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Chemical Communications (Cambridge, England)|May 26, 2012
A heme degradation enzyme, HutZ, from Vibrio choleraeTakeshi Uchida, Yukari Sekine, Toshitaka Matsui, et al.
The Journal of Biological Chemistry|November 6, 2004
Roles of distal Asp in heme oxygenase from Corynebacterium diphtheriae, HmuO: A water-driven oxygen activation mechanismToshitaka Matsui, Momoko Furukawa, Masaki Unno, et al.
Inorganic Chemistry|April 13, 2010
Dioxygen activation for the self-degradation of heme: reaction mechanism and regulation of heme oxygenaseToshitaka Matsui, Mari Iwasaki, Ryota Sugiyama, et al.
Angewandte Chemie (International Ed. in English)|March 1, 2021
Optical Manipulation of Subcellular Protein Translocation Using a Photoactivatable Covalent Labeling SystemToshiyuki Kowada, Keisuke Arai, Akimasa Yoshimura, et al.
Journal of the American Chemical Society|December 25, 2003
Kinetic isotope effects on the rate-limiting step of heme oxygenase catalysis indicate concerted proton transfer/heme hydroxylationRoman Davydov, Toshitaka Matsui, Hiroshi Fujii, et al.
The Journal of Biological Chemistry|February 20, 2013
A new way to degrade heme: the Mycobacterium tuberculosis enzyme MhuD catalyzes heme degradation without generating COShusuke Nambu, Toshitaka Matsui, Celia W Goulding, et al.
Chemical Communications (Cambridge, England)|December 20, 2007
Ligand design for the improvement of stability of metal complex.protein hybridsNorihiko Yokoi, Takafumi Ueno, Masaki Unno, et al.
Journal of the American Chemical Society|January 26, 2006
Compound I of heme oxygenase cannot hydroxylate its heme meso-carbonToshitaka Matsui, Sun Hee Kim, Hiromichi Jin, et al.
Nature Chemical Biology|June 18, 2024
Quantitative control of subcellular protein localization with a photochromic dimerizerTakato Mashita, Toshiyuki Kowada, Hayashi Yamamoto, et al.
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