Removal of the H subunit results in enhanced exposure of the semiquinone sites in the LM dimer from Rhodobacter sphaeroides to oxidation by ferricyanide and by O2
Author:
Funder
National Science Foundation
Publisher
Springer Science and Business Media LLC
Subject
Cell Biology,Plant Science,Biochemistry,General Medicine
Link
http://link.springer.com/article/10.1007/s11120-017-0404-9/fulltext.html
Reference30 articles.
1. Agalidis I, Reiss-Husson F (1983) Several properties of the LM unit extracted with sodium dodecyl sulfate from Rhodopseudomonas sphaeroides purified reaction centers. Biochim Biophys Acta. doi: 10.1016/0005-2728(83)90093-2
2. Agalidis I, Nuijs AM, Reiss-Husson F (1987) Characterization of an LM unit purified by affinity chromatography from Rhodobacter sphaeroides reaction centers and interactions with the H subunit. Biochim Biophys Acta 890(2):242–250. doi: 10.1016/0005-2728(87)90025-9
3. Bensasson R, Land EJ (1973) Optical and kinetic properties of semireduced plastoquinone and ubiquinone: electron acceptors in photosynthesis. Biochim Biophys Acta 325(1):175–181. doi: 10.1016/0005-2728(73)90163-1
4. Clayton RK, Wang RT (1971) [69] Photochemical reaction centers from Rhodopseudomonas spheroides. In: Methods in enzymology, vol 23. Academic Press, New York, pp 696–704. doi: 10.1016/S0076-6879(71)23145-1
5. Debus RJ, Feher G, Okamura MY (1985) LM complex of reaction centers from Rhodopseudomonas sphaeroides R-26: characterization and reconstitution with the H subunit. Biochemistry 24:2488–2500
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