Encyclopedia of Astrobiology

Living Edition
| Editors: Muriel Gargaud, William M. Irvine, Ricardo Amils, Henderson James Cleaves, Daniele Pinti, José Cernicharo Quintanilla, Michel Viso

Histidine

Living reference work entry
DOI: https://doi.org/10.1007/978-3-642-27833-4_728-4

Definition

Histidine is one of the 20 ribosomally encoded protein amino acids. It was first isolated by the German physician and biochemist Albrecht Kossel in 1896. It is distinguished by having a side chain with an imidazole ring, which has a pKa of approximately 6. Histidine has an isoelectric point (pI) of 7.6; thus, at typical intracellular pH values, relatively small shifts in pH can greatly change its average charge. When protonated, the imidazole ring is positively charged, with the positive charge distributed between both ring nitrogen atoms, which can be represented by two resonance structures. The imidazole ring of histidine is aromatic at all pH values as it contains six π electrons, is a common coordinating ligand in metalloproteins, and is a part of the catalytic sites of many enzymes.

Histidine has not been identified in carbonaceous chondrites and is difficult to be formed in Miller-type prebiotic synthesis experiments, while imidazole can be easily obtained in them.

See...

Keywords

Nitrogen Atom Positive Charge Bioorganic Chemistry Isoelectric Point Resonance Structure 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
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Copyright information

© Springer-Verlag Berlin Heidelberg 2014

Authors and Affiliations

  1. 1.Earth-Life Science Institute (ELSI), Tokyo Institute of TechnologyMeguro-kuJapan
  2. 2.Institute for Advanced StudyPrincetonJapan
  3. 3.Blue Marble Space Institute of ScienceWashingtonUSA
  4. 4.Center for Chemical Evolution, Georgia Institute of TechnologyAtlantaUSA