John T. Shen
Lawrence Berkeley National Laboratory
4 Papers
John T. Shen is an academic researcher from Lawrence Berkeley National Laboratory. The author has contributed to research in topics: Succinate dehydrogenase & Electron Transport Complex II. The author has an hindex of 4, co-authored 4 publications.
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Papers
3-Nitropropionic Acid Is a Suicide Inhibitor of Mitochondrial Respiration That, upon Oxidation by Complex II, Forms a Covalent Adduct with a Catalytic Base Arginine in the Active Site of the Enzyme
Li-Shar Huang,Gang Sun,David Cobessi,Andy C. Wang,John T. Shen,Eric Y. Tung,Vernon E. Anderson,Edward A. Berry +7 more
TL;DR: Three new structures of mitochondrial respiratory Complex II support the role of Arg297 as a general base catalyst accepting a proton in the dehydrogenation of succinate and suggest the residues involved in substrate binding and catalysis at the dicarboxylate site.
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•Journal Article
3-Nitropropionic Acid is a Suicide Inhibitor of Mitochondrial Respiration that, Upon Oxidation by Complex II, Forms a Covalent Adduct With a Catalytic Base Arginine in the Active Site of the Enzyme
Li-Shar Huang,Gang Sun,David Cobessi,Andy C. Wang,John T. Shen,Eric Y. Tung,Vernon E. Anderson,Edward A. Berry +7 more
TL;DR: Huang et al. as mentioned in this paper reported three new structures of mitochondrial respiratory complex II (succinate ubiquinone oxidoreductase, E.C.1) at up to 2.5.
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Crystallization of mitochondrial respiratory complex II from chicken heart: A membrane-protein complex diffracting to 2.0 A
TL;DR: A procedure is presented for preparation of diffraction-quality crystals of a vertebrate mitochondrial respiratory complex II that should allow determination of the structure of this important and medically relevant membrane-protein complex at near-atomic resolution and provide great detail of the mode of binding of substrates and inhibitors at the two substrate-binding sites.
Crystallographic studies of the binding of ligands to the dicarboxylate site of Complex II, and the identity of the ligand in the “oxaloacetate-inhibited” state
TL;DR: It may be useful for understanding the mechanism and regulation of the enzyme to identify the malate-like intermediate and its pathway of formation from oxaloacetate or fumarate, and for developing a library of UV/Vis spectral effects induced by binding different ligands to the site.