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Probing the bacteriochlorophyll binding site by reconstitution of the light-harvesting complex of Rhodospirillum rubrum with bacteriochlorophyll a analogs

Parkes-Loach, Pamela S ; Michalski, Tomasz J ; Bass, Wendy J ; Smith, Ursula ; Loach, Paul A

Biochemistry (Easton), 1990-03, Vol.29 (12), p.2951-2960 [Periódico revisado por pares]

Washington, DC: American Chemical Society

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Título:
Probing the bacteriochlorophyll binding site by reconstitution of the light-harvesting complex of Rhodospirillum rubrum with bacteriochlorophyll a analogs
Autor: Parkes-Loach, Pamela S ; Michalski, Tomasz J ; Bass, Wendy J ; Smith, Ursula ; Loach, Paul A
Assuntos: 550201 - Biochemistry- Tracer Techniques ; BACTERIA ; Bacterial Proteins - metabolism ; bacteriochlorophyll a ; Bacteriochlorophylls - chemical synthesis ; Bacteriochlorophylls - metabolism ; BASIC BIOLOGICAL SCIENCES ; BIOCHEMISTRY ; Biological and medical sciences ; CARBOXYLIC ACIDS ; Cell structures and functions ; CHEMISTRY ; CHLOROPHYLL ; Chlorophyll - analogs & derivatives ; CHLOROPHYLL-BINDING PROTEINS ; Chloroplast, photosynthetic membrane and photosynthesis ; Circular Dichroism ; DICHROISM ; Fundamental and applied biological sciences. Psychology ; HETEROCYCLIC ACIDS ; HETEROCYCLIC COMPOUNDS ; light ; Light-Harvesting Protein Complexes ; MAGNETIC CIRCULAR DICHROISM ; Magnetic Resonance Spectroscopy ; MEMBRANE PROTEINS ; MICROORGANISMS ; Molecular and cellular biology ; MOLECULAR STRUCTURE ; ORGANIC ACIDS ; ORGANIC COMPOUNDS ; ORGANIC NITROGEN COMPOUNDS ; Photosynthetic Reaction Center Complex Proteins ; PHOTOSYNTHETIC REACTION CENTERS ; PHYTOCHROMES ; PIGMENTS ; PORPHYRINS ; PROTEINS ; RECEPTORS ; RHODOSPIRILLUM ; Rhodospirillum rubrum - metabolism ; Spectrophotometry ; Structure-Activity Relationship
É parte de: Biochemistry (Easton), 1990-03, Vol.29 (12), p.2951-2960
Notas: ark:/67375/TPS-ZVFG3QV2-D
istex:46824143ADE4AE66EAF13CBF3930605125CFC448
ObjectType-Article-1
SourceType-Scholarly Journals-1
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Descrição: Structural features of bacteriochlorophyll (BChl) a that are required for binding to the light-harvesting proteins of Rhodospirillum rubrum were determined by testing for reconstitution of the B873 or B820 (structural subunit of B873) light-harvesting complexes with BChl a analogues. The results indicate that the binding site is very specific; of the analogues tested, only derivatives of BChl a with ethyl, phytyl, and geranylgeranyl esterifying alcohols and BChl b (phytyl) successfully reconstituted to form B820- and B873-type complexes. BChl analogues lacking magnesium, the C-3 acetyl group, or the C-13(2) carbomethoxy group did not reconstitute to form B820 or B873. Also unreactive were 13(2)-hydroxyBChl a and 3-acetylchlorophyll a. Competition experiments showed that several of these nonreconstituting analogues significantly slowed BChl a binding to form B820 and blocked BChl a-B873 formation, indicating that the analogues may competitively bind to the protein even though they do not form red-shifted complexes. With the R. rubrum polypeptides, BChl b formed complexes that were further red-shifted than those of BChl a; however, the energies of the red shifts, binding behavior, and circular dichroism (CD) spectra were similar. B873 complexes reconstituted with the geranylgeranyl BChl a derivative, which contains the native esterifying alcohol for R. rubrum, showed in-vivo-like CD features, but the phytyl and ethyl B873 complexes showed inverted CD features in the near infrared. The B820 complex with the ethyl derivative was about 30-fold less stable than the two longer esterifying alcohol derivatives, but all formed stable B873 complexes.
Editor: Washington, DC: American Chemical Society
Idioma: Inglês

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Probing the bacteriochlorophyll binding site by reconstitution of the light-harvesting complex of Rhodospirillum rubrum with bacteriochlorophyll a analogs

Parkes-Loach, Pamela S ; Michalski, Tomasz J ; Bass, Wendy J ; Smith, Ursula ; Loach, Paul A

Washington, DC: American Chemical Society

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