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您的检索式：作者名="Stephen G.Bell"
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| 1 | Chain length-dependent cooperativity in fatty acid binding and oxidation by cytochrome P450_(BM3)(CYP102A1)显示文摘Fatty acid binding and oxidation kinetics for wild type P450_(BM3)(CYP102A1)from Bacillus megaterium have been found to display chain length-dependent homotropic behavior.Laurate and 13-methyl-myristate display Michaelis-Menten behavior while there are slight deviations with myristate at low ionic strengths.Palmitate shows Michaelis-Menten kinetics and hyperbolic binding behavior in 100 mmol/L phosphate,pH 7.4,but sigmoidal kinetics(with an apparent intercept)in low ionic strength buffers and at physiological phosphate concentrations.In low ionic strength buffers both the heme domain and the full-length enzyme show complex palmitate binding behavior that indicates a minimum of four fatty acid binding sites,with high cooperativity for the binding of the fourth palmitate molecule,and the full-length enzyme showing tighter palmitate binding than the heme domain.The first flavin-to-heme electron transfer is faster for laurate,myristate and palmitate in 100 mmol/L phosphate than in 50mmol/L Tris(pH 7.4),yet each substrate induces similar high-spin heme content.For palmitate in low phosphate buffer concentrations,the rate constant of the first electron transfer is much larger than kcat.The results suggest that phosphate has a specific effect in promoting the first electron transfer step,and that P450_(BM3) could modulate Bacillus membrane morphology and fluidity via palmitate oxidation in response to the external phosphate concentration. | Benjamin Rowlatt Jake A.Yorke Anthony J.Strong Christopher J.C.Whitehouse Stephen G.Bell Luet-Lok Wong | 2011 | Protein & Cell2011，2，8： | 0 |
| 2 | 细胞色素P450 153C1蛋白的表达、纯化及初步晶体学研究显示文摘细胞色素P450,又称CYP,是最大的酶类超家族之一,属于血红素蛋白的一个大家族[1]。它们在生物界分布极其广泛,从细菌到高等的动植物中都有分布。 | 周卫红 杨文 Stephen G.Bell Mark Bartlam Luet-Lok Wong 饶子和 | 2009 | 生物物理学报2009，0，S1： | 0 |
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