 47 was entirely devoted to contributions related to iron –sulfur clusters. The latest issue (Vol. 51) continues the bioinorganic theme and contains nine articles, all dedicated to heme –Fe proteins. Non-biological chemists should not be put off by the specialist nature of this volume. Many of the enzymes will be familiar even to the non-expert since they are now taught at the undergraduate level. Thus, there are articles on Myoglobin (E. Lloyd Raven and A.G. Mauk), Catalases (P. Nicholls, I. Fita and P.C. Loewen), Peroxidase (N.C. Veitch and A.T. Smith) and Cytochrome cd1 Nitrite Reductase (V. Fu¨lo¨p, N.J. Watmough and S.J. Ferguson). All these articles show the enormous explosion of structural and mechanistic information that has occurred in these areas in recent years. The volume also contains articles on some heme-containing proteins with which even some bioinorganic chemists will be less familiar. These include contributions on Hemopexin, which binds and transports Fe –porphyrins (W.T. Morgan and A. Smith), NO Synthase (T.L. Poulos, H. Li, C.S. Raman and D.J. Schuller), Nitrophorins, which are NO-releasing proteins stored in the saliva of certain blood-sucking insects to ensure that the insect gets a good meal (F.A. Walker and W.R. Montfort), and Heme Oxygenase (P.R. Ortiz de Montellano and A. Wilks). All eight of these articles focus on the enzymology of the various proteins with little discussion of the so-called model compounds. Attempts to build the entire active
site is an emerging theme in modelling metalloenzymes, and in the final article the de novo design of heme proteins (B.R. Gibney and P.L. Dutton) is described. Here the authors describe how designed polypeptides are used to mimic not only the coordination environment of the heme centre, but also the arrangement of other amino acid side chains contained within the active site cavity. After reading all the articles in this volume one is struck by how sophisticated is the understanding of the mechanisms of these proteins. In particular, key roles have been identified for amino acid side chains remote from the metal. This is a salutary lesson to those who think that just binding the correct type of ligands in the right coordination geometry to a metal ion constitutes ‘‘modelling’’ the active sites of enzymes. I enjoyed reading all the articles in this volume, but found two things disappointing. First, Heme Oxygenase was covered in the article by Poulos et al. and also in the article by Ortiz de Montellano et al. Although I appreciate that Heme Oxygenase is presented in each of these chapters from quite different perspectives (CO and NO as signalling molecules on the one hand, and degradative oxidation of heme to bilivendin on the other) nevertheless, the result is that the structural features of this enzyme are extensively duplicated. Secondly, there was no introduction to the volume. One goes straight from the contents list to the first article. Considering the diverse range of biological roles for heme –Fe proteins a short rationale why this group of articles had been selected would have helped to put the volume into context. That having been said, I found all the articles to be of the high standard expected of this series, but more than that, they are all easy to read. Certainly this is a volume which is targeted at a specialist audience, since the reader is exposed to detailed discussions such as protein folding, the application of recombinant DNA technology and even phylogenetic trees, with which most inorganic chemists are not very familiar. Nonetheless, even the pure organometallic or coordination chemist will, I believe, find the articles interesting.
0022-328X/01/$ - see front matter © 2001 Published by Elsevier Science B.V. PII: S 0 0 2 2 - 3 2 8 X ( 0 1 ) 0 0 7 2 1 - 5
The study of heme– Fe proteins is a mature area of research. However, the collection of nine articles in Vol. 51 of Ad6ances in Inorganic Chemistry shows that the use of contemporary genetic and structural biology techniques are allowing us to understand how this fascinating family of proteins accomplishes a diverse range of reactivities.
6 February 2001 R.A. Henderson Department of Chemistry, Uni6ersity of Newcastle, Newcastle-upon-Tyne NE1 7RU, UK