Less Common Metals in Proteins and Nucleic Acid Probes

244 Pages·1998·17.14 MB·English

by  Michael J. Maroney

29
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Editorial Board:
M. J. Clarke-J. B. Goodenough
.C K. Jorgensen. D. M. P. Mingos" .G A. Palmer
P. J. Sadler. R. Weiss" R. J. P. Williams
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New York
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Budapest
Hong Kong
London
Milan
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sseL Common Metals ni Proteins
dna Nucleic Acid seborP
Volume Editor: M. .J Clarke
With Contributions by
.C .B Allan, .G Davidson, .J Figlar,
W. .R Harris, .J M. Kelly,
A. Kitsch De Mesmaeker, M. .J Maroney,
.C Moucheron, .S .J Nieter Burgmayer
r e g n~ i r p S
In references Structure and Bonding is abbreviated
Struct.Bond. and is cited as a journal.
Springer www home page: HTTP://www.springer.de
ISSN 0081-5993
ISBN 3-540-63925-X
Springer-Verlag Berlin Heidelberg New York
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Volume Editor
Prof. M. J. Clarke
Merkert Chemistry Center
Boston College
2609 Beacon St. Chestnut Hill
Massachusetts 02167-3860, USA
E-maih [email protected]
Editorial Board
Prof. Michael .J Clarke Prof. John .B Goodenough
Merkert Chemistry Center Center of Materials Science and Engineering
Boston College University of Texas at Austin
2609 Beacon .tS Chestnut Hill Austin, Texas 78712, ASU
Massachusetts 02167-3860, USA E-maih ,liam@hguonedoogj utexas.edu
E-mail: ude.cb@ekralC
Prof. David .M .P Mingos
Prof. Christian .K orgensen Chemistry Department
D~partment de Chimie Minerale Imperial College of Science
de l'Universit~ Technology and Medicine
Section de Chimie - Sciences II South Kensington
03 quai Ernest Ansermet London 7WS 2AY, Great Britain
CH-1211 Gen~ve ,4 Switzerland E-mail: [email protected]
Prof. Graham A. Palmer Prof. Peter .J Sadler
Department of Biochemistry Department of Chemistry
Wiess School of Natural Sciences The University of Edinburgh
Rice University Joseph Black Chemistry Building
P.O. Box 2981 King's Building, West Mains Road
Houston, Texas 77251, USA Edinburgh EH9 3JJ, Great Britain
E-mail: UDE.ECIR.YFFAT@MAHARG E-maih [email protected] uk
Prof. Raymond Weiss Prof. Robert .J .P Williams
Institut eL leB Inorganic Chemistry Laboratory
Laboratoire de Cristallochimie University of Oxford
et de Chimie Structurale Oxford 1XO 3QR, Great Britain
4, rue Blaise Pascal E-mail: ,[email protected] uk
F-67070 Strasbourg Cedex, France
E-maih [email protected]
ecaferP
Bioinorganic chemistry encompasses both naturally occurring metal ions and
the use of metal complexes as probes of biological systems. Some of the more
interesting elements in the chemistry of life are the less commonly occurring
ones such as nickel and molybdenum. This volume elucidates the chemistry of
these elements in important enzymes and also explores the chemistry of new
probes of biological structure and function.
In proteins, Ni may serve as either a Lewis acid or redox center. Nature has
evolved ways of acquiring, transporting and incorporating Ni into a wide
variety of proteins, including: ureases, hydrogenases, carbon monoxide
dehydrogenases, acetyl coenzyme A synthases, methyl coenzyme M reductases
and superoxide dismutases. In his chapter on nickel proteins, Mike Maroney
provides a survey of the bioinorganic chemistry of this element beginning with
its uptake in bacteria. Drawing on recent crystal structures of Ni proteins, he
then affords a better understanding of Ni-active sites at the mechanistic level.
Pterins display multi-electron redox reactivity in biological systems. They
are also curiously tethered to Mo in a number of vital enzymes. When non-
innocent pterins combine with transition metal ions, which also display multi-
electron redox activity, the result challenges the chemist's traditional concepts
of oxidation state. Sharon Burgmayer explores the chemistry of the pterin
complexes with Mo and other elements (Fe, Cu, Ru) along with the chemistry
of the closely related flavins in an effort to determine the possible interactions
between these multi-redox active partners in biological systems.
Transferrin normally transports iron in the blood, but in serum is only
partially saturated with iron. This enables this protein to also bind and
transport significant concentrations other metal ions. Wes Harris's review
emphasizes metals for which transferrin appears to play a significant role in
+4
serum transport. These include highly toxic metal ions such as Pu and others
such as Ga 3+ and In 3+ , whose biodistribution is important in the chemistry of
radiopharmaceutical agents.
Targeting DNA with transition metal probes has become an area of
widespread research interest. Much of this has been engendered by the longer-
lived excited states displayed by some metal polypyridyl complexes when
bound to DNA. Conversely, for other polypyridyl complexes, the excited state
may be quenched by electron transfer involving the nucleobases. Such
photochemical interactions can result in oxidative damage, photocleavage and
the formation of covalent photoadducts between the metal complexes and the
VIII ecaferP
nucleobases. John Kelly considers design strategies necessary to generate
molecular DNA photoprobes for DNA sequences or structures of particular
biological interest.
Taken as a whole, this volume illustrates new directions for traditional
protein biochemists, molecular biologists endeavoring to discover new ways to
probe DNA, and those engaged in the design of metallopharmaceuticals.
Michael .J Clarke
stnetnoC
The Structure and Function of Nickel Sites in Metalloproteins
M. J. Maroney, G. Davidson, C. .B Allan, J. Figlar ................
Electron Transfer in Transition Metal-Pteridine Systems
S. .J Nieter Burgmayer .................................... 67
Binding and Transport of Nonferrous Metals by Serum Transferrin
W. R. Harris ........................................... 121
Photophysics and Photochemistry of Metal Polypyridyl
and Related Complexes with Nucleic Acids
C. Moucheron, A. Kirsch-De Mesmaeker, .J M. Kelly .............. 361
Author Index Volumes 1-92 ............................... 217
Contents of Volume 88
Metal Sites ni Proteins dna Models
Iron sertneC
Volume Editor. P. J. Sadler
Polyiron Oxides, Oxyhydroxides and Hydroxides
as Models for Biomineralisation Processes
A. .K Powell
Heme: The Most Versatile Redox Centre in Biology?
.S .K Chapman, .S Daft, A. W. Munro
Rationalisation of Metal-Binding to Transferrin: Prediction
of Metal-Protein Stability Constants
H. Sun, M. .C Cox, H. Li, P. .J Sadler
Metal Centres of Bacterioferritins or Non-Heam-Iron-Containing
Cytochromes bss7
N. .E Le Brun, A. .J Thomson, .G R. Moore
Ribonucleotide Reductases - A Group of Enzymes with Different
Metallosites and a Similar Reaction Mechanism
B.-M. Sj6berg
Protein Engineering of Cytochrome m P450ca
L.-L. Wong, A. .C .G Westlake, D. P. Nickerson