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The Biological Chemistry of Iron: A Look at the Metabolism of Iron and Its Subsequent Uses in Living Organisms Proceedings of the NATO Advanced Study Institute held at Edmonton, Alberta, Canada, August 13 – September 4, 1981 PDF

510 Pages·1982·14.09 MB·English
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Preview The Biological Chemistry of Iron: A Look at the Metabolism of Iron and Its Subsequent Uses in Living Organisms Proceedings of the NATO Advanced Study Institute held at Edmonton, Alberta, Canada, August 13 – September 4, 1981

The Biological Chemistry of Iron NATO ADVANCED STUDY INSTITUTES SERIES Proceedings of the Advanced Study Institute Programme, which aims at the dissemination ofa dvanced knowledge and the formation of contacts among scientists from different countries The series is published by an international board of publishers in conjunction with NATO Scientific Affairs Division A Life Sciences Plenum Publishing Corporation B Physics London and New York C Mathematical D. Reidel Publishing Company and Physical Dordrecht, Boston and London Sciences D Behavioural and Social Sciences Martinus Nijhoff Publishers E Engineering and The Hague, London and Boston Materials Sciences F Computer and Springer Verlag Systems Sciences Heidelberg G Ecological Sciences Series C - Mathematical and Physical Sciences Volume 89 - The Biological Chemistry of Iron The Biological Chemistry of Iron A Look at the Metabolism of Iron and Its Subsequent Uses in Living Organisms Proceedings oft he NATO Advanced Study Institute held at Edmonton, Alberta, Canada, August 23 -September 4, 1981 edited by H. BRIAN DUNFORD Dept. of Chemistry, University ofA lberta, Edmonton, Canada DA VID DOLPHIN Dept. of Chemistry, University of British Columbia, Vancouver, Canada KENNETH N. RAYMOND Dept. of Chemistry, University of California, Berkeley, U.S.A. and LARRY SIEKER Dept. ofM olecular Structure, University of Washington, Seattle, U.S.A. D. Reidel Publishing Company Dordrecht: Holland / Boston: U.S.A. / London: England Published in cooperation with NATO Scientific Affairs Division library of Congress Cataloging in Publication Data NATO Advanced Study Institute (1981: Edmonton, Alta.) The biological chemistry of iron. (NATO advanced study institute series. Series C, mathematical and physical sciences, v. 89) Includes index. 1. Iron proteins-Congresses. 2. Iron-Metabolism- Congresses. I. Dunford, H. Brian. II. North Atlantic Treaty Organization. Division of Scientific Affairs. III. Title. IV. Series. QP552.l67N37 1981 574.19'214 82-9843 ISBN-13: 978-94-009-7884-3 e-ISBN-I3: 978-94-009-7882-9 DOl: 10.1007/978-94-009-7882-9 Published by D. Reidel Publishing Company P.O. Box 17,3300 AA Dordrecht, Holland Sold and distributed in the U.S.A. and Canada by Kluwer Boston Inc., 190 Old Derby Street, Hingham, MA 02043, U.S.A. In all other countries, sold and distributed by Kluwer Academic Publishers Group, P.O. Box 322, 3300 AH Dordrecht, Holland D. Reidel Publishing Company is a member of the Kluwer Group All Rights Reserved Copyright ¢) 1982 by D. Reidel Publishing Company, Dordrecht, Holland Softcover reprint of the hardcover 1st edition 1982 No part of the material protected by this copyright notice may be reproduced or utilized in any form or by any means, electronic or mechanical, including photocopying, recording or by any informational storage and retrieval system, without written permission from the copyright owner CONTENTS PREFACE ix SECTION A. INTRODUCTION H. Allen o. Hill IRON: AN ELEMENT WELL-FITTED FOR ITS TASK? 3 Ralph G. Wilkins SUBSTITUTION AND ELECTRON TRANSFER IN METAL COMPLEXES - PARTICULARLY THOSE OF IRON 13 Christopher A. Reed OXIDATION STATES, REDOX POTENTIALS AND SPIN STATES 25 SECTION B. IRON METABOLISM Robert R. Crichton FERRITIN-THE STRUCTURE AND FUNCTION OF AN IRON STORAGE PROTEIN 45 Philip Aisen CHEMISTRY AND PHYSIOLOGY OF THE TRANSFERRINS 63 Kenneth N. Raymond and Thomas P. Tufano COORDINATION CHEMISTRY OF THE SIDEROPHORES AND RECENT STUDIES OF SYNTHETIC ANALOGUES 85 Gunther Winkelmann SPECIFICITY OF SIDEROPHORE IRON UPTAKE BY FUNGI 107 B.R. Byers, C.V. Sciortino, P. Cox and P. Robinson IRON UPTAKE AND INTRACELLULAR IRON DISTRIBUTION IN CULTURED RAT HEART CELLS: EFFECTS OF IRON CHELATORS 117 SECTION C. SOME PROPERTIES OF THE CYTOCHROMES A.V. Xavier, I. Moura, J.J.G. Moura, M.H. Santos and J. Vi11a1ain NMR STUDIES OF LOW-SPIN CYTOCHROMES 127 ~ CONTENTS SECTION D. EXAMPLE OF AN OXYGEN CARRIER Patricia C. Harrington, Ralph G. Wilkins, Barry B. Muhoberac and David C. Wharton SUBSTITUTION AND ELECTRON TRANSFER PROCESSES IN HEMERYTHRIN 145 L.C. Sieker, R.E. Stenkamp and L.H. Jensen THE ENVIRONMENT OF THE BINUCLEAR IRON COORDINATION COMPLEX IN METHEMERYTHRIN 161 SECTION E. IRON-SULFUR CLUSTERS AND ENZYMES Isabel Moura and Jose J.G. Moura SIMPLE IRON-SULFUR PROTEINS: METHODOLOGY FOR ESTABLISHING THE TYPE OF CENTER 179 H.J. Grande, C. van Dijk, W.R. Dunham and C. Veeger CATALYSIS BY HIGHLY ACTIVE 12Fe-12S CONTAINING HYDROGENASES 193 Jean LeGa11 and Harry D. Peck Jr. HYDROGENASES: PHYSIOLOGY, LOCATION AND RELEVANCE FOR SULFATE REDUCING AND METHANE FORMING BACTERIA 207 A. Braaksma, H. Grande, H. Haaker, C. Laane and C. Veeger GENERATION, TRANSPORT AND TRANSFER OF LOW-POTENTIAL REDUCING EQUIVALENTS IN NITROGENASE CATALYSIS 223 B.H. Huynh, E. Munck and W.H. Orme-Johnson MOSSBAUER AND EPR EVIDENCE ON THE PROSTHETIC GROUPS OF THE MoFe PROTEIN 241 SECTION F. HEME MODEL SYSTEMS W. Robert Scheidt MAGNETIC COMPLEXITIES IN PORPHINATOIRON(III) COMPLEXES 261 Philip George, Charles W. Bock and Mendel Trachtman THE EVALUATION OF STABILIZATION ENERGIES (EMPIRICAL RESONANCE ENERGIES) FOR BENZENE, PORPHINE AND [18] ANNULENE FROM THERMOCHEMICAL DATA AND FROM AB INITIO CALCULATIONS 273 David Dolphin MODELS FOR PEROXIDASE AND CYTOCHROME P-450 ENZYMES 283 CONTENTS Gilda Loew, Dale Spangler and Andrew Pudzianowski STRUCTURE AND SPECTRA OF STABLE AND TRANSIENT STATES AND MECHANISMS OF OXIDATION OF MODEL CYTOCHROME P-450 295 C.K. Chang HEMES OF HYDROPORPHYRINS 313 SECTION G. HEME ENZYMES H.B. Dunford, T. Araiso, D. Job, J. Ricard, R. Rutter, L.P. Hager, R. Wever, W.M. Kast, R. Boelens, N. E11fo1k and M. Ronnberg PEROXIDASES 337 Gerd N. LaMar, V.P. Chacko and Jeffrey S. de Ropp THE STATE OF PROTONATION OF THE PROXIMAL HISTIDYL IMIDAZOLE IN HORSERADISH PEROXIDASE 357 Teizo Kitagawa and Junji Teraoka COORDINATION CHARACTERISTICS OF PROXIMAL HISTIDINE OF PLANT PEROXIDASES AND THEIR RELEVANCE TO THE HEME-LINKED IONIZATION 375 Brian M. Hoffman COMPOUNDS I OF HORSERADISH AND YEAST CYTOCHROME C PEROXIDASES 391 G.C. Wagner and I.C. Gunsa1us CYTOCHROME p450: STRUCTURE AND STATES 405 V. Ullrich, H.J. Ahr, L. Castle, H. Kuthan, W. Nastainczyk and H.H. Ruf CYTOCHROME p450 AS A REDUCTASE AND OXENE TRANSFERASE: WHICH IS ITS CHARACTERISTIC FUNCTION? 413 Peter Jones CATALASES AND IRON-PORPHYRIN MODEL SYSTEMS: ROLES OF THE COORDINATION ENVIRONMENT OF IRON IN CATALYTIC MECHANISMS 427 M.R.N. Murthy, T.J. Reid III, A. Sicignano, N. Tanaka and Michael G. Rossmann THE STRUCTURE OF BEEF LIVER CATALASE 439 Howard S. Mason THE SUBUNITS OF CYTOCHROME C OXIDASE 459 viii CONTENTS Robert A. Scott EXTENDED X-RAY ABSORPTION FINE STRUCTURE OF THE COPPER SITES IN CYTOCHROME C OXIDASE 475 LIST OF PARTICIPANTS 485 AUTHOR INDEX 491 SUBJECT INDEX 493 PREFACE The results of a NATO Advanced Study Institute (ASI) entitled "Coordination Chemistry Environments in Iron-Containing Proteins and Enzymes - Including Smaller Molecules and Model Systems" are summarized in this book. The ASI was held in the Province of Alberta, Canada, from August 23 to September 4, 1981. The first half of the conference was held on the campus of the University of Alberta, Edmonton, and the second half at the Overlander Lodge, Hinton. Two other conferences had the greatest impact upon the planning for this ASI. One was a NATO ASI held in Tomar, Portugal in September of 1979, entitled "Metal Ions in Biology". Among the organizers for that conference were Allen Hill and Antonio Xavier; we are happy to acknowledge their beneficial influence on our subsequent conference. The other most influential conference was one organized by Ralph Wilkins and Dennis Darnell entitled "Methods for Determining Metal Ion Environments in Proteins" which was held in Las Cruces, New Mexico, U.S.A., January 10-12, 1979. The Las Cruces conference invited lectures were published as Volume 2 of "Advances in Inorganic Biochemistry", G. Eichhorn and L. Marzilli, editors. Most of the physical techniques used to probe metal ion environ- ments are eloquently described in the latter volume. The under- signed organizers for the Alberta ASI made two decisions which shaped its format: first, to narrow the scope of "Metal Ions in Biology" to iron-containing systems. Second, to emphasize a description of the results obtained by investigation of the biological systems, and not the physical techniques used to probe the systems. One exception is Mossbauer spectroscopy, a technique not described in the proceedings of the Las Cruces conference, which is uniquely suited to iron-containing systems. This volume contains an excellent description of both the technique and the type of results which can be obtained from it. The title of this book "The Biological Chemistry of Iron" is simplicity itself. It also is misleading, because justice to the title would require a monumental multivolume series. Nevertheless, we have used it for the sake of brevity. To the best of our knowledge this volume is the first to attempt to describe in some detail both sides of the story of the biology of iron. One side is the gathering of iron, its storage and transport, in other words the metabolism of iron. The other is the utilization of the iron by living systems. Most animal systems use most of their iron to transport or store oxygen. Myoglobin and hemoglobin immediately come to mind. However, these molecules have been intensively studied and well ix H. B. Dunford et al. (eds.), The Biological Chemistry ofI ron, ix-xii. Copyright © 1982 by D. Reidel Publishing Company. x PREFACE described elsewhere (see for example "Hemoglobin and Myoglobin in their Reactions with Ligands" by E. Antonini and M. Brunori, North-Holland, Amsterdam - a book which is still of great value although it was published in 1971. We do not mean to imply that research on these molecules is anywhere near complete.) There are many references to hemoglobin in this volume, but we describe in detail a less well-known oxygen transport molecule, hemerythrin. Another well known heme protein, cytochrome c is discussed briefly, but we have concentrated more on the remark- able four-heme molecule cytochrome c3. With these types of decisions the conference was held to a viable two week format. Most of our interest centered on iron-containing enzymes and model systems, as essential for aerobic life as oxygen transport. It would appear that we may be approaching the point where we have enough structural and mechanistic information to elucidate completely the mechanism of an enzyme reaction. One may judge for oneself how well the criteria of complete mechanistic information as defined by biologists, chemists and/or physicists are being met for the enzymes discussed in this volume. Many important iron enzymes are not discussed; it was our concern to obtain some depth for which we paid a price in breadth of coverage. The participants at the conference ranged from graduate students to senior investigators, from theoretical chemists to medical doctors, from microbiologists to physicists. The mix of participants was truly interdisciplinary providing an accurate match to the types of research required to push back the research frontier on the biological chemistry of iron. This book is organized in sections which we describe briefly. Speakers (as distinct from coauthors) are also listed. Section A, the introduction, contains the keynote lecture by Allen Hill. It also contains two lectures which were organized as an "inorganic chemistry teach-in" to review the basic principles of inorganic and physical chemistry which must apply equally to non-biological and biological iron. The first, by Ralph Wilkins, describes ligand reaction dynamics. The second, by Chris Reed, discusses the influence of structure, spin state, ligand equilibria, coordination number, redox potential and oxidation state. The remainder of the book might be summarized as follows. It is concerned with the elucidation of ways in which the biological environment and the iron (or in'a few cases, copper or molybdenum) influence each other according to the basic principles of physics and chemistry. Iron metabolism is summarized in Section B. Robert Crichton describes the iron storage protein, ferritin. The iron transport protein, transferrin, is the topic of Philip Aisen. Ken Raymond

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