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The physiological transient complex between cytochrome f (Cf) and cytochrome c 6 (Cc 6) from the cyanobacterium Nostoc sp. PCC 7119 has been analysed by NMR spectroscopy. The binding constant at low ionic strength is 8 ± 2 mM−1, and the binding site of Cc 6 for Cf is localized around its exposed haem edge. On the basis of the experimental data, the resulting docking simulations suggest that Cc 6 binds to Cf in a fashion that is analogous to that of plastocyanin but differs between prokaryotes and eukaryotes.
Models, Molecular, Cytochromes c6, Transient interactions, Cytochrome c6, Cytochrome f, Nuclear Magnetic Resonance, Biomolecular, Cytochromes f
Models, Molecular, Cytochromes c6, Transient interactions, Cytochrome c6, Cytochrome f, Nuclear Magnetic Resonance, Biomolecular, Cytochromes f
| selected citations These citations are derived from selected sources. This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | 35 | |
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| influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | Top 10% | |
| impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network. | Average |
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