C
Chang Sun
Researcher at University of Illinois at Urbana–Champaign
Publications - 16
Citations - 416
Chang Sun is an academic researcher from University of Illinois at Urbana–Champaign. The author has contributed to research in topics: Cytochrome c oxidase & Coenzyme Q – cytochrome c reductase. The author has an hindex of 7, co-authored 15 publications receiving 297 citations.
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Journal ArticleDOI
Structure of the alternative complex III in a supercomplex with cytochrome oxidase
Chang Sun,Samir Benlekbir,Padmaja Venkatakrishnan,Padmaja Venkatakrishnan,Yuhang Wang,Sangjin Hong,Jonathan P. Hosler,Emad Tajkhorshid,John L. Rubinstein,Robert B. Gennis +9 more
TL;DR: The structure of alternative complex III, a key enzyme in the bacterial electron transport chain, is reported both alone and as a supercomplex with an aa3-type cytochrome c oxidase.
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Characterization of Lipid-Protein Interactions and Lipid-Mediated Modulation of Membrane Protein Function through Molecular Simulation.
Melanie P. Muller,Melanie P. Muller,Tao Jiang,Chang Sun,Muyun Lihan,Shashank Pant,Paween Mahinthichaichan,Anda Trifan,Emad Tajkhorshid +8 more
TL;DR: A broad survey of MD simulations focusing on exploring lipid-protein interactions and characterizing lipid-modulated protein structure and dynamics that have been successful in providing novel insight into the mechanism of membrane protein function is provided.
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Single-particle cryo-EM studies of transmembrane proteins in SMA copolymer nanodiscs.
Chang Sun,Robert B. Gennis +1 more
TL;DR: Three recent cryo-EM studies on the efflux transporter AcrB and the alternative complex III: cyt c oxidase supercomplex have demonstrated the potential of SMA nanodisc samples to yield high-resolution structure information of membrane proteins.
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Location of the Substrate Binding Site of the Cytochrome bo3 Ubiquinol Oxidase from Escherichia coli.
TL;DR: Cytochrome bo3 is a respiratory proton-pumping oxygen reductase that is a member of the heme-copper superfamily that utilizes ubiquinol-8 (Q8H2) as a substrate and the current work shows that the Q8 bound to the QH site is more dynamic than previously thought.
Journal ArticleDOI
Ultrafast Electron Transfer Kinetics in the LM Dimer of Bacterial Photosynthetic Reaction Center from Rhodobacter sphaeroides.
TL;DR: The results are consistent with the concept that the removal of the H-subunit results in increased flexibility in the region around the quinone and an associated shift in the reorganization energy associated with charge separation and recombination.