User:Clara Costa D'Elia/Sandbox 1

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== Function ==
== Function ==
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Purple bacterial light-harvesting complexes modify the absorption properties of their chromophores to wavelengths such that the spectrum available to them in vivo is maximised; and the energy so absorbed is productively transferred and made available for photochemistry.
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The environment of the chromophores in the light-harvesting complex is governed by protein. The protein creates the conditions determining the relative disposition of the pigments, and contributes to the local environment that modulates their absorption spectra.
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In order to increase the spectral cross-section of absorption, purple bacteria also produce light-harvesting complexes. In most cases a primary light-harvesting complex (LH1) and peripheral light-harvesting complexes (LH2) are synthesised
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LH2 complexes are produced in variable amounts according to the available light levels, the absorbance range of the particular LH2 (800 and 850, 800 and 820 nm), the temperature, and the bacterial species and strain (Zuber & Brunisholz, 1991).
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When purple bacteria are grown under anaerobic conditions they incorporate the photosynthetic apparatus described above into invaginated intracytoplasmic phospholipid membranes. RC, LH1 and LH2 are integral trans-membrane assemblies. After absorption of a photon by a pigment molecule all energy transfer processes occur within the membrane until energy is “trapped” by the RC complex
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Each individual light-harvesting complex is composed of oligomers of short peptides (α and β) with associated pigments (Hawthornthwaite & Cogdell, 1991). αβ apoproteins with their non-covalently bound carotenoid and bacteriochlorophyll (Bchl ) pigments form the multi-subunit complexes LH1 and LH2
== Disease ==
== Disease ==

Revision as of 13:50, 9 May 2022

Light Harvesting Complex II

Caption for this structure

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References

  1. Hanson, R. M., Prilusky, J., Renjian, Z., Nakane, T. and Sussman, J. L. (2013), JSmol and the Next-Generation Web-Based Representation of 3D Molecular Structure as Applied to Proteopedia. Isr. J. Chem., 53:207-216. doi:http://dx.doi.org/10.1002/ijch.201300024
  2. Herraez A. Biomolecules in the computer: Jmol to the rescue. Biochem Mol Biol Educ. 2006 Jul;34(4):255-61. doi: 10.1002/bmb.2006.494034042644. PMID:21638687 doi:10.1002/bmb.2006.494034042644

Proteopedia Page Contributors and Editors (what is this?)

Clara Costa D'Elia

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