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Book Review Perspectives on Bioinorganic Chemistry Volume 1. Edited by R. W. Hay J. R. Dilworth and K. B

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and the reorganization energy. The authors also discuss ET
processes between proteins and inorganic complexes. in
modified proteins, and between different proteins.
J. G. Wright, M. J. Natan, F. M. MacDonnell, D. M. Ralston, and T. V. O’Halloran present a detailed review of the
state of mercury(r1)-thiolate chemistry. As a closely related
topic they describe the receptor MerR, which is specific for
Hg”; this DNA-binding protein controls the mechanism of
the detoxification of Hg” ions in certain bacteria.
Transition metal complexes can be used as probes for investigating nucleic acids, for example as a way of recognizing
different types of DNA, o r in sequencing. Metal complexes
are especially suitable for this purpose since they can react in
many different ways, have useful spectroscopic and electrochemical properties, and can if necessary have rigid structures with defined symmetry. This fascinating subject is covered by A. M. Pyle and J. K. Barton.
In the final article S. L. Bruhn, J. H. Toney, and S. J. Lippard discuss the structure and biochemistry of D N A molecules that have been modified by the action of platinum
compounds. As expected the main emphasis is o n the antitumor agent cisplatin, but the properties of the corresponding
frans compound are also discussed.
The experiment mentioned in the preface whereby the usual proofreading has been omitted, so as to produce a more
up-to-date text, is not without its adverse effects. Even without a systematic search, more than 30 printing errors were
noticed, of which more than 20 were in the article by J. G .
Wright et al. However, most of these were not very serious.
The figures are, with only a few exceptions, of good quality,
and the index is adequate.
The potential readership should particularly include advanced students. The idea of publishing the book in a (relatively!) cheap paperback version at the outset was a good
one. not only with students in mind. The advanced level of
treatment could present problems for the average student,
but despite this some of the chapters may be suitable as a
basis for student seminar discussions. In any case, however,
the students will first need to be familiar with the fundamentals of bioinorganic chemistry, for example through an introductory lecture course or from a textbook such as that by
Kaim and Schwederski (see above).
To summarize, everyone interested in the latest developments in bioinorganic chemistry is strongly recommended to
buy this book. I t is, in any case, a must for every departmental library.
Perspectives on Bioinorganic Chemistry, Volume 1. Edited by
R. W. Hrij., J. R. Dihrortli, and K . B. Nolan. JAI Press
Ltd.. London, 1991. XI. 284 pp.. hardcover $78.50 (in
North America).- ISBN 1-55938-1 84-1
The new series “Perspectives on Bioinorganic Chemistry”
aims t o present the current state of research in this field. The
first five volumes are already planned, and will appear a t
approximately yearly intervals, as implied by the subtitle of
Volume 1 : “A Research Annual”. This first volume contains
seven review articles varying in length from 26 to 51 pages.
The fact that the individual chapters are short and not very
broad in scope is perhaps a justification for the absence of an
index.
The first topic is the formation of complexes between
metal ions and peptides, reviewed by L. D. Pettit, J. E. Gregor. and H. Kozlowski. The article is arranged according to
the various metals. with particular emphasis on copper, and
the authors limit their treatment essentially to a factual
account in the style of the “Specialist Periodical Reports”.
However, this is not typical of the book as a whole. Surprisingly, there is no mention of the phytochelatins, a class of
plant peptides with an important role in the homeostasis of
metal ions.
In the second article T. H. Fife describes the action of
metal ions in catalyzing the hydrolysis of esters and amides,
starting with simple small-molecule systems and then going
on to the example of carboxypeptidase A. The author discusses kinetic and mechanistic aspects which are, of course,
intimately related to the structures of the complexes, substrates, and ligands.
There are already numerous reviews on the topic of “blue
copper proteins”, and the article here by S. K. Chapman is
therefore to be seen as updating the position. A description
of the structural and spectroscopic properties of the blue
copper centers is followed by a list of the individual proteins.
Lastly several special topics are covered, such as rutheniummodified proteins.
F. A. Armstrong contributes an article o n voltammetry of
metal centers in proteins. The versatile capabilities of this
technique, which has hitherto been viewed with some skepticism, are well described. Among other aspects, the special
importance of the electrode surfaces is emphasized. Of the
systems that have been investigated, iron-sulfur proteins
receive particular attention.
W. E. Smith and J. Reglinski report on the use of gold
compounds for the treatment of rheumatoid arthritis. After
briefly describing the nature of the disease and the clinical
aspects, the authors discuss the chemistry of gold compounds,
especially complexes with sulfur-containing ligands. The distribution of gold in living organisms, reactions with enzymes
and cells, clinical trials, and the mechanism of the therapeutic action are also discussed.
R. C. Hider and A. D. Hall deal with iron chelating agents
that can be used for therapeutic applications. The discussion
centers mainly on derivatives of 3-hydroxypyridin-4-one.
The first clinical tests on compounds of this class have yielded promising results. The work reported includes studies on
the mobilization of iron from proteins with transport and
storage functions.
In the final article R. R. Eady collects together information on nitrogenases that d o not depend on molybdenum.
The aspects reported on include the genetics of nitrogen fixation, the biochemistry of the nitrogenase, and the iron
proteins, VFe proteins, and FeFe proteins.
Some of the figures and formulas are unsatisfactory in
their quality and size. However, this criticism definitely does
not apply to the chapters by T. H. Fife and by R. C. Hider
and A. D. Hall. The incidence of factual and printing errors
is tolerably low. Some particularly noticeable examples are
as follows: on page 10 rubredoxin has an Fe,S, core; the
formulas given for the lysine side-chain on page 21 and for
serine on page 274 contain errors; on page 28 “Glu-CysGly” for glutathione is not strictly correct; in the discussion
of CH,Hg+ complexes on page 30, the stability constants
given are for Cd”; in Figure 5 on page 198 no unit is given
for the ordinate axis; Ref. [47] on page 208 gives the names
of the authors but not the journal; on page 280 the text refers
to Table 5, but this cannot be found.
On the basis of the quality of the contributions in this first
volume, the series “Perspectives on Bioinorganic Chemistry” should find a place in every relevant library. Research
groups with interests in bioinorganic chemistry are also recommended to buy the series.
Henrv Stuasdeii
Fachbereich Cheinie
der Universitat Oldenburg (FRG)
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