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Book Review Principles of Nucleic Acid Structure. By W. Saenger

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That the rigid fulvalene bridging ligand can bind two
metal atoms in close proximity is well
As demonstrated by the synthesis of 2 , this has now also been
accomplished with the rarely investigated Zr"' complexes.
The potential of universally modifying such complexes by
replacement of the chloro ligands by other functionalities
is now receiving our active attention.
Received: November 12, 1985;
supplemented: December 18, 1985 [ Z 1534 IE]
German version: Angew. Chem. 98 (1986) 278
[ I ] K. I. Gell, T. V. Harris, J. Schwartz, lnorg. Chem. 20 (1981) 481.
[2] K. 1. Gell, J. Schwartz, J . Am. Chem. Soc. 103 (1981) 2687; G. Fochi, G.
Guidi, C. Floriani, J. Chem. Soc. Dalton Trans 1984, 1253; T. Cuenca,
P. Roya, J. Organornet. Chem. 293 (1985) 61; S. R. Wade, M. G. H.
Wallbridge, G. R. Willey, J. Chem. SOC.Dalton Trans. 1983, 2555.
[3] G. P. Pez, J. N. Armor, Ado. Organomet. Chem. 19 (1981) I : M. Bottrill,
P. D. Gavens. J. McMeeking in G. Wilkinson, F. G. A. Stone, E. W. Abel
(Eds.): Comprehensive Organometallic Chemistry, Vol. 3. Pergamon, Oxford 1982, p. 281.
141 Titanium complexes of fulvalenes: a) H. H. Brintzinger, J. E. Bercaw, J.
Am. Chem. Soc. 92 (1970) 6182; b) A. Davison, S. S. Wreford, ibid. 96
(1974) 3017; c) L. J . Guggenberger, F. N. Tebbe, ibid. 95 (1973) 7870; d)
ibrd. 98 (1976) 4137: e) J. J. Salzmann, P. Mosiman, Helv. Chim. Acta 50
(1976) 1831: f ) G. J. Olthof, J. Organomet. Chem. 128 (1977) 367: g) E.
G. Perevalova, 1. F. Urazowski, D. A. Lemenovskii, Y L. Slovokhotov,
Y. T. Struchkov, ibid. 289 (1985) 319.
[5] D. J. Cardin, M. F. Lappert, C. L. Raston, P. I. Riley in 0. Wilkinson, F.
G. A. Stone, E. W. Abel (Eds.): Comprehensive Organometallic Chemrstry. Vol. 3, Pergamon, Oxford 1982, p. 606.
16) A structure analogous to 2 has been proposed for [{Zrl(C5H4)(+
C<H,)J,J (n>2),''] although no mass spectrum could be obtained, and
cryoscopic molecular weight studies suggested a concentration-dependent oligomerization.
171 Experimental: A solution of 1 (1.17 g, 4 mmol) in toluene (50 mL) was
treated with 1% Na/Hg (0.138 g Na, 6 mmol) and stirred for 12 h under
nitrogen. The resultant dark red reaction mixture was then heated under
reflux for 8 h. After filtration, evaporation, and recrystallization from
toluene/n-hexane, the product was obtained as a dark red air-sensitive
powder. Yield: 0.76 g (75%). An analytically pure sample was obtained
by vacuum sublimation (lo-' torr). At ca. 120°C the 0x0 derivative 3
sublimed and pure 2 was obtained at 190"C.-Spectra: EI-MS: 2, M a
508; 3, M e 524: both molecular ions exhibit an isotopic pattern typical
of an ion containing a Zr2CIzmoiety.--IR of 3 (KBr, r;jZrOZr), cm-'):
735 s a n d 702 s.-NMR (270 MHz, C6Da, 34°C): 2 : 'H:6=5.57 (s, IOH,
C,H,), 4.93 (pseudotriplet, 4 H), and 3.97 (pseudotriplet, 4 H). The pseudotriplets arise from an AA'BB' spin system with J,,,=JAB.=2.7 Hz.''C: 6= 104.7 (CsH5), 104.6 and 101.1 (C2, C3), 106.2 (Cl).-3: ' H (270
MHz,CDCI1, +28"C): 6=6.27 (s, lOH, C5H5),6.7S (m*, 2H),6.56 (M*,
2 H), 6.32 ( m a , 2 H), 5.97 (m*, 2 H); m* = multiplets of an ABCD system.-"-'C- 6 = 114.2 (C,H,), 104.2, I 11.8, 113.7, 114.6 (C2-5), C I not observed.
181 B. A. Frenz et al.: SDP, Structure Determination Package. College Station, TX 77840 (USA). 3, pale yellow crystals (from toluene);
V z 2 5 8 3 . 9 ~10" pm', C2/c, 2 = 4 , FOo0=794,p= 1.59 g cm-', p = 10.2
cm - ' ;CAD-4 (Enraf Nonius), MaKn,graphite monochromator, w-scan
(A@=0.80" +0.30tgH, 2" G O < 227, I,,, = 60 S , h( - l6/ l6), k(O/ l3),
I(- 15/15), 1471 reflections ( I > lo(/)).-Solution of structure: Patterson and difference Fourier methods; all non-hydrogen atoms refined
anisotropically; H-atoms calculated from ideal geometry, included in
structure factor calculations, but not refined; R=0.046, Rw=O.OSS.Further details of the crystal structure determination are available on
request from the Fachinformationszentrum Energie, Physik, Mathematik GmbH, D-75 14 Eggenstein-Leopoldshafen 2, o n quoting the depository number CSD-51661, the names of the authors, and the full citation of the journal.
[9] S. Motherwell, PLUTO, Program for Plotting Molecules and Crystal
Structures. Cambridge (UK).
1101 J. F. Clarke, M. G. 8. Drew, Acta Crystallogr. B30 (1974) 2267.
[ I I] J. L. Peterson, J . Organornet. Chem. 166 (1979) 179, and references
[I21 K. P. C. Vollhardt, T. W. Weidman, Organometallrcs 3 (1984) 82: J. C.
Smart, C. J. Curtis, lnorg Chem. 16 (1977) 1788, and references therein.
Principles of Nucleic Acid Structure. By W. Saenger.
Springer Verlag, Berlin 1984. xx, 556 pp., bound, DM
79.00.-ISBN 3-540-90761-0
Wolfram Saenger has done a considerable service for
the community of scientists interested in nucleic acids with
the publication of his monograph "Principles of Nucleic
Acid Structure". The book is a rich compendium of information about the three dimensional properties of DNA,
RNA, and related compounds, with particular emphasis
on structure at the level of nucleosides and nucleotides.
The magnitude of the task can be appreciated by examination of the size of the reference list, which includes over
1400 items.
Particularly commendable features include the careful
definition of terms provided in Chapter 2, much needed in
a field beleaguered for years by competing systems of
nomenclature. The book states clearly the standard definitions recommended in 1983 by the IUPAC-IUB subcommission, and adheres to their use with high fidelity. The
same chapter includes a detailed description of the nomenclature of pseudorotation, which provides a systematic
scheme for describing the conformation of the ribose ring.
This is followed in Chapter 4 with an authoritative account
of the principles which underlie the preference for particular sugar ring puckers. The distinction between syn and
anti conformations of the base relative to the sugar ring is
also examined in detail, as are the principles which govern
the rotational orientations about P - 0 bonds.
Chapters 5 and 6 consider physical properties of the nucleic bases, such as charge densities, protonation and tautomerization equilibria, spectroscopic properties, and the
tendency to hydrogen-bond in solution. Stacking forces
and the thermodynamics of double helix formation are
also treated. These subjects are followed by a chapter detailing the properties of modified nucleotides, including
those of general biochemical interest such as the cyclic nucleotides and pyrophosphate-containing compounds.
The book devotes considerable space to several nicely
illustrated chapters describing the many possible helical
structures of nucleic acids, including the extensive polymorphism of DNA. Both crystallographic results and models built from fiber diffraction studies are presented in
some detail. Even some of the generally discredited models are dredged u p from the past, presumably to give a flavor of the nature of debate in the field.
Later chapters in the book will be found widely useful
for their structural account of subjects such as tRNA,
drug-DNA complexes, and the rapidly developing field of
protein-nucleic acid interactions. Included among the latter are some general principles of amino acid-nucleotide
interactions and the structural features underlying the interaction of ordered protein segments with nucleic acid
Angew. Chem. lnt. Ed. Engl. 25 (1986) No. 3
helices. Specific structures examined in detail include tobacco mosaic virus, specific DNA-binding proteins such as
CAP and cro, and nucleosomes.
The early chapters of the book are rather intensively
technical, and unfortunately lacking in general signposts,
so that the non-specialist reader will find the going rather
tortuous; the later chapters are significantly better in this
regard, and should be quite useful as reference material for
students and professionals alike in the fields of molecular
biology and biochemistry.
All research-level monographs contain errors, and this
one is no exception, although I did not find many. The
proofreading was generally very good, but a too-generous
sprinkling of double bonds around the purine and pyrimidine ring systems was allowed to sneak through in Chapter 2, which may confuse beginning students. The only error of principle which I feel obliged to mention is the incorrect treatment of the dissection of linking number into
twist and writhe. Both the text and the figures make it
seem that one can determine the writhe of a superhelical
structure simply by counting the number of superhelical
turns. This error (the writhe of a superhelix depends on its
pitch) sets back understanding of D N A topology substantially.
This is a valuable reference book, which should be on
the shelves of all who are interested in the structure and
function of nucleic acids.
Donald M . Crothers [hB 722 IE]
Department of Chemistry,
Yale University, New Haven (USA)
Bio-inorganic Chemistry. By R . W . Hay. Ellis Horwood,
Chichester 1984. 191 pp., stitched, $ 24.95.--ISBN 0470-20066-9
Inorganic biochemistry is in a turbulent state of development. An up-to-date introduction to this field which is
not only aimed at specialists is years overdue. Thus, Hay’s
book will encounter a n eagerly expectant public-and, to
come straight to the point, it is therefore particularly disappointing.
The introductory chapter, short and informative, is concerned with biologically essential metal ions, with their ligands in physiological media and with some of their
chemical characteristics that are relevant in this context.
Subsequently, the important physical methods of inorganic
biochemistry are described, necessarily by means of examples. Only the section on EXFAS, the most important of
the new sources of information for the investigation of metal binding in proteins, is more extensive.
Apart from a short (and adequate) chapter on the biochemistry of the alkali metals and alkaline earths, the book
is devoted to the r61e of the transition metals in biology.
Here, the reader is confronted with a lamentably disorganized collection of partly out-of-date information with very
arbitrary emphases and exclusions. To begin with the positive: the chapter on substrate-activating metalloenzymes
(carboxypepsidase, carboanhydrase and alcohol dehydrogenase) amounts to a n up-to-date, well thought out introduction. It is clear that the author’s own research interests
lie in this area. Unfortunately, in the case of carboanhydrase, of the many model systems examined, the most convincing one by Groves (1981) is missing. Equally well handled are oxygen fixation and iron-sulfur proteins-a considerable achievement in light of the abundance of proAngew. Chem. Int. Ed. Engl. 25 (1986) No. 3
teins with Fe-S clusters known today.
Set against this, the presentation of the theme “oxygen
transport” suffers from Hay’s after all very “inorganic”
viewpoint. The willful impression is conveyed that ironporphyrin can accomplish the transport perfectly well on
its own and that the protein is only a sort of packing. Hemoglobin itself is pushed into the background by the depth
and extent of the treatment of model systems and of the
(biochemically irrelevant) cobalt-oxygen complexes.
It becomes really annoying in the section on the fascinating catalytic properties of cytochromes of type P450.
These heme proteins “can” hydroxylate alkanes under
physiological conditions. In 1982 (for which year the book
claims to present the state of knowledge) much was already known about the mechanism responsible for this.
We are offered a random selection from the state of discussion around 1980; the r6les of the axially coordinated sulfur and of the active Fe-0 species are either quite wrongly
represented or simply not referred to. Cytochrome P450,
catalase and hemoglobin are three heme proteins whose
remarkably different interactions with oxygen are decisively determined by axial ligands of the heme iron: the
opportunity of a comparative discussion of these three is
let slip. This is particularly regrettable because in this case
“inorganic” and “biochemical” interests really have coalesced in ideal fashion to a genuine “bioinorganic” research area.
The biochemistry of iron in aerobic media offers the
chance of a sheer “exciting” account of how the insolubility of iron(ii1) hydroxide has been come to terms with. On
uptake, transport and storage, before and during its inclusion in functional proteins, the iron is kept in solution
through a seamless sequence of strong complexing agents.
Unfortunately, the few particulars on this are dotted right
through the whole book so that the connection is lost in
exotic detail and is not made very comprehensible. The
biochemistry of copper is equally unsystematically handled: a direct comparison of the three types of copper
binding centers in proteins is sought in vain; this certainly
does not facilitate the understanding of the not-yet-expert
(and the book is aimed at students!).
It only remains to be pointed out that one of the functionally most important and “bio-inorganically” interesting metallo-proteins-cytochrome-c-oxidase, currently the
subject of much research, receives no more than a passing
reference from the author. The purchase of this book can
be recommended to no-one-least of all its intended readership of advanced students.
Michael Weller [NB 700 IE]
VCH Verlagsgesellschaft, Weinheim (FRG)
Methods of Enzymatic Analysis. Vol. 6. Metabolites 1: Carbohydrates. Edited by H. U. Bergmeyer, .
and M . Grassl. 3rd Edition. Verlag Chemie, Weinheim
1984. xxix, 701 pp., bound, D M 295.00.--ISBN 3-52726046-3
This volume describes analyses for carbohydrates and
related compounds. The coverage is broad: from poly-,
oligo-, and disaccharides through monosaccharides to
three-, two-, and one-carbon compounds. The four chapters of this volume are subdivided into sections. Each section normally covers the analysis of a single metabolite, although, several metabolites which can be co-analyzed are
occasionally grouped together. Certain important com29 1
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