Chemistry of

complex compounds
07.03.2023
 A covalent bond is formed
when two atoms share
electrons. A coordinate
covalent bond, also known as a
dative covalent bond, is a type
of covalent bond in which the
shared pair of electrons comes
from one of the atoms.

The atoms are held

together because both of
the nuclei attract the
electron pair. Once the
covalent bond is formed,
it is impossible to
distinguish the origin of
the electrons.
Chemistry of complex compounds
◼ This kind of bond (coordinative covalent) is typically observed
in the bonding of metal ions to ligands. However, nonmetals
can also participate in this bonding. The reaction between
Lewis acid and base is a coordinate covalent bond.
◼ A complex ion is made of two things, a metal ion and
compounds called ligands.
◼ Ligands are neutral molecules or ions containing lone electron
pairs that can bond with the metal ion. Common ligands are
ammonia (NH3), water (H2O), and halide ions (Cl–, Br–). Ligands
are considered Lewis bases because they are sharing their
electron pairs with the metal ion.
◼ Metal ions are always positive, so they are quite attractive to
lone pairs of electrons.
Biologically Important Chelate Complexes
◼ A chelate is an organic compound formed when a
polydentate ligand bonds to a central metal atom.
◼ Chelation, according to the IUPAC, involves the
formation of two or more separate coordinate bonds
between the ligand and central atom. The ligands are
terms of chelating agents, chelants, chelators, or
sequestering agents.
Summary
◼ Ligand and chelate are related terms that
are discussed mainly under the field of
coordination chemistry. The key difference
between ligand and chelate is that ligands
are the chemical species that are donating
or sharing their electrons with a central
atom through coordination bonds, whereas
chelates are compounds containing a
central atom bonded with surrounding
ligands.
 Biologically Important Chelate Complexes
• Many essential biological chemicals are chelates.
• Chelates play important roles in oxygen transport and in
photosynthesis.
• Many biological catalysts (enzymes) are chelates.
• In addition to their significance in living organisms, chelates are also
economically important, both as products in themselves and as
agents in the production of other chemicals.
• A chelate is a chemical compound composed of a metal ion and a
chelating agent.
• A chelating agent is a substance whose molecules can form several
bonds to a single metal ion.
• In other words, a chelating agent is a multidentate ligand.
Ligands
◼ Neutral molecule or ion having a lone electron
pair that can be used to form a bond to a metal
ion.
▪ Monodentate ligand – one bond to a metal ion
▪ Bidentate ligand (chelate) – two bonds to a metal ion
▪ Polydentate ligand – more than two bonds to a metal ion
Coordinate Covalent Bond

◼ Bond resulting from the interaction between a

Lewis base (the ligand) and a Lewis acid (the
metal ion).
Chelation Definition-
◼ Chelation is the ability of ions and molecules to form bonds
with metal ions. Between a polydentate ligand and a single
central atom, two or more different coordinate bonds are
formed or present.
◼ Ligand- A ligand is an ion or molecule that forms a
coordination complex by donating a pair of electrons to the
central metal atom or ion.
◼ Polydentate- The number of atoms used to bind to a central
metal atom or ion varies among polydentate ligands.
◼ Hexadentate ligands, such as EDTA, have six donor atoms with
electron pairs that can bind to a central metal atom or ion.
The Bidentate
Ligand
Ethylenediamine
and the

Monodentate
Ligand Ammonia
The Coordination
of EDTA with a 2+
Metal Ion

ethylenediaminetetraacetate
Chelate complex
Chelate, any of a class of coordination or complex compounds
consisting of a central metal atom attached to a large molecule,
called a ligand, in a cyclic or ring structure.
An example of a chelate ring occurs in the ethylenediamine-
cadmium complex:

The stability of a chelate is also related to the number of atoms

in the chelate ring. In general, chelates containing five- or six-
membered rings are more stable than chelates with four-,
seven-, or eight-membered rings.
Chelate complex
◼ In medical practice, chelating agents, particularly salts
of EDTA, or edetic (ethylenediaminetetraacetic) acid, are
widely used for direct treatment of metal poisoning
because they bind the toxic metal ions more strongly than
do the vulnerable components of the living organism.
◼ Chelating agents are also employed as extra reactants in
industrial and laboratory separation of metals and as
metal-ion buffers and indicators in analytical chemistry.
◼ Many commercial dyes and a number of biological
substances, including chlorophyll and hemoglobin, are
chelate compounds.
 Transition Metal Complexes in Biological
Molecules
Metal ion complexes are used in humans:
▪ for the transport and storage of oxygen
▪ as electron-transfer agents
▪ as catalysts and
▪ as drugs.

20
Biological Importance of Iron

◼ Plays a central role in almost all living cells.

◼ Component of hemoglobin and myoglobin.
◼ Involved in the electron-transport chain.
The Heme Complex
Heme is a cofactor consisting of an Fe2+ (ferrous) ion
contained in the centre of a
large heterocyclic organic ring called a porphyrin,
made up of four pyrrolic groups joined together
by methine bridges.
Not all porphyrins contain iron, but a substantial
fraction of porphyrin-
containing metalloproteins have heme as their
prosthetic group; these are known
as hemoproteins.

Hemes are most commonly recognized as

components of hemoglobin, the red pigment
in blood, but are also found in a number of other
biologically important hemoproteins such
as myoglobin, cytochrome, catalase, heme
peroxidase, and endothelial nitric oxide synthase.
 In which compounds can we find a heme
group?
Hemoproteins
• Hemoglobin (Hb)
• Myoglobin (Mb)
• Cytochromes
• Catalases (decomposition of 2
H2O2 to 2 H2O and O2)
• Peroxidases
 Properties of iron in heme

•Coordination number of iron

in heme = 6

6 bonds:
• 4x pyrrole ring (A,B,C,D)
• 1x link to a protein
• 1x link to an oxygen
Myoglobin
Myoglobin is an iron- and oxygen-
binding protein found in the muscle tissue of
vertebrates in general and in almost all
mammals. It is related to hemoglobin, which is
the iron- and oxygen-binding protein in blood,
specifically in the red blood cells. In humans,
myoglobin is only found in the bloodstream after
muscle injury. It is an abnormal finding, and can
be diagnostically relevant when found in blood.
Myoglobin is the primary oxygen-
carrying pigment of muscle tissues. High
concentrations of myoglobin in muscle cells
allow organisms to hold their breath for a longer
period of time.

◼ The Fe2+ ion is coordinated to four nitrogen atoms in the porphyrin of the heme
(the disk in the figure) and on nitrogen from the protein chain.
◼ This leaves a 6th coordination position available for an oxygen molecule.
Hemoglobin
Hemoglobin abbreviated Hb or Hgb, is
the iron-containing oxygen-
transport metalloprotein in the red blood
cells of all vertebrates (with the exception of
the fish family Channichthyidae) as well as
the tissues of some invertebrates.
Hemoglobin in the blood carries oxygen from
the respiratory organs (lungs or gills) to the
rest of the body (i.e. the tissues). There it
releases the oxygen to permit aerobic
respiration to provide energy to power the
functions of the organism in the process
called metabolism.

◼ Each hemoglobin has two α chains and two β chains, each with a heme complex
near the center.
◼ Each hemoglobin molecule can complex with four O2 molecules.
 Chlorophyll
◼ Chlorophyll, the green pigment of plants, is another
biologically important porphyrin chelate. In chlorophyll
the central ion is magnesium. There are several forms of
chlorophyll. The structure of one form, chlorophyll a, is
shown.

◼ Chlorophyll is one of the most important chelates in

nature. It is capable of channeling the energy of sunlight
into chemical energy through the process of
photosynthesis. In photosynthesis, the energy absorbed
by chlorophyll transforms carbon dioxide and water into
carbohydrates and oxygen.
Structure and properties of water
Water Balance in the Body
Water makes up 50-60% of
total body weight.
Main entry way is through
food, most lost in urine
unless there is excessive
sweating or diarrhea .
Homeostasis maintains
water balance unless there
is pathology or an abnormal
ingestion of water.
Men have more water than
women

Figure 20-2
Structure of water
 Phase Change of Water
The transitions between the solid,
liquid, and gaseous phases of a
single component, due to the effects of temperature and/or pressure:
･Solid-to-liquid transition: melting
･Liquid-to-solid transition: freezing
･Liquid-to-gas transition: evaporation
･Gas-to-liquid transition: condensation
･Solid-to-gas transition: sublimation
･Gas-to-solid transition: deposition
Molecular Structure of Water
-
◼ One oxygen atom O
◼ Two hydrogen atoms H H
◼ H2O + +
◼ Not symmetrical
◼ Electrons spend more time near the oxygen
and less near the hydrogen
◼ Water molecule is polar
Hydrogen Bonding

◼ + attracted to –
◼ Each H2O is bonded
to its nearest
neighbor
Physical States Vapor
Properties of water
◼ Physical properties
◼ Polar molecules
◼ Hydrophilic substances dissolve
◼ Hydrophobic substances aggregate
◼ Osmosis
◼ Cohesion
◼ Adhesion
◼ Chemical properties
◼ Dissociation of water molecules
◼ Acids and bases
Solvent Properties
◼ Interacts with other polar compounds
◼ Is repelled by non-polar compounds
◼ Because is polar, it readily dissolves most
biomolecules, which are generally charged or polar
molecules
◼ Compounds that dissolve easily in water are
hydrophilic
◼ In contrast, nonpolar solvents such as chloroform and
benzene are poor solvents for polar biomolecules but
easily dissolve thse that are hydrophobic - nonpolar
molecules such as lipids and waxes
 Water as a Strong Solvent:
• Waters small size and polarity makes it a
very powerful dissolving agent (solvent) for
many compounds (solute) when they are
added to water, particularly salts and polar
solutes, like sugar.
• Notice how multiple water molecules
surround the ions by charge – partial
charge attractions.
• Water dissolves salts such as NaCl by
hydrating and stabilizing the Na and Cl ions,
weakening the electrostatic interactions
between them .
• The same factors apply to charged
biomolecues.
• Water readily dissolves such compounds by
replacing solute- solute hydrogen bonds
with solute-hydrogen bonds, thus screening
the electrostatic interactions between
solute molecules.
Solvation and Hydration Spheres
Water as a Solvent

• Water is a good solvent for charged and polar

substances
– amino acids and peptides
– small alcohols
– carbohydrates
• Water is a poor solvent for nonpolar substances
– nonpolar gases
– aromatic moieties
– aliphatic chains
Flickering Clusters and Clathrate Cages
Substrates Must Displace Water to Bind Enzymes

➔
Temperature Effects (for Aqueous Solutions)

◼ Although the solubility of most solids in water

increases with temperature, the solubilities of
some substances decrease with increasing
temperature.
◼ Predicting temperature dependence of
solubility is very difficult.
◼ Solubility of a gas in solvent typically decreases
with increasing temperature.
The Solubilities of Several Solids as a Function
of Temperature
The Solubilities of Several Gases in Water
 Acids and Bases
• Water, like a salt, can become dissociated into
a proton (H+) and a hydroxyl ion (OH-). In
pure water there is an equal balance of
protons and hydroxyl ions. We refer to the
solution as neutral (pH = 7).
• Acids are compounds that add protons (H+) to
water. Extra protons make a solution acidic
(pH < 7).
• Bases are compounds that add a hydroxyl
ion(OH-) to water. Extra hydroxyl ions makes
the solution basic, or alkaline (pH > 7).
• pH = -log [H+]
Common H-bonds in Biochemistry
Some Biologically Important H-bonds
Importance of Hydrogen Bonds
◼ Source of unique properties of water
◼ Structure and function of proteins
◼ Structure and function of DNA
◼ Structure and function of polysaccharides
◼ Binding of substrates to enzymes
◼ Binding of hormones to receptors
◼ Matching of mRNA and tRNA
“I believe that as the methods of structural chemistry are further applied to
physiological problems, it will be found that the significance of the hydrogen
bond for physiology is greater than that of any other single structural
feature.”
–Linus Pauling, The Nature of the Chemical Bond, 1939
Approximate Bond Distance,
Strength, kJ/mole nm

12-30 0.3

20 0.25

<40 -

0.4 – 4.0 0.2