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Hemerythrin
 Non-heme Fe containing protein found
in invertebrates
 Contain Fe(II) and binds oxygen
reversibly
 Contains 8 subunits with 113
aminoacids and 2 Fe(II) active sites.
 difference b/W Hb and Mb is in the
binding of oxygen
 He does not exhibit cooperativity.
 Each subunit in He consists 2 Fe active sites connected by 3 bridged gps.
 Two of which are carbonyl anions from Glutamate and Aspartate and the other is
either H2O, Oh or o22-, but probably OH.
 Remaing coordinates to N-atom of His residue.
 Deoxy-He are strongly antiferromagnetically coupled through the Fe-O-Fe bridge
 Deoxy-He paramagnetic and High spin.
 Fe atom is pseudo Oh.
Hemocyanin
• It suggests the presence of Heme gp and as well as cyanide ion.
• Copper containing protein carries oxygen in invertribartes.
• Deoxy Hc contains Cu(I) ion and is colorless.
• Oxygenation provides Cu with normal coordinated structure and remove a strain.
• Deoxy-Hc is diamagnetic, colorless in which both Cu atom in +1 oxidation state.
cytochromes
• Found in both plants and animals and serves as electron carriers.
• Contain heme like prosthetic group
• A prosthetic group is compound required by an enzyme to facilitate a particular reaction, such compounds are also called as
coenzymes.
• The peptide portion of an enzyme that requires a prostetic group is called the Haloenzyme.
• There are three main types of cytochromes
1) Cytochrome a
2) Cytochrome b
3) Cytochrome c
 As in Hb, the Fe(II) ion of heme gp is attached to a N-atom of His.
 6th coordination site is occupied by atightly bound S atom form Methionine of protein.
 For this reason Cyt are inert not only to the oxygen but also CO which affects oxygen carrier.
 The reduction potentials of cyt increases in the order: Cyt-b(0.26v), Cyt-c (026v) and Cyt-a(0.4v).
 Therefore the flow of electrons is in the order: b---- c --- a --- oxygen.
 ETC allows energy from Glucose oxidation to be released gradually and to be stored in the form of ATP.
 Cyt-c-oxidase, the terminal member of the cyt chain, which binds the inner membrane of the mitochondria contains Cyt-a,
Cyt-a3 and two Cu(II) ions (CuA & CuB).
 Electron transfer involves the Cyt-a, CuA
• The electron being transported form Cyt-c to CuA and then to Cyt-a.
• The Cyt-a3 and CuB provides site for oxygen binding and conversion of oxygen to
water.
• Cyt-a3 and CuB are 5 and 3 coordinated respectively and therefore binds oxygen.
• Cyt chain not only involves the transfer of electrons but also transport prontos
across the mitochondrial membrane.
• The oxidized form of Cyt a3 is susceptible to bind CN- that renders cyanide toxic.

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Hemoerythrine and Hemocyanin.pptx

  • 1. Hemerythrin  Non-heme Fe containing protein found in invertebrates  Contain Fe(II) and binds oxygen reversibly  Contains 8 subunits with 113 aminoacids and 2 Fe(II) active sites.  difference b/W Hb and Mb is in the binding of oxygen  He does not exhibit cooperativity.  Each subunit in He consists 2 Fe active sites connected by 3 bridged gps.  Two of which are carbonyl anions from Glutamate and Aspartate and the other is either H2O, Oh or o22-, but probably OH.  Remaing coordinates to N-atom of His residue.  Deoxy-He are strongly antiferromagnetically coupled through the Fe-O-Fe bridge  Deoxy-He paramagnetic and High spin.  Fe atom is pseudo Oh.
  • 2. Hemocyanin • It suggests the presence of Heme gp and as well as cyanide ion. • Copper containing protein carries oxygen in invertribartes. • Deoxy Hc contains Cu(I) ion and is colorless. • Oxygenation provides Cu with normal coordinated structure and remove a strain. • Deoxy-Hc is diamagnetic, colorless in which both Cu atom in +1 oxidation state.
  • 3. cytochromes • Found in both plants and animals and serves as electron carriers. • Contain heme like prosthetic group • A prosthetic group is compound required by an enzyme to facilitate a particular reaction, such compounds are also called as coenzymes. • The peptide portion of an enzyme that requires a prostetic group is called the Haloenzyme. • There are three main types of cytochromes 1) Cytochrome a 2) Cytochrome b 3) Cytochrome c  As in Hb, the Fe(II) ion of heme gp is attached to a N-atom of His.  6th coordination site is occupied by atightly bound S atom form Methionine of protein.  For this reason Cyt are inert not only to the oxygen but also CO which affects oxygen carrier.  The reduction potentials of cyt increases in the order: Cyt-b(0.26v), Cyt-c (026v) and Cyt-a(0.4v).  Therefore the flow of electrons is in the order: b---- c --- a --- oxygen.  ETC allows energy from Glucose oxidation to be released gradually and to be stored in the form of ATP.  Cyt-c-oxidase, the terminal member of the cyt chain, which binds the inner membrane of the mitochondria contains Cyt-a, Cyt-a3 and two Cu(II) ions (CuA & CuB).  Electron transfer involves the Cyt-a, CuA
  • 4. • The electron being transported form Cyt-c to CuA and then to Cyt-a. • The Cyt-a3 and CuB provides site for oxygen binding and conversion of oxygen to water. • Cyt-a3 and CuB are 5 and 3 coordinated respectively and therefore binds oxygen. • Cyt chain not only involves the transfer of electrons but also transport prontos across the mitochondrial membrane. • The oxidized form of Cyt a3 is susceptible to bind CN- that renders cyanide toxic.