Haem group: Difference between revisions
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Haem group in haemoglobin is a non-[[ | Haem group in haemoglobin is a non-[[Protein|protein]] component of [[Haemoglobin|haemoglobin]] which is made up of a [[Prosthetic porphyrin ring|prosthetic porphyrin ring]] with an [[Iron|iron]] [[Ion|ion]] centre (Fe<sup>2+</sup>). | ||
The characteristic constant oxidation state of [[ | The characteristic constant [[Oxidation|oxidation ]]state of [[Iron|Fe]] throughout the whole process of oxygenation and deoxygenation is one of the unique properties of haem caused by the [[Hydrophobic|hydrophobic]] interaction and [[Electron|electron ]]rearrangement of haem when bound to [[Oxygen|oxygen]], allowing [[Haem_group|haem ]]to recombine with oxygen after deoxygenation<ref>http://www.pearsonhighered.com/mathews/ch07/c07mobhp.htm</ref>. The large number of [[Double_bond|double bonds]] within haem allows electromagnetic wave absorption in the [[Visible_light|visible light spectrum]] whereas the interaction between the iron atom and the surrounding protein chain results in different colours of light to be given off<ref>http://www.chm.bris.ac.uk/motm/hemoglobin/hemoglobh.htm</ref>. | ||
=== References === | === References === | ||
<references /> | <references /> | ||
Revision as of 10:50, 23 October 2018
Haem group in haemoglobin is a non-protein component of haemoglobin which is made up of a prosthetic porphyrin ring with an iron ion centre (Fe2+).
The characteristic constant oxidation state of Fe throughout the whole process of oxygenation and deoxygenation is one of the unique properties of haem caused by the hydrophobic interaction and electron rearrangement of haem when bound to oxygen, allowing haem to recombine with oxygen after deoxygenation[1]. The large number of double bonds within haem allows electromagnetic wave absorption in the visible light spectrum whereas the interaction between the iron atom and the surrounding protein chain results in different colours of light to be given off[2].