An atypical haem in the cytochrome b6f complex

By David Stroebel, Y. Choquet, J. Popot, D. Picot. Nature, 2003

660 citations recorded by the source corpus.

Subfields: Atomic and Molecular Physics, and Optics, Cell Biology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/59e6206c40706cb4cb7ef654ec4051904e96a225

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In Atomic and Molecular Physics, and Optics

In Cell Biology

Robert Eugene Blankenship

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Citations in the corpus

The evolution of the plastid chromosome in land plants: gene content, gene order, gene function (2011, background): “These participate in electron transfer, generating a proton gradient across the thylakoid membrane (Stroebel et al. 2003).”
Chlorophyll a Fluorescence: A Bit of Basics and History (2004, background): “The most intriguing observation is the existence of a single Chl a molecule in Cyt b6 f complex (Kurisu et al., 2003; Stroebel et al., 2003).”
Supramolecular organization of thylakoid membrane proteins in green plants. (2005, background): “5 nm [10,11,113].”
Structure and function of photosystems I and II. (2006, background): “Thus, heme x could function in Fddependent cyclic electron transport (70, 178, 280).”
Molecular mechanisms of photosynthesis (2002, background): “This was first discovered in the cytochrome b6 f complex isolated from the green alga Chlamydomonas reinhardtii (Stroebel et al., 2003), but is also found in the complex from cyanobacteria.”
An Overview of Chlorophylls and Bacteriochlorophylls: Biochemistry, Biophysics, Functions and Applications (2006, background): “…cytochrome b6 f complex located between the two photosystems in oxygenic organisms (Pierre et al., 1997; Peterman et al., 1998; Kurisu et al., 2003; Stroebel et al., 2003), and several plant species contain non-photosynthetic, watersoluble Chl proteins which may serve for storage or transport of…”
Integrating the proton circuit into photosynthesis: progress and challenges (2005, background): “(4) Finally, the cyt b6f complex itself has been suggested to act as a ferredoxin:PQ oxidoreductase, as supported by the discovery of an unexpected heme group, termed heme ci or heme x, in the recent X-ray structures (Kurisu et al. 2003; Stroebel et al. 2003).”