Titlebook: Oxygen Homeostasis and Its Dynamics; Yuzuru Ishimura (Professor and Chairman),Hideo Shi Conference proceedings 1998 Springer-Verlag Tokyo

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Rapid Formation of a Semiquinone Species on Oxidation of Quinol by the Cytochrome ,, Oxidase from ,inol oxidase is cytochrome .. from .. In this work, the initial oxidation of ubiquinol by this ubiquinol oxidase is examined. Stopped-flow UV-visible spectroscopy and rapid freeze-quench electron paramagnetic resonance (EPR) spectroscopies were used to examine the oxidation of ubiquinol-2 (UQ.H.) by

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Coupling of Ion and Charge Movements: From Peroxidases to Protonmotive Oxidasesropriately placed residues. Such protonations can be important in peroxidases and other soluble proteins, and are likely to be central to the protonmotive mechanism of oxidases. Three residues in subunit I of cytochrome oxidase that are likely to interfere with such protonations have been examined b

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Ligand Dynamics in the Binuclear Site in Cytochrome Oxidase proton delivery and efflux channels in the protein that are relevant to substrate reduction and proton pumping is considered, and the current status of this area is summarized. Carbon monoxide photodissociation and the ligand dynamics that occur subsequent to photolysis have been valuable tools in

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Redox Behavior of Copper A in Cytochrome Oxidase in the Brain In Vivo: Its Clinical Significancef the redox state of cytochrome oxidase resolves the most difficult problem, that the in vivo absorption coefficient of cytochrome oxidase is unknown, in addition to other problems such as the light-scattering effects and marked overlap of absorbance changes attributed to hemoglobin. We applied this

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Crystallization of Bovine Heart Mitochondrial Cytochrome , Oxidase for X-Ray Diffraction at Atomic Ronent membrane protein. Three of these crystals (hexagonal bipyramidal, tetragonal plate, and tetragonal column) were obtained from an enzyme preparation stabilized with alkyl polyethelene glycol monoether-type detergents. The tetragonal column crystals diffracted X-rays up to 5Å resolution, but thi

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Coupling of Proton Transfer to Oxygen Chemistry in Cytochrome Oxidase: the Roles of Residues I67 and. In this chapter, we describe the effects of a mutation in the residue I67. The mutation alters the redox properties of heure ., probably by perturbing the pK of E243, a conserved residue that we propose to be a protonation site that is redox-linked to heme . This mutation has little effect on the

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