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1.
Sci Adv ; 8(47): eabo4492, 2022 Nov 25.
Artículo en Inglés | MEDLINE | ID: mdl-36427300

RESUMEN

Fractional crystallization plays a critical role in generating the differentiated continental crust on Earth. However, whether efficient crystal-melt separation can occur in viscous felsic magmas remains a long-standing debate because of the difficulty in discriminating between differentiated melts and complementary cumulates. Here, we found large (~1 per mil) potassium isotopic variation in 54 strongly peraluminous high-silica (silicon dioxide >70 weight %) leucogranites from the Himalayan orogen, with potassium isotopes correlated with trace elemental proxies (e.g., strontium, rubidium/strontium, and europium anomaly) for plagioclase crystallization. Quantitative modeling requires up to ~60 to 90% fractional crystallization to account for the progressively light potassium isotopic composition of the fractionated leucogranites, while plagioclase accumulation results in enrichment of heavy potassium isotopes in cumulate leucogranites. Our findings strongly support fractional crystallization of high-silica magmas and highlight the great potential of potassium isotopes in studying felsic magma differentiation.

2.
Science ; 370(6519)2020 11 20.
Artículo en Inglés | MEDLINE | ID: mdl-33214250

RESUMEN

The photosynthetic apparatus of green sulfur bacteria (GSB) contains a peripheral antenna chlorosome, light-harvesting Fenna-Matthews-Olson proteins (FMO), and a reaction center (GsbRC). We used cryo-electron microscopy to determine a 2.7-angstrom structure of the FMO-GsbRC supercomplex from Chlorobaculum tepidum The GsbRC binds considerably fewer (bacterio)chlorophylls [(B)Chls] than other known type I RCs do, and the organization of (B)Chls is similar to that in photosystem II. Two BChl layers in GsbRC are not connected by Chls, as seen in other RCs, but associate with two carotenoid derivatives. Relatively long distances of 22 to 33 angstroms were observed between BChls of FMO and GsbRC, consistent with the inefficient energy transfer between these entities. The structure contains common features of both type I and type II RCs and provides insight into the evolution of photosynthetic RCs.


Asunto(s)
Proteínas Bacterianas/química , Chlorobi/enzimología , Fotosíntesis , Complejo de Proteína del Fotosistema I/química , Complejo de Proteína del Fotosistema II/química , Microscopía por Crioelectrón , Citoplasma/enzimología , Transferencia de Energía , Periplasma/enzimología , Conformación Proteica
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