Bacteriochlorin-protein interactions in native B800-B850, B800 deficient and B800-Bchlap-reconstituted complexes fromRhodopseudomonas acidophila, strain 10050

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B800-->B850 energy transfer mechanism in bacterial LH2 complexes investigated by B800 pigment exchange.

Femtosecond transient absorption measurements were performed on native and a series of reconstituted LH2 complexes from Rhodopseudomonas acidophila 10050 at room temperature. The reconstituted complexes contain chemically modified tetrapyrrole pigments in place of the native bacteriochlorophyll a-B800 molecules. The spectral characteristics of the modified pigments vary significantly, such that...

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The complete amino acid sequences of the B800-850 antenna polypeptides from Rhodopseudomonas acidophila strain 7750.

Spectrally pure B800-850 light harvesting complexes of Rhodopseudomonas acidophila 7750 were prepared by chromatography of LDAO-solubilised photosynthetic membranes on Whatmann DE-52 ion exchange resin. Two low molecular mass polypeptides (alpha, beta) have been isolated by organic solvent extraction of the lyophilised B800-850 light harvesting complexes. Their primary structures were determine...

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Light-harvesting II (B800-B850 complex) structural genes from Rhodopseudomonas capsulata.

The light-harvesting II (LHII) structural genes coding for the (B800-B850 complex) beta- and alpha-polypeptides have been cloned and the nucleotide and deduced polypeptide sequences have been determined. This completes the sequencing of all seven structural genes coding for the structural polypeptides of the photosynthetic apparatus that bind the pigments and cofactors participating in the prim...

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The crystallographic structure of the B800-820 LH3 light-harvesting complex from the purple bacteria Rhodopseudomonas acidophila strain 7050.

The B800-820, or LH3, complex is a spectroscopic variant of the B800-850 LH2 peripheral light-harvesting complex. LH3 is synthesized by some species and strains of purple bacteria when growing under what are generally classed as "stressed" conditions, such as low intensity illumination and/or low temperature (<30 degrees C). The apoproteins in these complexes modify the absorption properties of...

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ژورنال

عنوان ژورنال: FEBS Letters

سال: 1999

ISSN: 0014-5793

DOI: 10.1016/s0014-5793(99)00410-x