Delipidation of cytochrome c oxidase from Rhodobacter sphaeroides destabilizes its quaternary structure.

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Delipidation of cytochrome c oxidase from Rhodobacter sphaeroides destabilizes its quaternary structure.

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2016 nî lūn-bûn

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2016年の論文

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2016年論文

@yue

2016年論文

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2016年論文

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2016年論文

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2016年論文

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2016年论文

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2016年论文

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2016年论文

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Delipidation of cytochrome c o ...... izes its quaternary structure.

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Delipidation of cytochrome c o ...... izes its quaternary structure.

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Delipidation of cytochrome c o ...... izes its quaternary structure.

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P1476

Delipidation of cytochrome c o ...... izes its quaternary structure.

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P2093

Andrej Musatov

http://www.w3.org/2001/XMLSchema#string

Jonathan P Hosler

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Rastislav Varhač

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P2860

Crystal structures of photosynthetic reaction center and high-potential iron-sulfur protein from Thermochromatium tepidum: thermostability and electron transfer

Specific roles of protein-phospholipid interactions in the yeast cytochrome bc1 complex structure.

The X-ray crystal structures of wild-type and EQ(I-286) mutant cytochrome c oxidases from Rhodobacter sphaeroides

Disruption of a specific molecular interaction with a bound lipid affects the thermal stability of the purple bacterial reaction centre

Structures and physiological roles of 13 integral lipids of bovine heart cytochrome c oxidase

The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 A

Membrane protein folding and stability: physical principles

Mass spectrometric detection of protein, lipid and heme components of cytochrome c oxidase from R. sphaeroides and the stabilization of non-covalent complexes from the enzyme.

Cardiolipin deficiency in Rhodobacter sphaeroides alters the lipid profile of membranes and of crystallized cytochrome oxidase, but structure and function are maintained

Phospholipase digestion of bound cardiolipin reversibly inactivates bovine cytochrome bc1.

P304

23-31

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P31

scholarly article

P356

10.1016/J.BIOCHI.2016.02.013

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P478

125

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P50

Erik Sedlák

P577

2016-02-25T00:00:00Z

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P5875

296480863

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P698

26923069

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P932

4867122

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