Cytochrome b 559 in Photosystem II

Müh, Frank; Zouni, Athina

doi:10.1007/978-94-017-7481-9_8

Cited by 9 publications

(16 citation statements)

References 142 publications

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“…This list demands some comments: PsbE and F are particular in that they bind a heme group and thus constitute the α‐ and β‐subunit, respectively, of cytochrome b 559 . Like its membrane‐extrinsic heme‐binding counterpart in cyanobacteria, red algae and diatoms, cyt c 550 (PsbV, see above), cyt b 559 has no function that could so far unambiguously be assigned to it . PsbY is closely attached to PsbE/F and could be considered part of cyt b 559 , if it were not apparently absent in all but the cyanobacterial lineage.…”

Section: Subunits Of the Core Complexmentioning

confidence: 99%

“…Like its membrane‐extrinsic heme‐binding counterpart in cyanobacteria, red algae and diatoms, cyt c 550 (PsbV, see above), cyt b 559 has no function that could so far unambiguously be assigned to it . PsbY is closely attached to PsbE/F and could be considered part of cyt b 559 , if it were not apparently absent in all but the cyanobacterial lineage. However, a psbY gene is found in algae and plants suggesting that PsbY is either not permanently bound to PSIIcc or lost in the biochemical preparation.…”

Section: Subunits Of the Core Complexmentioning

confidence: 99%

“…The two extra Chls, Chlz D1 , and Chlz D2 bound to PsbA and PsbD, respectively, do not belong to the RC. Their function is unclear, but Chlz D2 may be involved in slow ET reactions associated with cyt b 559 …”

Section: Pigments and Lipids Of The Core Complexmentioning

confidence: 99%

“…We propose that these two Car should be referred to by their traditional names Car D1 and Car D2 , not least because they are in close contact with Chlz D1 and Chlz D2 , respectively (Figure ). As with Chlz D2 , Car D2 may be involved in redox reactions …”

Section: Pigments and Lipids Of The Core Complexmentioning

confidence: 99%

“…β‐Carotene: Car D1 , Car D2 ; yellow. Heme: cytochrome b 559 ; red. Nonheme iron: Fe with bound bicarbonate .…”

Section: Introductionmentioning

confidence: 99%

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Structural basis of light‐harvesting in the photosystem II core complex

Müh

Zouni

2020

Protein Science

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Photosystem II (PSII) is a membrane-spanning, multi-subunit pigment-protein complex responsible for the oxidation of water and the reduction of plastoquinone in oxygenic photosynthesis. In the present review, the recent explosive increase in available structural information about the PSII core complex based on X-ray crystallography and cryo-electron microscopy is described at a level of detail that is suitable for a future structure-based analysis of light-harvesting processes. This description includes a proposal for a consistent numbering scheme of protein-bound pigment cofactors across species. The structural survey is complemented by an overview of the state of affairs in structure-based modeling of excitation energy transfer in the PSII core complex with emphasis on electrostatic computations, optical properties of the reaction center, the assignment of long-wavelength chlorophylls, and energy trapping mechanisms.

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Section: Subunits Of the Core Complexmentioning

confidence: 99%

Section: Subunits Of the Core Complexmentioning

confidence: 99%

Section: Pigments and Lipids Of The Core Complexmentioning

confidence: 99%

Section: Pigments and Lipids Of The Core Complexmentioning

confidence: 99%

“…β‐Carotene: Car D1 , Car D2 ; yellow. Heme: cytochrome b 559 ; red. Nonheme iron: Fe with bound bicarbonate .…”

Section: Introductionmentioning

confidence: 99%