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Effect of the Side Chain Structure of Coenzyme Q on the Steady State Kinetics of Bovine Heart NADH: Coenzyme Q Oxidoreductase

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Abstract

Steady state kinetics of bovine heart NADH: coenzyme Q oxidoreductase using coenzyme Q with two isoprenoid unit (Q2) or with a decyl group (DQ) show an ordered sequential mechanism in which the order of substrate binding and product release is NADH-Q2 (DQ) -Q2H2 (DQH2)-NAD+ in contrast to the order determined using Q1 (Q1-NADH-NAD+-Q1H2) (Nakashima et al., J. Bioenerg. Biomembr. 34, 11–19, 2002). The effect of the side chain structure of coenzyme Q suggests that NADH binding to the enzyme results in a conformational change, in the coenzyme Q binding site, which enables the site to accept coenzyme Q with a side chain significantly larger than one isoprenoid unit. The side chains of Q2 and DQ bound to the enzyme induce a conformational change in the binding site to stabilize the substrate binding, while the side chain of Q1 (one isoprenoid unit) is too short to induce the conformational change.

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Authors and Affiliations

  1. Department of Life Science, Himeji Institute of Technology, Kamigohri, Akoh Hyogo, 678-1297, Japan

    Nobuko Hano, Yumiko Nakashima, Kyoko Shinzawa-Itoh & Shinya Yoshikawa

Authors
  1. Nobuko Hano
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  2. Yumiko Nakashima
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  3. Kyoko Shinzawa-Itoh
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  4. Shinya Yoshikawa
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Correspondence to Shinya Yoshikawa.

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Hano, N., Nakashima, Y., Shinzawa-Itoh, K. et al. Effect of the Side Chain Structure of Coenzyme Q on the Steady State Kinetics of Bovine Heart NADH: Coenzyme Q Oxidoreductase. J Bioenerg Biomembr 35, 257–265 (2003). https://doi.org/10.1023/A:1024663715931

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  • DOI: https://doi.org/10.1023/A:1024663715931

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