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So Iwata

Researcher at Kyoto University

Publications -  298
Citations -  26540

So Iwata is an academic researcher from Kyoto University. The author has contributed to research in topics: Membrane protein & Receptor. The author has an hindex of 68, co-authored 272 publications receiving 23718 citations. Previous affiliations of So Iwata include University of Tokyo & Max Planck Society.

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Journal ArticleDOI

Architecture of the Photosynthetic Oxygen-Evolving Center

Kristina N. Ferreira, +4 more
- 19 Mar 2004 - 
TL;DR: The data strongly suggest that the OEC contains a cubane-like Mn3CaO4 cluster linked to a fourth Mn by a mono-μ-oxo bridge, and the details of the surrounding coordination sphere of the metal cluster and the implications for a possible oxygen-evolving mechanism are discussed.
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Structure at 2.8 A resolution of cytochrome c oxidase from Paracoccus denitrificans.

So Iwata, +3 more
- 24 Aug 1995 - 
TL;DR: The crystal structure at 2.8 Å resolution of the four protein subunits containing cytochrome c oxidase from the soil bacterium Paracoccus denitrificans, complexed with an antibody Fv fragment, is described and mechanisms for proton pumping are discussed.
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Structure and mechanism of the lactose permease of Escherichia coli

Jeff Abramson, +5 more
- 01 Aug 2003 - 
TL;DR: The crystal structure at 3.5 angstroms of the Escherichia coli lactose permease reveals the sugar-binding site in the cavity, and residues that play major roles in substrate recognition and proton translocation are identified.
Journal ArticleDOI

Complete structure of the 11-subunit bovine mitochondrial cytochrome bc1 complex.

So Iwata, +8 more
- 03 Jul 1998 - 
TL;DR: In this article, crystal structures of the 11-subunit bc1 complex from bovine heart reveal full views of this bifunctional enzyme, and the "Rieske" iron-sulfur protein subunit shows significant conformational changes in different crystal forms.
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Architecture of succinate dehydrogenase and reactive oxygen species generation.

Victoria Yankovskaya, +11 more
- 31 Jan 2003 - 
TL;DR: The structure of Escherichia colisuccinate dehydrogenase (SQR), analogous to the mitochondrial respiratory complex II, has been determined, revealing the electron transport pathway from the electron donor, succinate, to the terminal electron acceptor, ubiquinone.