K
Kiyoshi Shiga
Researcher at Kumamoto University
Publications - 51
Citations - 1423
Kiyoshi Shiga is an academic researcher from Kumamoto University. The author has contributed to research in topics: Flavin group & D-amino acid oxidase. The author has an hindex of 19, co-authored 51 publications receiving 1368 citations. Previous affiliations of Kiyoshi Shiga include Kitasato University.
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Journal ArticleDOI
A blue-light-activated adenylyl cyclase mediates photoavoidance in Euglena gracilis
Mineo Iseki,Shigeru Matsunaga,Akio Murakami,Kaoru Ohno,Kiyoshi Shiga,Kazuichi Yoshida,Michizo Sugai,Tetsuo Takahashi,Terumitsu Hori,Masakatsu Watanabe,Masakatsu Watanabe +10 more
TL;DR: A new type of blue-light receptor flavoprotein, photoactivated adenylyl cyclase, is found in the photoreceptor organelle of Euglena gracilis, with molecular genetic evidence that it mediates the step-up photophobic response.
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Dynamics and Mechanisms of Ultrafast Fluorescence Quenching Reactions of Flavin Chromophores in Protein Nanospace
TL;DR: In this article, a femtosecond fluorescence up-conversion method was used to study the excited-state dynamics of non-fluorescent flavoproteins including riboflavin binding protein (RBP), d-amino acid oxidase benzoate complex (DAOB), and others.
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Three-Dimensional Structure of Porcine Kidney D-Amino Acid Oxidase at 3.0 Å Resolution
Hisashi Mizutani,Ikuko Miyahara,Ken Hirotsu,Yasuzo Nishina,Kiyoshi Shiga,Chiaki Setoyama,Retsu Miura +6 more
TL;DR: The X-ray crystallographic structure of porcine kidney D-amino acid oxidase, which had been expressed in Escherichia coli transformed with a vector containing DAO cDNA, was determined by the isomorphous replacement method for the complex form with benzoate.
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Structural and Mechanistic Studies on D-Amino Acid Oxidase-Substrate Complex: Implications of the Crystal Structure of Enzyme-Substrate Analog Complex.
Retsu Miura,Chiaki Setoyama,Yasuzo Nishina,Kiyoshi Shiga,Hisashi Mizutani,Ikuko Miyahara,Ken Hirotsu +6 more
TL;DR: This model enables the evaluation of the substrate-flavin interaction prior to electron transfer from the substrate to flavin and provides two possible mechanisms for the reductive-half reaction of DAO, i.e., the electron-proton-electron transfer mechanism and the ionic mechanism.
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Unusually high standard redox potential of acrylyl-CoA/propionyl-CoA couple among enoyl-CoA/acyl-CoA couples: a reason for the distinct metabolic pathway of propionyl-CoA from longer acyl-CoAs.
TL;DR: The molecular orbital calculations (MOPAC) for the enoyl and acyl forms of C(3) and C(4) revealed that this structural feature is the main cause for the higher standard redox potential of the C( 3) couple.