期刊
ANTIOXIDANTS & REDOX SIGNALING
卷 36, 期 16-18, 页码 1101-1118出版社
MARY ANN LIEBERT, INC
DOI: 10.1089/ars.2021.0114
关键词
respiratory supercomplex; lipid-preserving state; cryo-EM structure; dynamic substrate pool; intercomplex movement
资金
- Hanyang University internal grant
- biomedical technology development project, National Research Foundation, Korea [NRF-2015M3A9B5030302, 2017R1A3B1023591, IBS-R030-C1]
- Institute for Basic Science (IBS) [2021M3A9G8024747 to S.E.R. and 2017R1A3B1023591]
- [2021M3A9G8024747]
- National Research Foundation of Korea [2015M3A9B5030302, 2017R1A3B1023591] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
In this study, cryoelectron microscopy was used to investigate bovine respiratory supercomplexes, revealing large intercomplex motions and a dynamic substrate pool between complexes I and III. These findings provide insights into the regulation of metabolic flux and reactive oxygen species by supercomplexes.
Aims: Mitochondrial respiratory supercomplexes mediate redox electron transfer, generating a proton gradient for ATP synthesis. To provide structural information on the function of supercomplexes in physiologically relevant conditions, we conducted cryoelectron microscopy studies with supercomplexes in a lipid-preserving state.Results: Here, we present cryoelectron microscopy structures of bovine respiratory supercomplex I1III2IV1 by using a lipid-preserving sample preparation. The preparation greatly enhances the intercomplex quinone transfer activity. The structures reveal large intercomplex motions that result in different shapes and sizes of the intercomplex space between complexes I and III, forming a dynamic substrate pool. Biochemical and structural analyses indicated that intercomplex phospholipids mediate the intercomplex motions. An analysis of the different classes of focus-refined complex I showed that structural switches due to quinone reduction led to the formation of a novel channel that could transfer reduced quinones to the intercomplex substrate pool.Innovation and Conclusion: Our results indicate potential mechanism for the facilitated electron transfer involving a dynamic substrate pool and intercomplex movement by which supercomplexes play an active role in the regulation of metabolic flux and reactive oxygen species.
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