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|a pubmed25n0491.xml
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|a (DE-627)NLM147130271
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|a (NLM)15012298
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|a DE-627
|b ger
|c DE-627
|e rakwb
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|a eng
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|a Cramer, W. A.
|e verfasserin
|4 aut
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|a SOME NEW STRUCTURAL ASPECTS AND OLD CONTROVERSIES CONCERNING THE CYTOCHROME b6f COMPLEX OF OXYGENIC PHOTOSYNTHESIS
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|c 1996
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|a Text
|b txt
|2 rdacontent
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|a ohne Hilfsmittel zu benutzen
|b n
|2 rdamedia
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|a Band
|b nc
|2 rdacarrier
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|a Date Revised 09.01.2024
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|a published: Print
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|a Citation Status Publisher
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|a The cytochrome b6f complex functions in oxygenic photosynthetic membranes as the redox link between the photosynthetic reaction center complexes II and I and also functions in proton translocation. It is an ideal integral membrane protein complex in which to study structure and function because of the existence of a large amount of primary sequence data, purified complex, the emergence of structures, and the ability of flash kinetic spectroscopy to assay function in a readily accessible ms-100 mus time domain. The redox active polypeptides are cytochromes f and b6 (organelle encoded) and the Rieske iron-sulfur protein (nuclear encoded) in a mol wt = 210,000 dimeric complex that is believed to contain 22-24 transmembrane helices. The high resolution structure of the lumen-side domain of cytochrome f shows it to be an elongate (75 A long) mostly beta-strand, two-domain protein, with the N-terminal alpha-amino group as orthogonal heme ligand and an internal linear 11-A bound water chain. An unusual electron transfer event, the oxidant-induced reduction of a significant fraction of the p (lumen)-side cytochrome b heme by plastosemiquinone indicates that the electron transfer pathway in the b6f complex can be described by a version of the Q-cycle mechanism, originally proposed to describe similar processes in the mitochondrial and bacterial bc1 complexes
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|a Journal Article
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|a Soriano, G. M.
|e verfasserin
|4 aut
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|a Ponomarev, M.
|e verfasserin
|4 aut
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|a Huang, D.
|e verfasserin
|4 aut
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|a Zhang, H.
|e verfasserin
|4 aut
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|a Martinez, S. E.
|e verfasserin
|4 aut
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|a Smith, J. L.
|e verfasserin
|4 aut
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|i Enthalten in
|t Annual review of plant physiology and plant molecular biology
|d 1990
|g 47(1996) vom: 17. Juni, Seite 477-508
|w (DE-627)NLM098188720
|x 1040-2519
|7 nnns
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|g volume:47
|g year:1996
|g day:17
|g month:06
|g pages:477-508
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|a AR
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|d 47
|j 1996
|b 17
|c 06
|h 477-508
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