FEBS Letters | |
Cytochrome b 6/f complex from the cyanobacterium Synechocystis 6803: evidence of dimeric organization and identification of chlorophyll‐binding subunit | |
Barbato, Roberto1  Poggese, Chiara1  Giacometti, Giorgio M1  Polverino de Laureto, Patrizia2  Rigoni, Fernanda1  | |
[1] Dipartimento di Biologia, Università di Padova, Via Trieste 75, 35121 Padua, Italy;CRIBI, Università di Padova, Via Trieste 75, 35121 Padua, Italy | |
关键词: Cytochrome b 6/f; Pigment-binding protein; Dimeric/monomeric organization; Synechocystis 6803; Deriphat; N-lauryl iminodipropionate; disodium salt; FeS protein; iron-sulfur Rieske protein; TMBZ; N; N; N′; N′-tetramethylbenzidine; | |
DOI : 10.1016/S0014-5793(97)01078-8 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Fractionation of photosynthetic membranes from the cyanobacterium Synechocystis 6803 by polyacrylamide gel electrophoresis in the presence of Deriphat-160 allowed the isolation of a number of pigmented bands. Two of them, with molecular masses of 240±20 and 110±15 kDa respectively, showed peroxidase activity and, by means of polypeptide composition, immunoblotting and N-terminal sequencing, were identified as dimeric and monomeric cytochrome b 6/f complexes, containing 1.3±0.35 chlorophyll molecules per cytochrome f. Further fractionation of monomeric complexes by mild gel electrophoresis in the presence of sodium dodecyl sulfate indicated that it is the cytochrome b 6 polypeptide which provides the actual binding site for the chlorophyll molecule observed in the complex.
【 授权许可】
Unknown
【 预 览 】
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