This second edition of Bioinorganic Chemistry: A Short Course adopts the
same philosophy as the fi rst — that is, chapters of introductory material followed
by chapters featuring detailed discussions of specifi c bioinorganic chemistry
topics. This approach foregoes any attempt to exhaustively survey the
enormous range of bioinorganic topics that occupy the attention and research
of theoreticians and experimentalists currently engaged in the fi eld. In this
second edition, introductory Chapters 1 and 2 cover inorganic chemistry essentials
and biochemistry fundamentals for bioinorganic chemistry students whose
background in these topics may be less than ideal. Chapter 3 (Instrumental
Methods) concentrates on the physical and analytical methods used to describe
the bioinorganic systems discussed in Chapters 5 through 7 . Chapter 4 (Computer
Hardware, Software, and Computational Chemistry Methods) describes
some of the vast array of computer hardware, software, and drawing, visualization,
computational, and modeling programs used by every researcher studying
bioinorganic systems. Computational chemistry, for instance, allows
researchers to predict molecular structures of known and theoretical compounds
and to design and test new compounds on computers rather than at
the laboratory bench. Chapter 5 (Group I and II Metals in Biological Systems:
Homeostasis and Group I Biomolecules) discusses the vital roles of sodium
and potassium ions in maintaining cellular integrity, and features the Nobel
Prize - winning work of Roderick MacKinnon ’ s research group on potassium
ion channels. More structural work by the MacKinnon group confi rming the
selectivity of potassium ion channels for K +
over Na +
can be found in a recent
Science magazine article ( Science 2006, 314 , 1004 – 1007). Chapter 6 (Group I
and II Metals in Biological Systems: Group II) describes the importance of
magnesium ions in catalytic RNA (ribozymes). Readers interested in the
“ RNA World hypothesis ” , a theory connecting the origin of life with self -
replicating ribozymes, will want to read the recent article by Michael Robertson
and William Scott ( Science 2007, 315 , 1549 – 1553). A background perspective
on this article has been written by Gerald Joyce ( Science 2007, 315 , 1507 – 1508).
In addition, Chapter 6 discusses two calcium - containing biomolecules —
calmodulin, a primary receptor for intracellular calcium ions and a switch in
Ca2+ - dependent signaling pathways, and Ca 2+ - ATPase, a major player in muscle
contraction - relaxation cycles. Chapter 7 (Iron Containing Proteins and
Enzymes) devotes much of its descriptive material to proteins and enzymes
that contain their iron ions within a heme ligand system. This chapter extends
the fi rst edition ’ s discussion of myoglobin and hemoglobin, then reports on
some members of the ubiquitous cytochrome family — cytochrome P450, a
monooxygenase, cytochrome b(6)f, a green plant constituent, bacteria - based
cytochrome bc 1 , members of the cytochrome c superfamily, and cytochrome c
oxidase (CcO), the terminal electron transferring enzyme in the mitochondrial
respiratory chain. An update reported recently by the Collman group ( Science
2007, 315 , 1565 – 1568) connects the redox - active centers of cytochrome c
oxidase — Fe a3 , Cu B , and tyr244 — to the rapid accumulation of four electrons.
The four accumulated electrons are needed to reduce dioxygen, O 2 , to two
oxide, O 2 − , ions while avoiding the production of partially reduced, tissue -
damaging superoxide, O 2
− • , or peroxide, O 2
2 − , ions. A shorter section in Chapter
7 discusses non - heme iron - containing proteins and enzymes, many of which,
like aconitase, feature iron - sulfur clusters. Lastly, Chapter 7 reports on the
enzyme methane monooxygenase (MMO), utilized by methanotrophic bacteria
to oxidize methane to methanol with incorporation of one O 2 oxygen
atom.