与一氧化氮合酶的血红素结合氧分子的底物特异性相互作用。
Substrate-specific interactions with the heme-bound oxygen molecule of nitric-oxide synthase.
作者信息
Chartier François J M, Couture Manon
机构信息
Département de Biochimie et de Microbiologie and the Centre de Recherche sur la Fonction, la Structure, et l'Ingénierie des Protéines, Université Laval, Quebec City, Quebec G1K 7P4, Canada.
出版信息
J Biol Chem. 2007 Jul 20;282(29):20877-86. doi: 10.1074/jbc.M701800200. Epub 2007 May 30.
We report the characterization by resonance Raman spectroscopy of the oxygenated complex (Fe(II)O(2)) of nitric-oxide synthases of Staphylococcus aureus (saNOS) and Bacillus subtilis (bsNOS) saturated with N(omega)-hydroxy-l-arginine. The frequencies of the nu(Fe-O) and nu(O-O) modes were 530 and 1135 cm(-), respectively, in both the presence and absence of tetrahydrobiopterin. On the basis of a comparison of these frequencies with those of saNOS and bsNOS saturated with l-arginine (nu(Fe-O) at 517 cm(-1) and nu(O-O) at 1123 cm(-1)) and those of substrate-free saNOS (nu(Fe-O) at 517 and nu(O-O) at 1135 cm(-1)) (Chartier, F. J. M., Blais, S. P., and Couture, M. (2006) J. Biol. Chem. 281, 9953-9962), we propose two models that account for the frequency shift of nu(Fe-O) (but not nu(O-O)) upon N(omega)-hydroxy-l-arginine binding as well as the frequency shift of nu(O-O) (but not nu(Fe-O)) upon l-arginine binding. The implications of these substrate-specific interactions with respect to catalysis by NOSs are discussed.
我们报道了通过共振拉曼光谱对金黄色葡萄球菌（saNOS）和枯草芽孢杆菌（bsNOS）一氧化氮合酶的含氧复合物（Fe(II)O₂）进行的表征，该复合物用N(ω)-羟基-L-精氨酸饱和。无论是否存在四氢生物蝶呤，ν(Fe-O)和ν(O-O)模式的频率分别为530和1135 cm⁻¹。基于将这些频率与用L-精氨酸饱和的saNOS和bsNOS的频率（ν(Fe-O)为517 cm⁻¹，ν(O-O)为1123 cm⁻¹）以及无底物的saNOS的频率（ν(Fe-O)为517，ν(O-O)为1135 cm⁻¹）进行比较（沙蒂埃，F. J. M.，布莱斯，S. P.，和库蒂尔，M.（2006年）《生物化学杂志》281，9953 - 9962），我们提出了两个模型，这两个模型解释了N(ω)-羟基-L-精氨酸结合时ν(Fe-O)（而非ν(O-O)）的频率变化以及L-精氨酸结合时ν(O-O)（而非ν(Fe-O)）的频率变化。讨论了这些底物特异性相互作用对一氧化氮合酶催化作用的影响。
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