BIO-INORGANIC CHEMISTRY

SYLLABUS:
Elements of life: Essential major, trace and ultratrace
elements.

Basic chemical reactions in the biological systems and the

role of metal ions (specially Na+, K+, Mg2+, Ca2+, Fe3+/2+,
Cu2+/+, and Zn2+).
Metal ion transport across biological membrane Na +-ion
pump, ionophores.

OXYGEN CARRING PROTEINS

1. Hemoglobin(Hb)

2.

Myoglobin(Mb)

3. Hemerythrin
4. Hemocyanin

ELECTRON TRASPORT
PROTEINS
1. The iron-sulpher proteins: Ferredoxins.
2. A group of heme proteins: Cytochromes
carbonate bicarbonate buffering system and carbonic

anhydrase.
Biological nitrogen fixation: Nitrogenase enzyme

Photosynthesis: Photosystem-I & Photosystem-II.

 Toxic metal ions and their effects,

Chelation therapy: Pt and Au complexes as

drugs.

Metal dependent diseases.

Elements of life
The evolutionary processes have selected about 30 element as
essential elements, out of 92 naturally occurring ones, to
perform one or more of the physiological functions and have
rejected the others.
What is essential elements?
Essential elements are those in absence of which growth
is inhibited.
Nature

always

numbers(why?)

selects

elements

of

small

atomic

Almost 99% of the mass of the human body is made up of six

elements: what are these elements?
1.Oxygen
2.Carbon
3. Hydrogen
4.Nitrogen
5.Calcium
6. phosphorus.
Only about 0.85% is composed of another five elements:
potassium,
sulfur
sodium
chlorine
and magnesium. All are necessary to life.

Heavy elements are usually toxic.

In terms of weight percent 11 of these 30 essential

elements are

considered as major elements and the

rest of as trace elements.

Essential elements

Major elements

Trace elements

Ultra trace elements

MAJOR ELEMENTS
The elements which are present in bulk are called
major elements, as they are required in the living
body in relatively large amounts. Six elements of
organic matter.

And Na, K, Mg, Ca, Cl, five monoatomic ions ,I,e;

total 11 elements are collective known as major
elements.

Trace Elements

Trace elements are present at low levels in organisms and make up just
0.5% of living cells. However, living things would not be able to survive
without trace elements.
Trace elements include:
Iron(Fe)
Iodine(I)
Manganese(Mn)
Molybdenum(Mo)
Selenium(Se)
Silicon(Si)
Tin(Sn)
Vanadium(V)
Boron(B)
Chromium(Cr)
Cobalt(Co)
Copper(Cu) and
Fluorine(F).

 Iron is found in red blood cells and helps to

carry oxygen in the blood stream.
Iodine

is

important

for

making

different

forms of thyroid hormone, which regulates

growth and energy levels in humans. Many of
the trace elements are required by enzymes
in order to make chemical reactions happen.

Ultra-trace elements
The elements which presents in exceedingly small
amounts are called Ultra-trace elements.
For example: Cd, As, Pb, Ge, Li, Rb, Ba, Br.,etc.

STORAGE AND TRANSPORT OF METABOLIC ENERGY

The living cell requires large amount of fuel to sustain its activity.
Majority of the reactions in the cells are endergonic and nonspontaneous.

Spontaneous cell decomposition takes place upon death.

Adenosine triphosphate (ATP) is the energy currency for cellular

processes.

ATP

provides

the

energy

for

both

consuming endergonic reactions and

releasing exergonic reactions,
of activation energy.

which

energyenergy-

require

small

input

Metabolic energy is stored as the P-O bond energy of

nucleotides, particularly ATP.

An amount of energy equivalent to 7.3 k.cal.mole-1 is

required to phosphorylate ADP with inorganic phosphate to
produce ATP.

When the chemical bonds within ATP are broken, energy is

released and can be harnessed for cellular work. The more
bonds in a molecule, the more potential energy it contains.
Because the bond in ATP is so easily broken and reformed,
ATP is like a rechargeable battery that powers cellular
process ranging from DNA replication to protein synthesis.

Mg-ATP and Mg-ADP

In the biological Ph(7-7.5) ATP and ADP exist as
highly charged anionic species, viz. ATP4- and ADP3-.
Due

to

high

pyrophosphate

affinity

of

triphosphate

and

groups for bivalent metal ions and

relatively high concentration of Mg2+ ion in the

intracellular fluid in intact living cells, ATP4- and ADP3ions predominantly occur in the forms of their Mg2+
complex, viz. Mg-ATP2- and Mg-ADP

The affinity of ATP4- for Mg2+ ion is about 10 times stronger

than that of ADP3-.

ATP is an unstable molecule which hydrolyzes to ADP and

inorganic phosphate when it is in equilibrium with water. The
high energy of this molecule comes from the two high-energy
phosphate bonds. The bonds between phosphate molecules are
called phosphoanhydride bonds. They are energy-rich and
contain a G of -30.5 kJ/mol.

In the absence of metal ions, non-enzymic hydrolysis of ATP is

first order in the ATP species.

Metal ions catalysed hydrolysis of ATP is first order in M2+ ions

(M= Mg, Cu, Zn,Mn, Ni) and first order in the ATP species.

Reactivity's of the M2+ ions fall in the order :

Cu2+

Mg2+ Mn2+ Zn2+

which is almost parallel to the stability order of M 2+ -APT

complexes.

Hydrolysis of ATP

Removing or adding one phosphate group interconverts

ATP

to

ADP

or

ADP

to

AMP.

Breaking

one

phosphoanhydride bond releases 7.3 kcal/mol of energy.

ATP+H2OADP+Pi

G = -30.5 kJ/mol

ATP+H2OAMP+2Pi
2ADP+H2O2AMP+2Pi

G = -61 kJ/mol
G = -61 kJ/mol

At pH 7,
ATP4+H2OADP3+HPO42 + H+

Mechanism of ATP hydrolysis

Entropy of activation is negative in all these cases,

indicating an associative (SN2) path.

The transition is a 1:1 metal:ATP complex on which a

solvent H2O molecule makes a nucleophilic attack to
produce the metal-ADP complex and H2PO4H

O
O O

Ad-O-P-O-P-O-P-OH
O- O-

O-

M2+

Ad-O-P-O-P-OH + HO-P-OH
O
O O
M2+

Faster rate of hydrolysis in presence of M2+ ions

Rate of hydrolysis of ATP in the presence of M2+ ions is

much faster than in absence of metal ions(why?)

This is because, metal ions coordination to the phosphate

groups lowers the negative charge of the ATP species by
two units.

This favours nucleophilic attack by H2O molecules on the

terminal phosphorous atom.

Rate of hydrolysis of Mn2+ -ATP and Cu2+-ATP

Though

Mn2+

-ATP

and

Cu2+-ATP

complexes

have

comparable stabilities, Mn2+ ions catalysed hydrolysis of

ATP is much slower than the Zn2+ ions catalysed reaction.
This is because, Zn2+ ion binds to and phosphate groups
of ATP only, while, Mn2+ ion possibly binds to , and phosphate groups.
Thus, all the the P-O bonds are polarised in the Mn 2+-ATP
complex.
This results in an overall lower polarisation of the individual
P-O bonds, hence the slower rate of hydrolysis.

Why is ATP hydrolysis an exergonic reaction?

The entropy, which is the level of disorder, of ADP is greater than that of
ATP.

Therefore,

due

to thermodynamics,

the

reaction

spontaneously occurs because it wants to be at a higher entropy level.

Also, the Gibbs' free energy of ATP is higher than that of ADP. Naturally,
molecules want to be at a lower energy state, so equilibrium is shifted
towards ADP.
Electrostatic repulsion: of the four negative charges on the oxygens of the
ATP molecule. Naturally, like charges repel and opposite charges
attract. Therefore, if there are four negative charges in close proximity to
one another, they will naturally repel each other. This makes ATP a
relatively unstable molecule because it will want to give away its
phosphate groups, when given the chance, in order to become a more
stable molecule.

Creatine-Phosphocreatine interconversion and ATP

Creatine is a biochemically important amino acid derivative.over

90% of the Creatine in the body of an adult is present in the
msucles.

Its concentration in blood and body fluid is normally very low

reaches high values values under renal dysfunction.

Creatine,

whether

synthesized

naturally

in

the

body

or

supplemented by dietary sources, is important for energy

production in the human body. The initial energy needed for
muscle contraction is provided by the molecule ATP.

 ATP can only supply enough energy for a few seconds of

muscle movement, so in order for sustained muscle
contraction to occur, ATP must be regenerated.
This is where creatine comes in.

In skeletal muscle,

creatine exists in equilibrium with its phosphorylated form,

which is called creatine phosphate or phosphocreatine.

 One third of the creatine in skeletal muscle is free creatine, and the
remaining two thirds is phosphorylated.

Phosphocreatine can give up its phosphate group to the ADP molecule,

resulting in the regeneration of ATP.

According to Le Chteliers Principle, as the concentration of ATP is

depleted

in

the

first

few

seconds

of

intense

exercise,

the

phosphocreatine-creatine equilibrium shifts to favor the formation of

ATP. ATP can then be used again to power muscle contraction for up to
10 seconds of extremely intense activity, such as a 100-meter sprint.

Fuctions

Phosphocreatine can anaerobically donate a phosphate group to ADP to

form ATP during the first 2 to 7 seconds following an intense muscular
or neuronal effort.

 Conversely, excess ATP can be used during a

period

of

low

effort

to

convert creatine to

phosphocreatine.
The reversible phosphorylation of creatine (i.e.,
both the forward and backward reaction) is
catalyzed by severalcreatine kinases.
The

presence

of

creatine

kinase

in blood

plasma is indicative of tissue damage and is used

in the diagnosis of myocardial infarction.

 The

cell's

ability

to

generate

phosphocreatine

from

excess ATP during rest, as well as its use of phosphocreatine

for quick regeneration of ATP during intense activity, provides
a spatial and temporal buffer of ATP concentration.

In other words, phosphocreatine acts as high-energy reserve

in a coupled reaction; the energy given off from donating the
phosphate group is used to regenerate the other compound in this case, ATP.

Phosphocreatine plays a particularly important role in tissues

that have high, fluctuating energy demands such as muscle

and brain.

OXGEN TRANSPORT PROTEINS

Nature has designed four O2-carrying proteins for transport and
storage of oxygen in biological systems.
These are:
1. Hemoglobin (denoted as Hb)and 2. Myoglobin (Mb) are dioxygen
(O2) binding metalloproteins containing an iron porphyrin system, Fe(II)heme proteins.

Hemoglobin is present in Red Blood Cells (RBC) and helps in transport of

dioxygen from lungs to tissues. Whereas, myoglobin stores dioxygen
and is present in muscles.

 3. Hemerythrin, a non -heme Fe(II)

proteins
Occurring in several marine
invertebrates and lower forms of life.
Its main function is O2-storage.

Active site of hemerythrin before and after oxygenation.

4. Hemocyanin
Hemocyanine

are

copper

containing

oxygen

transport proteins, occuring in a number of

invertibrate, viz., snail, quids, cuttle, octopus etc.

HEMOGLOBIN & MYOGLOBIN

ACTIVE SITE STRUCTURE

Mb is a monomeric protein (MW = 17,100daltons) having a

single poly peptide chain that is not conductive of self
association.

On

the

other

hand,

Hb

is

tetrameric

protein

(MW=

64500daltons), consisting of two and two peptide chains

interlinked

trough

hydrogen

bonded

(COO-..NH3+

interactions.

X-ray study showed that the disappearance of these salt bridge

bonds oxygenation.

 The active site of both Hb and Mb contains the

heme

group

in

which

Fe(II)

is

equatorially

coordinated by the four pyrrole nitrogen atom of

protoporphyrin IX.
The 5th position is

coordinated by the imidazole

nitrogen atom of histidine of the chain(i.e., the

globin).
The 6th position in deoxy-Hb or deoxy-Mb is
vacant, but hdrophobically shielded by the protein
chain.
As a result, only non polar neutral molecules such
as o2 CO, etc. can bind to the sixth position.

 In the absence of the

protein (globin), the 6th

position is irreversibly oxidised by oxygen of the

air to Fe(III)- heme, hematin.
The latter, because of its residual positive charge,
is reluctant to bind uncharged ligands such as
O2 , but readily binds charged liands such as CN - ,
S2- , OH- etc.; which inhibit the oxygenetion.
(Globin) Fe(II) heme
( Fe(II) heme

+
O2

O2

(Globin) Fe(II)-heme-O2
Fe(III)-heme (i.e., hemetin)

BIOLOGICAL IMPORTANCE OF
Hb&Mb
Hemoglobin(Hb)

and

Myglobin(Mb)

are

responsible for the transport and storage of

oxygen in higher animals. Viz., mammals. Hb
transports oxygen from its source(vis., lungs, skin
and gills) to the site of its use inside the muscle
cells, where oxygen is transferred to Mb for use in
mictrochondrial oxidatio9i.e., respiration.

Role of Distal(E7)and Proximal(F8) Histidine Residues

in Hb & Mb
In deoxy-hemoglobin, four of the coordinated sites of iron are
occupied by nitrogens of porphyrin ring. The fifth site is
occupied by Histidine residue (called proximal histidine) of
globin. The sixth position is occupied by weakly bonded water
molecule. Hence some authors tend to report Fe(II) ion in deoxy
form as pentacoordinated. Deoxy-hemoglobin is said to be in Tstate (tense).
On the opposite side of the proximal histidine, there is one more
histidine group (called distal histidine) placed near the iron ion.
It forces the binding of dioxygen in "end on bent" confirmation.

Function of proximal Histidine Residues(F8)

The proximal histidine (F8) residue acts as a good -donor to

facilitate the central metal to act as a better -donor towards
the -acid ligand(e.g.O2)at the trans-position.

This largely helps O2 to acts as a better -acid ligand(i.e. acceptance) to induce the spin at iron, i.e. O 2 acts as a
relatively strong field ligand.

If the base(B) is itself a good -acid ligand, then formation of

the O2-adduct will be disfavoured. CO is a powerful poison to
Hb and Mb,as the heme group has very high affinity for the
-acid ligand like CO.

Function of Distal Histidine Residues(E7)

Presence of distal histidine residue in the region of sixth

coordination site, it does not allow CO to form the linear FeCO bond and CO is forced to make a bent bond.

The bent conformation discourages the binding of CO to

heme iron. Otherwise, CO may have even more affinity with
the iron ion. It is observed that CO binds to hemoglobin
200X stronger than dioxygen but binds 20,000X stronger
with unprotected heme.

Thus the distal histdine (protein) weakens the interaction

with CO and optmises the binding of O 2 in Hb and Mb

Additionally the imidazole moity of distal histidine stabilizes

the oxygenated compound through H-bonding.

Nature of bonding
The bonding mechanism of oxy-Bb and oxy-Mb can be
explain by considering simplest possibilities:
Coordination of singlet O2 to low spin Fe(II); O2 as a
one electron acceptor leading to low-spin Fe(III) and
O2- (Superoxide).
In the de-oxy form, if square pyramidal geometry is
consider the the electonic configuration of high spin
Fe(II)
In

the

oxy-condition,

if

FeIII

O2interaction

is

considered then the electronic configuration of lowspin FeIII is t2g5(assuming octahedral geometry)

 If FeII(L.S)-singlet O2 interaction is considered then

then the electronic configuration of low spin FeII is t2g6.
Oxy Hb/Mb is paramagnetic/diamagnetic?
In

the

model

system,

electron(t2g5 ) of FeIII

FeIII

O2-

the

unpaired

undergoes anti-ferromagnetic

coupling with the unpaired electron in g* of O2-.Thus

both the models explain the diamagnetic character of
oxygenated heme unit.

dx2-y2

dz2
dxy
dxz, dyz

Posing of Hb and Mb

Different -acid ligands like CO, NO,PF3 which are electrically neutral
and not much bulky can compititively replace O 2 from the sixth
octahedral site of Hb & Mb.

Consequently the O2 transport mechanism gets arrested and toxic

effect arises.

CN- may also bind the site but due to presence of heme pocket
surrounded by hydrophobic environment does not welcome CN easily.

CO affinity of Hb and Mb is drastically diminished due to the steric

hindrance by the distal histidine (E7).

But in the industrial pollution and automobile exhaust produce a

large

amount

of

CO

carboxyhemoglobin(HBCO).

which

on

inhelation

produces

This is why, it is now almost mandatoty to use catalytic

convertersinto the exhaust system to convert CO and NO
int CO2 and N2 respectively.

Recent report demend that ZnO + CuO catalyst can

effectively convert CO into CO2 .

It is very interesting that the posoning effect of CO is not

cumulative, as it can be replaced by O2 in fresh air.

Hb(CO) + O2

Hb(O2) + CO

ALLOWABLE CONCENTRATION OF CO

The maximum allowable concentration of CO in air is 50 ppm

for working 8 hours.

Working of 4 hors in the atmosphere of 300ppm CO, leads to

blocking of 35% of Hb.

Working of 4 hors in the atmosphere of 800ppm CO, leads

to blocking of 60% of Hb.

During cigarette smoking, CO concentration may go upto

200-400 ppm and in a heavy smoker 5-15% of Hb remain as
HbCO.

Detoxification of Hb & Mb

Some oxidising agent such as nitrite, chlorates, etc. can oxidise

Fe(II) present in hemoglbine and myoglobin giving rise to
methemoglbin (Met-Hb) i.e. ferrihemoglobin and metmyoglobin
(Met-Mb) respectively which are not able to transport O2.

Why CN- is deadly toxic?

CN-

actually blocks the cytochrome c oxidase involved in the

respiratory chain.

Treatment:

To remove the bound CN- from cytochrome c oxidase, some

methemoglobins (Met-Hb) are to be generated either by
inhalation of amylnitrite vapour or by injection of NaNO2
solution. (Met-Hb) bearing Fe(III) can bind CN- more
strongly than the cytochrome c oxidase. Consequently, CN is removed from the respiratory chain to regenerate the
electron tunneling path.

Presently Co(II)-edta comlpex is also therapeutic use.

Acid-base balance and Hb

Both the deoxy and oxy-forms of hemoglobin can acts as

weak Bronsted acids. Hence in the presence of corresponding
cojugate base, it can acts as a buffer to restore the biological
Ph as the corresponding pKa values lies close to 7.0.

Besides this, hemoglobin plays an active role in transporting

carbon dioxide from the tissues(i.e. sites of generation of
CO2) to lungs.

Electron Transport Proteins

Electron transport proteins are responsible for the transport

of reducing equivalents (electrons) from a biological redox
couple having a lower standard redox potential to one
having a higher standard redox potential.

standard redox potential of an electron transport protein

should be intermediate between those of the electron
acceptor and the electron donor couples.

Electron transporting mettallo proteins are mainly the

1. Iron-sulpher proteins, viz.,Ferredoxins

2. The Fe(III)-heme proteins, viz., cytochromes.

Both

this groups operate through their Fe(III)-Fe(II)

couples.

Cytochromes

Cytochromes are a group of Fe(III)- heme proteins that

function as electron carriers in mitochondrial oxidation,
photosynthesis etc.

They are classified as a, b, c, etc. depending on their

absorption spectra, their porphyrin substitution and in iron
coordination.

Fe in cytochromes is equatorially coordinated by four pyrrole

nitrogen atoms of the porphyrin ring system. 5 th amd 6th
positions of iron are axially coordinated by different groups
of the protein chain.

Active site structure of cytochrome c

The active site of cytochrome c is the heme group

which is covalently bonded with the polypeptide chain
of 104 amino acid residues.
Fe remains octahedrally coordinated in both the
oxidised and reduced forms.
One axial position is coordinated by the imidazole
Natom of histdine-18 and the other axial position is
occupied by the thioether S atom of methionine-80.
Three dimentional shape of the protein chain looks
roughly sperical. The heme group is surrounded by a
hydrophobic polypeptide chain.

Electron transfer

Rate of electron transfer with cytochrome c is 103 times

slower than the rate of electron transferwith analogous
compounds of iron.

E.g.,

kobs (sec.-)

for

cytIII/

cytII

is

5x104,

while

for

FeIII(phen)3/FeII(phen)3 it is 1x107.

Slow rate of electron transfer indicates that the heme c is

buried in a hydrophobic protein pocket and only an edge of
the prosthetic group is near to the surface.

Electron transfer occurs through this exposed heme edge

and involves the

Fe(III) + e

Fe(II)

redox couple

Why slow rate of electron transfer

Due to hydrophobic wrapping of the heme group by the

protein chain, the electron donating groups fails to make
direct contact with the ultimate electron accepting site (i.e.,
FeIII in heme c), hence slow rate of electron transfer.

Fe in both the oxidised and reduced forms of cytochrome c

is in low spin configurations which are favourable for outer
sphere electron transfer.

Significance of cyt.c

There is a great significance of cyt.c in the evolution process.

Cyt.c is the oldest chemical compound evolved more than 1.5
years ago and it is widely distributed in the biological world.
The different cyt.c from different sources mainly differ in the
amino acid sequence of the polypeptide chains.

In fact, a family tree of the evolution process from lower

animal to higher animal can be constructed in terms of the
amino acid sequence of the protein chain in cyt.c.

Iron-sulphur proteins

Iron-sulphur

proteins

function

as

electron

carriers

in

biological redox reactions, viz., photsynthesis, nitrogen

fixation and mitochondrial respiration.

These consist of non-heme iron, coordinated by cysteine

sulphur(-SH) and acid labile inorganic sulphide sulphur(S2-).

Iron-sulphur proteins are often abbeaviated as n-(Fe-S*)

centres, where, n stand for the number of iron cations per
protein and S* stands for the inorganic sulphide sulpher (S2) usually n in number.

These

labile

sulphur

atoms

are liberated

as

H 2S

on

acidificationof the proteins and are readily air oxidised to

elemental sulphur.

 Iron

in

these

proteins

are

approximately

tetrahedraly

coordinated by four sulpher atoms, of which at least one is

cysteine sulpher from the protein chain.

The electron transpot by ferredoxins take place via Fe(III)/Fe(II)

couple but the redox potential of Fe-S proteins are close to that
of the H+/H2 couple and vary widely depending upon the nature
of the protein environment around iron(where as redox potential
of aqueous Fe(III)/Fe(II) is 0.785v).

E.g., E0 of ferredoxine in photosynthetic bactrium, chromatium

= -0.49 but the E0 of ferredoxine in beef-heart mitochondria =
+0.22v.

Ferredoxins,2Fe-2S

Occurrence: 2Fe-2S Ferredoxins occur in the chloroplasts of

many plants, in several bacteria, beef-heart mitochondria
and in pig adrenal glands.

Active site structure: These consist of a single poly peptide

chain of 98 amino acids (MW 10,500 daltons).

Its active site contains two iron centres bridged by two acid
labile (S2-) sulphur and each Fe is bound to two cysteine
sulphur atoms of the protein chain in such a maner that the
individual (cys-S)2Fe(S2-)2 units appear tetrahedral, providing
high spin configuration to iron.

Mechanism of electron transfer

Oxidised form: In the oxidised form, both the iron atom ar e in

Fe(III) state with high spin( t2g4eg2 , S = 5/2) configuration.

Yet the protein is diamagnetic and is e.p.r. silent due to

antiferromagnetic FeIII ..FeIII coupling.

The dz2 orbital of each iron makes a overlap with the orbital of
S2- ions.

The dxz and dyz orbitals of iron make -overlaps wiyh the vacant
d orbitals of the two cysteine sulphur atoms.the d xy orbital, of iron
atom remain non-bonding.

The

bridging

sulphide

(S2-)

ligands

enable

the

individual

paramagnetic Fe(III) centres to pair up with each others spin

throug super-exchange interaction.

The reduced form of 2Fe-2S

The reduced form of the protein is paramagnetic for one unpaired
electron and is e.p.r. active(gI=1.97). Which corresponds to
reduction of one of the two Fe(III) centres to Fe(II).

2Fe-2S ferredoxins, therefore, function as one-electron transport

proteins.
[(cys-S)2 FeIII (S2-)2 FeIII (S-cys)2]2- +e

[(cys-S)2 FeIII (S2-)2 FeII (S-cys)2]3-

In the reduced form, a high spin FeIII (S= 5/2) and a high spin FeII
(S=4/2) are anti-ferromagnetically coupled to give a net electron
spin(S=1/2) in the ground state.

Electron transport occurs with very small energy transfer,

as the redox potential (E0) of this protein is very low(e.g.
-0.2to -0.4v).

Iron centre in the reduced form are non-eqivalent, though

they are equivalent in the oxidised form.

Due to reduction, the ionic radius changes from 0.63A 0 in

high spin Fe(III) to 0.77A0 in high spin Fe(II).This distort
the planarity of Fe (S2-)Fe moity and initiates nonvalence(tertiary and quaternary) interactions in the proein
chain.

Conversely, alteration in the protein conformation may alter

the redox potential at the avtive site of these proteins.

4Fe-4S, Ferredoxins

These proteins can undergo one electron redox reactions,

though their biochemical functions are less well known.

These are not generally classed as ferredoxins, rather, these

are often called high potential fron proteins and are
abbreviated as HIPIP.

Active site of these proteins consist of four iron atoms, four

acid labile sulphide sulphur(S2-) and four cysteinyl sulpher
atoms arranged in a cubic structure.

Mode of bonding
Mode of bonding of iron and sulphur(S2-) in 4Fe-4S proteins is the
same as in 2Fe-2S proteins. The cubic Fe4(S2-)4 clusters in 4Fe-4S
proteins may be vitualised as a cobination of two Fe(S2-)2Fe
clusters of 2F2-2S ferredoxins.
Each Fe in these Fe4(S2-)4 cluster is tetrahedrally coordinated by
three acid labile sulphide sulpher(S2-) and one cysteine sulpher
(cys-S) as shown in the Fig.

The oxidised form

The oxidised form contains three high spin Fe(III) and one
high spin Fe(II) and its paramagnetism is equivalent to one
unpaired electron due to antiferromagnetic interaction.

The oxidised form of HIPIP is e.p.r. active(g=2.02)

The reduced form contain two Fe(III) and two Fe(II) and is
diamagnetic due to antiferromanetic interaction.

These proteins, therfore, function as one-electron carriers:

[(FeIII)3 (FeII) (S2-)4 (S-cys)4]- + e

[(FeIII)2 (FeII)2 (S2-)4 (S-cys)4]2-

8Fe-8S, Ferredoxins

Thes ferredoxine are small (MW=6000 daltons) and cosist

of two 4Fe-4S, clusters situted at 12A0 apart each of which
can undergo one electron change with E0 = -0.4volts.

[(FeIII)2 (FeII)2 (S2-)4 (S-cys)4]2- + e

2[(FeIII)2 (FeII)2 (S2-)4 (S-cys)4]2- +2e

[(FeIII) (FeII)3 (S2-)4 (S-cys)4]3-

2[(FeIII) (FeII)3 (S2-)4 (S-cys)4]3-

As a result, the whole protein functions as atwo-electron carrier.

The oxidised form contain equal number of Fe(III) and Fe(II), but shows
lower magnetic moment(1.2B.M. per iron) due to extensive
antiferromagnetic coupling and spin delocalisation