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By Hartmut Michel, So Iwata, Christian Ostermeier (auth.), Yuzuru Ishimura M.D., Ph.D., Hideo Shimada Ph.D., Makoto Suematsu M.D., Ph.D. (eds.)

This first quantity in a projected sequence includes the lawsuits of the 1st of the Keio collage overseas Symposia for all times Sciences and drugs below the sponsorship of the Keio college scientific technological know-how Fund. As said within the deal with through the President of Keio collage on the beginning of the 1996 symposium, the fund of Dr. Mitsunada Sakaguchi. The Keio used to be demonstrated through the beneficiant donation college overseas Symposia for all times Sciences and drugs represent one of many middle actions of the fund. the target is to give a contribution to the overseas neighborhood via constructing human assets, selling medical wisdom, and inspiring mutual alternate. each year, the administrative Committee of the Interna­ tional Symposia for all times Sciences and drugs selects the main attention-grabbing subject matters for the symposium from functions obtained in line with a decision for papers to the Keio clinical group. The book of those complaints is meant to publicize and distribute details coming up from the full of life discussions of the main intriguing and present matters in the course of the symposium. Weare thankful to Dr. Mitsunada Sakaguchi, who made the symposium attainable, the individuals of this system committee, and the workplace employees whose aid guaran­ teed the good fortune of the symposium. eventually, we thank Springer-Verlag, Tokyo, for his or her information in publishing this paintings. Akimichi Kaneko, M. D. , Ph. D.

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Example text

It is a member of the superfamily of heme-copper terminal oxidases, as is cytochrome c oxidase [1], for which two crystal structures have recently been solved [2-4]. Cytochrome b0 3 catalyzes the two-electron oxidation of ubiquinol-8 in the bacterial membrane and reduces dioxygen to water. For each dioxygen, four protons are pumped electrogenically across the membrane bilayer, contributing to the generation of a protonmotive force. In addition, four protons are released into the bacterial periplasm and another four protons (per 02) are taken up from the bacterial cytoplasm to form water (2H 20).

Considering the fact that the dicyanovinyl group is bulky and conformationally rigid, the para-substituent of the molecule may be out of a binding pocket for the benzoquinone ring. Among the BQ derivatives examined, 2,6-dimethyl-BQ (see Fig. 1) was found to be the most potent competitive inhibitor, and 2-methyl-BQ and 2,6-dichloro-BQ were comparable to HHQNO and piericidin A [13]. Replacing a methyl group of 2methyl-BQ and 2,6-dimethyl-BQ by an ethyl group causes a marked decrease in the inhibitory activity.

Similarly, the counterpart of cytochrome bo seems to catalyze the oxidation of quinols [8], lipid-soluble two-electron, two-proton redox components (Fig. 1), although it lacks CUA [1-4,7]. Subsequently, it transfers electrons to the heme o-CuB center through heme b. Cytochrome bo is closely related to bacterial cytochrome e oxidases [9]; however, the location and structural features of the substrate oxidation site remain obscure. In this chapter, we discuss the structural features of a low-affinity quinol oxidation site (QL) of cytochrome bo and the functional role of a high-affinity quinone binding site (QH) that connects electron flow from the two-electron redox component (quinols) to a one-electron transfer system (heme irons).

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