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

510 Pages·1982·14.09 MB·English

by  H. Allen, O. Hill (auth.), H. Brian Dunford, David Dolphin, Kenneth N. Raymond, Larry Sieker (eds.)

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
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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
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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