Mass spectroscopy locates the extrinsic proteins of photosystem II
نویسندگان
چکیده
منابع مشابه
Mass spectroscopy locates the extrinsic proteins of photosystem II.
The photosynthetic oxidation of water is catalyzed by photosystem II (PSII), a multisubunit pigment-protein embedded in the thylakoid membranes of cyanobacteria, algae, and plants. This remarkable photoenzyme is capable of generating the highly oxidizing chemical species required to extract four tightly bound electrons of two substrate water-molecules, yielding biosynthetically useful reductant...
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Photosystem II (PSII), which catalyzes photosynthetic water oxidation, is composed of more than 20 subunits, including membrane-intrinsic and -extrinsic proteins. The PSII extrinsic proteins shield the catalytic Mn4CaO5 cluster from the outside bulk solution and enhance binding of inorganic cofactors, such as Ca(2+) and Cl(-), in the oxygen-evolving center (OEC) of PSII. Among PSII extrinsic pr...
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One form of carbonic anhydrase (CA) has been observed in maize (Zea mays) thylakoids and photosystem II (PSII)-enriched membranes. Here, we show that an antibody produced against a thylakoid lumen-targeted CA found in Chlamydomonas reinhardtii reacts with a single 33-kD polypeptide in maize thylakoids. With immunoblot analysis, we found that this single polypeptide could be identified only in m...
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In one of the final stages of cyanobacterial Photosystem II (PS II) assembly, binding of up to four extrinsic proteins to PS II stabilizes the oxygen-evolving complex (OEC). Growth of cyanobacterial mutants deficient in certain combinations of these thylakoid-lumen-associated polypeptides is sensitive to changes in environmental pH, despite the physical separation of the membrane-embedded PS II...
متن کاملSecondary structure and thermal stability of the extrinsic 23 kDa protein of photosystem II studied by Fourier transform infrared spectroscopy.
The secondary structure and thermal stability of the extrinsic 23 kDa protein (OEC23) of spinach photosystem II have been characterized in solution between 25 and 75 degrees C using Fourier transform infrared spectroscopy. Quantitative analysis of the amide I band (1700-1600 cm(-1)) shows that OEC23 contains 5% alpha-helix, 37% beta-sheet, 24% turn, and 34% disorder structures at 25 degrees C. ...
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ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 2014
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.1402022111