scholarly journals Genes and transcripts for the polypeptides of the cytochrome b6/f complex from spinach thylakoid membranes

1983 ◽  
Vol 2 (6) ◽  
pp. 979-986 ◽  
Author(s):  
Juliane Alt ◽  
Peter Westhoff ◽  
B.B. Sears ◽  
Nathan Nelson ◽  
Eduard Hurt ◽  
...  
2008 ◽  
Vol 1778 (4) ◽  
pp. 997-1003 ◽  
Author(s):  
Sashka B. Krumova ◽  
Cor Dijkema ◽  
Pieter de Waard ◽  
Henk Van As ◽  
Győző Garab ◽  
...  

1991 ◽  
Vol 88 (18) ◽  
pp. 8262-8266 ◽  
Author(s):  
O. Vallon ◽  
L. Bulte ◽  
P. Dainese ◽  
J. Olive ◽  
R. Bassi ◽  
...  

FEBS Letters ◽  
1981 ◽  
Vol 134 (2) ◽  
pp. 231-234 ◽  
Author(s):  
Deborah A. Berthold ◽  
Gerald T. Babcock ◽  
Charles F. Yocum

1996 ◽  
Vol 23 (3) ◽  
pp. 305 ◽  
Author(s):  
MV Sailaja ◽  
VSR Das

Highly characteristic responses of thylakoid membranes were observed in function and composition when fully developed plants of Amaranthus hypochondriacus L. grown under light sufficient (2000 μmol m-2 s-1) conditions were transferred to light limited conditions (650 μmol m-2 s-1 and 200 μmol m-2 s-1). The whole-chain, photosystem I and photosystem II electron transport rates were depressed in both bundle sheath and mesophyll thylakoids with remarkable differences between them in variation of rates under limiting light. The reduction in PSI electron transport in the mesophyll could be attributed to reduced PSI centres, while in the bundle sheath, a modulation of cytochrome b6/f complex regulated the rates of PSI electron transport. The requirement for an unaltered number of PSI centres under limiting light in the bundle sheath is ascribed to operation of an energy-consuming C4 pump.


2009 ◽  
Vol 185 (7) ◽  
pp. 1195-1207 ◽  
Author(s):  
Denis Saint-Marcoux ◽  
Francis-André Wollman ◽  
Catherine de Vitry

In chloroplasts, binding of a c′-heme to cytochrome b6 on the stromal side of the thylakoid membranes requires a specific mechanism distinct from the one at work for c-heme binding to cytochromes f and c6 on the lumenal side of membranes. Here, we show that the major protein components of this pathway, the CCBs, are bona fide transmembrane proteins. We demonstrate their association in a series of hetero-oligomeric complexes, some of which interact transiently with cytochrome b6 in the process of heme delivery to the apoprotein. In addition, we provide preliminary evidence for functional assembly of cytochrome b6f complexes even in the absence of c′-heme binding to cytochrome b6. Finally, we present a sequential model for apo- to holo-cytochrome b6 maturation integrated within the assembly pathway of b6f complexes in the thylakoid membranes.


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