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Biochemistry. 2008 May 13;47(19):5259-65. doi: 10.1021/bi800179b. Epub 2008 Apr 12.

b6f-Associated chlorophyll: structural and dynamic contribution to the different cytochrome functions.

Author information

1
UMR 7099, CNRS and Université Paris-7, and UMR 7141, CNRS and Université Paris-6, Institut de Biologie Physico-Chimique, 13 rue Pierre et Marie Curie, F-75005 Paris, France.

Abstract

Cytochromes bc1/b6f complexes catalyze electron transfer from lipid- to water-soluble carriers in both the respiratory and photosynthetic processes. They contain several common redox cofactors, while a chlorophyll a molecule, the function of which is still enigmatic, is only present in b b6f-type complexes. In this work, we describe a mutagenesis approach aimed at characterizing the role of this pigment. Mutants of the binding pocket were constructed to obtain cytochrome (cyt) b6f f complexes altered in chlorophyll position and/or stability. On the basis of a combined biochemical and functional analysis, we conclude that the chlorophyll plays a major structural role in the complex. Moreover, the chlorophyll and its binding pocket may also be implicated in the regulation of photosynthetic state transitions, a function that is specific to cyt b6f complexes.

PMID:
18407657
DOI:
10.1021/bi800179b
[Indexed for MEDLINE]

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