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Class 11 MSc III Sem

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7 views

Class 11 MSc III Sem

Uploaded by

meghamkadcms
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© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
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Iron-Sulphur Proteins

• Iron-sulphur proteins are found in all organisms, in mitochondria and chloroplasts.


• Especially in mitochondria, they are found in terminal electron transport pathways of
respiration.
• They involve in respiration, photosynthesis and nitrogen fixation.
• Approximately 1% of iron content in mammals is present as iron-sulphur proteins.
• They act as one electron donors and one electron acceptors in electron transfer
process. Eg: Iron-Sulphur clusters cycles between the Fe(II) (reduced) and Fe(III)
(oxidized) state.
• Structure of Iron-Sulphur Proteins: Fe-S proteins are non-haeme proteins. That means it
does not contain haeme group.
• Central iron atom is not connected to porphyrin ring as in the case of cytochromes.
• Instead of that these proteins are bound by S atoms. These S atoms are in the form of
inorganic sulphide (S2-) or cysteine residues of the protein chain.
• Classification is based on the number of iron atoms and number of inorganic
sulphur atoms present.
• They are generally representing as [nFe-mS*].
• Protein contain single iron atom are called Rubredoxins and proteins contain
2Fe and 4Fe clusters are known as Ferredoxins.
• Rubredoxins [1Fe-0S*]:
These are found only in bacteria and the simplest type of Fe-S protein.
Rubredoxin contains a single high spin iron(II) or iron(III). Fe centre is
coordinated to the sulfhydryl groups of four cysteine residues. Geometry is
tetrahedral.
• Therefore, crystal field splitting energy is very low. So, Fe ions are always in high spin
state.
• The main Fe-S distances in all Rubredoxins are nearly identical.
Ferredoxins
a. [2Fe-2S*] Proteins
• They are dinuclear clusters that contain two iron atoms (Cys)S S S(Cys) bridging by two
inorganic sulphides.
• The two iron atoms are tetrahedrally coordinated. The remaining four coordination sites
are occupied by cysteine residues.
b. Rieske Proteins [2Fe-2S*] (Cys)S S N(His)
• This is a subclass of ferredoxin proteins.
• The centre is with unsymmetrical structure where one Fe atom linked to two cysteine
residues and other Fe atom is linked to two histidine residues.

[4Fe-4S*]
• This is the most common and most stable iron-sulphur cluster.
• These S clusters are cubic and contain four iron atoms and four inorganic sulphides.
Iron atoms occupied altered corners of the cube. Remaining S corners are occupied
by inorganic sulphides which are triply bridged. Resulting geometry of the iron
centers are distorted tetrahedrally.
What is ferritin?
• Ferritin is a protein that stores iron, releasing it when the body needs it.
• Ferritin usually lives in the body’s cells, with very little actually circulating in the blood.
• The greatest concentrations of ferritin are typically in the cells of the liver (known as
hepatocytes) and immune system (known as reticuloendothelial cells).
• Ferritin is stored in the body’s cells until it’s time to make more red blood cells. The
body will signal the cells to release ferritin. The ferritin then binds to another
substance called transferrin.
Transferrin
• Transferrin is a protein that combines with ferritin to transport it to where new red
blood cells are made.
• While it’s important for a person to have normal iron levels, having enough stored iron
is important too. If a person doesn’t have enough ferritin, iron stores can deplete
quickly.
Low ferritin levels High ferritin levels
Your doctor may order a ferritin test if
You can also have very high ferritin
you have some of the following
levels, which can cause unpleasant
symptoms associated with low ferritin
symptoms as well. Symptoms of
levels:
excess ferritin include:
• unexplained fatigue
• dizziness • stomach pain

• chronic headaches • heart palpitations or chest pains


• unexplained weakness • unexplained weakness
• ringing in your ears • joint pain
• irritability • unexplained fatigue
• leg pains
• shortness of breath
• Transferrin is the major iron transport protein (transports iron through
blood).
• Fe3+ is the form of iron that binds to transferrin, so the Fe2+ transported
through ferroprotein must be oxidized to Fe3+.
• There are 2 copper-containing proteins that catalyze this oxidation of Fe2+:
hephaestin and ceruloplasmin.
• Hephaestin is found in the membrane of enterocytes, while ceruloplasmin
is the major copper transport protein in blood.
• Hephaestin is the primary protein that performs this function in a coupled
manner (need to occur together) with transport through ferroportin.
• This means that the Fe2+ needs to be oxidized to
be transported through ferroportin. Evidence
suggests that ceruloplasmin is involved in
oxidizing Fe2+ when iron status is low. Once
oxidized, Fe3+ binds to transferrin and is
transported to a tissue cell that contains a
transferrin receptor. Transferrin binds to the
transferrin receptor and is endocytosed, as shown:

• Once inside cells, the iron can be used for


cellular purposes (cofactor for enzyme etc.) or it
can be stored in the iron storage proteins
ferritin or hemosiderin. Ferritin is the primary
iron storage protein, but at higher
concentrations, iron is also stored in
• Siderophores are low-molecular-weight molecules that chelate
iron with a very high and specific affinity.
• Many bacteria, both G+ and G−, produce and secrete siderophores to
scavenge iron from the extracellular environment.
• Siderophore–iron complexes are transported into the cell through
receptors in the membrane.
• Enterobactin is a high affinity siderophore that acquires iron for
microbial systems.
• It is primarily found in Gram-negative bacteria, such as
Escherichia coli and Salmonella typhimurium.
• Enterobactin is the strongest siderophore known, binding to the
ferric ion with affinity K = 10⁵² M⁻¹.

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