Type‐II NADH:quinone oxidoreductase from Staphylococcus aureus has two distinct binding sites and is rate limited by quinone reduction

Publisher： John Wiley & Sons Inc

E-ISSN： 1365-2958|98|2|272-288

ISSN： 0950-382x

Source： MOLECULAR MICROBIOLOGY, Vol.98, Iss.2, 2015-10, pp. : 272-288

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Abstract

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The type‐II NADH:quinone oxidoreductase (NDH‐2) from Staphylococcus aureus has been recognized as a potential target for antimicrobial therapy. Structural and biochemical studies reveal that NDH‐2 is a dimeric protein with distinct binding sites for the two substrates (NADH and quinones). Kinetic studies identify quinone reduction as the rate limiting step. For details, see the article by Sena et al. on pp. 272–288 of this issue.

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MOLECULAR MICROBIOLOGY, Vol. 950-382X, Iss. 2, 2015-10 ,pp. : i-i

John Wiley & Sons Inc

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The type‐II NADH:quinone oxidoreductase (NDH‐2) from Staphylococcus aureus has been recognized as a potential target for antimicrobial therapy. Structural and biochemical studies reveal that NDH‐2 is a dimeric protein with distinct binding sites for the two substrates (NADH and quinones). Kinetic studies identify quinone reduction as the rate limiting step. For details, see the article by Sena et al. on pp. 272–288 of this issue.

By  

MOLECULAR MICROBIOLOGY, Vol. 98, Iss. 2, 2015-10 ,pp. : i-i

John Wiley & Sons Inc

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