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Title: Retinaldehyde  
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Subject: Aldehyde, Lipid signaling
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This article is about the chemical compound. For the light-sensitive eye tissue, see Retina.
Not to be confused with Retinol.
CAS number 116-31-4 YesY
PubChem 1070
UNII RR725D715M YesY
Jmol-3D images Image 1
Molecular formula C20H28O
Molar mass 284.44 g mol−1
Appearance Orange crystals from petroleum ether[1]
Melting point

61-64 °C[1]

Solubility in water Nearly insoluble
Solubility in fat Soluble
Related compounds
Related compounds retinol; retinoic acid; beta-carotene; dehydroretinal; 3-hydroxyretinal; 4-hydroxyretinal
 YesY (verify) (what is: YesY/N?)
Except where noted otherwise, data are given for materials in their standard state (at 25 °C, 100 kPa)
Infobox references

Retinal, also called retinaldehyde or vitamin A aldehyde, is one of the many forms of vitamin A (the number of which varies from species to species). Retinal is a polyene chromophore, and bound to proteins called opsins, is the chemical basis of animal vision. Bound to proteins called type 1 rhodopsins, retinal allows certain microorganisms to convert light into metabolic energy.

Vertebrate animals ingest retinal directly from meat, or produce retinal from one of two carotenes (α-carotene, β-carotene), and also from another type of carotenoid known as β-cryptoxanthin, a type of xanthophyll, these must be obtained from plants or other photosynthetic organisms. No other carotenoids can be converted by animals to retinal, and some carnivores cannot convert any carotenoids at all. The other main forms of vitamin A, retinol, and a partially active form, retinoic acid, may both be produced from retinal.

Invertebrates such as insects and squid use hydroxylated forms of retinal in their visual systems, which derive from conversion from other xanthophylls.

Vitamin A metabolism

Living organisms produce retinal (RAL) by irreversible oxidative cleavage of carotenoids.[2] For example

beta-carotene + O2 → 2 retinal

catalyzed by a beta-carotene 15,15'-monooxygenase[3] or a beta-carotene 15,15'-dioxygenase.[4] Just as carotenoids are the precursors of retinal, retinal is the precursor of the other forms of vitamin A. Retinal is interconvertible with retinol (ROL), the transport and storage form of vitamin A

retinal + NADPH + H+ is in equilibrium with retinol + NADP+
retinol + NAD+ is in equilibrium with retinal + NADH + H+

catalyzed by retinol dehydrogenases (RDHs)[5] and alcohol dehydrogenases (ADHs).[6] Retinol is called vitamin A alcohol, or more often, simply vitamin A. Retinal can also be oxidized to retinoic acid (RA)

retinal + NAD+ + H2O → retinoic acid + NADH + H+ (catalyzed by RALDH)
retinal + O2 + H2O → retinoic acid + H2O2 (catalyzed by retinal oxidase)

catalyzed by retinal dehydrogenases[7] also known as retinaldehyde dehydrogenases (RALDHs)[6] as well as retinal oxidases.[8] Retinoic acid, sometimes called vitamin A acid, is an important signaling molecule and hormone in vertebrate animals.


Vision begins with the photoisomerization of retinal. When the 11-cis-retinal chromophore absorbs a photon it isomerizes from the 11-cis state to the all-trans state. The absorbance spectrum of the chromophore depends on its interactions with the opsin protein to which it is bound; different opsins produce different absorbance spectra.


Opsins are proteins and the retinal-binding visual pigments found in the photoreceptor cells in the retinas of eyes. An opsin is arranged into a bundle of seven transmembrane alpha-helices connected by six loops. In rod cells the opsin molecules are embedded in the membranes of the disks which are entirely inside of the cell. The N-terminus head of the molecule extends into the interior of the disk, and the C-terminus tail extends into the cytoplasm of the cell. In cone cells the disks are defined by the cell's plasma membrane so that the N-terminus head extends outside of the cell. Retinal binds covalently to a lysine on the transmembrane helix nearest the C-terminus of the protein through a Schiff base linkage. Formation of the Schiff base linkage involves removing the oxygen atom from retinal and two hydrogen atoms from the free amino group of lysine, giving H2O. Retinylidene is the divalent group formed by removing the oxygen atom from retinal, and so opsins have been called retinylidene proteins.

Opsins are prototypical G protein-coupled receptors (GPCRs).[9] Bovine rhodopsin, the opsin of the rod cells of cattle, was the first GPCR to have its X-ray structure determined.[10] Bovine rhodopsin contains 348 amino acid residues. The retinal chromophore binds at Lys296.

Although mammals use retinal exclusively as the opsin chromophore, other groups of animals additionally use four chromophores closely related to retinal. These are 3,4-didehydroretinal, (3R)-3-hydroxyretinal, (3S)-3-hydroxyretinal, and (4R)-4-hydroxyretinal. Many fish and amphibians use 3,4-didehydroretinal, also called dehydroretinal. With the exception of the dipteran suborder Cyclorrhapha, the so-called higher flies, all insects examined use the (R)-enantiomer of 3-hydroxyretinal. The (R)-enantiomer is to be expected if 3-hydroxyretinal is produced directly from xanthophyll carotenoids. Cyclorrhaphans, including Drosophila, use (3S)-3-hydroxyretinal.[11][12] Firefly squid have been found to use (4R)-4-hydroxyretinal.

Visual cycle

The visual cycle is a circular enzymatic pathway, which is the front-end of phototransduction. It regenerates 11-cis-retinal. For example, the visual cycle of mammalian rod cells is as follows:

  1. all-trans-retinyl ester + H2O → 11-cis-retinol + fatty acid; RPE65 isomerohydrolases,[13]
  2. 11-cis-retinol + NAD+ → 11-cis-retinal + NADH + H+; 11-cis-retinol dehydrogenases,
  3. 11-cis-retinol + aporhodopsinrhodopsin + H2O; forms Schiff base linkage to lysine, -CH=N+H-,
  4. rhodopsin + hν → metarhodopsin II; 11-cis photoisomerizes to all-trans,
    rhodopsin + hν → photorhodopsin → bathorhodopsin → lumirhodopsin → metarhodopsin I → metarhodopsin II,
  5. metarhodopsin II + H2O → aporhodopsin + all-trans-retinal,
  6. all-trans-retinal + NADPH + H+ → all-trans-retinol + NADP+; all-trans-retinol dehydrogenases,
  7. all-trans-retinol + fatty acid → all-trans-retinyl ester + H2O; lecithin retinol acyltransferases (LRATs).[14]

Steps 3,4,5,6 occur in rod cell outer segments; Steps 1, 2, and 7 occur in retinal pigment epithelium (RPE) cells.

RPE65 isomerohydrolases are homologous with beta-carotene monooxygenases;[2] the homologous ninaB enzyme in Drosophila has both retinal-forming carotenoid-oxygenase activity and all-trans to 11-cis isomerase activity.[15]

Type 1 rhodopsins

All-trans-retinal is also an essential component of type I, or microbial, opsins such as bacteriorhodopsin, channelrhodopsin, and halorhodopsin. In these molecules, light causes the all-trans-retinal to become 13-cis retinal,[16] which then cycles back to all-trans-retinal in the dark state.


The American biochemist George Wald and others had outlined the visual cycle by 1958. For his work, Wald won a share of the 1967 Nobel Prize in Physiology or Medicine with Haldan Keffer Hartline and Ragnar Granit.[17]

See also


Further reading

  • The oceans are full of type 1 rhodopsin.
  • Good historical review.

External links

  • First Steps of Vision - National Health Museum
  • Vision and Light-Induced Molecular Changes
  • Retinal Anatomy and Visual Capacities
  • Retinal
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