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plastocyanin/karijes

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ČlanciKliničkim ispitivanjimaPatenti
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The location of plastocyanin in vascular plant photosystem I.

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We have studied the binding sites of the electron donor and acceptor proteins of vascular plant photosystem I by electron microscopy/crystallography. Previously, we identified the binding site for the electron acceptor (ferredoxin). In this paper we complete these studies with the characterization

Cryo-EM structure of the spinach cytochrome b6 f complex at 3.6 Å resolution.

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The cytochrome b6 f (cytb6 f ) complex has a central role in oxygenic photosynthesis, linking electron transfer between photosystems I and II and converting solar energy into a transmembrane proton gradient for ATP synthesis1-3. Electron transfer within

HMA6 and HMA8 are two chloroplast Cu+-ATPases with different enzymatic properties.

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Copper (Cu) plays a key role in the photosynthetic process as cofactor of the plastocyanin (PC), an essential component of the chloroplast photosynthetic electron transfer chain. Encoded by the nuclear genome, PC is translocated in its apo-form into the chloroplast and the lumen of thylakoids where
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