氧气激活和减轻呼吸:还原活性铁素244的参与
D A Proshlyakov1, M A Pressler, C DeMaso
1Department of Chemistry and Department of Biochemistry, Michigan State University, East Lansing, MI 48824, USA.
概括
研究人员研究了细胞染色体氧化酶的一个关键中间体,揭示了它的结构和氧化还原活性. 这一发现澄清了呼吸过程中能量如何转移,以防止有毒副产品和控制质子送.
科学领域:
- 生物化学 生物化学
- 分子生物学分子生物学
- 生物能源学 生物能源学
背景情况:
- 细胞染色体氧化酶对于细胞呼吸至关重要,催化氧气减少到水中.
- 它将这种反应与氨酸5'-三酸盐 (ATP) 合成的质子转位结合起来.
- 一个中心的中间体,P,连接了氧气的减少和质子.
研究的目的:
- 为了阐明细胞染色体氧化酶中中间P的结构.
- 要了解中间P的氧化还原活性.
- 为了澄清氧降解过程中能量转移的机制.
主要方法:
- 细胞氧化酶的放射性化物标记.
- 片映射用于分析蛋白质结构.
- 谱分析以确定中间P的氧化还原状态.
主要成果:
- 交叉链接的histidine 240-tyrosine 244 (His240-Tyr244) 物种被确定为具有氧化还原活性.
- 中间P的结构被确定为Fe(IV) =O/Cu(B) 2+-H240-Y244.
- 从O2转移到蛋白质部分的能量被证实是关键的监管步骤.
结论:
- 介质P的确定的结构对于其在细胞染色体氧化酶中的功能至关重要.
- His240-Tyr244的氧化还原活性对于P的形成和能量转移至关重要.
- 这种机制可以防止有毒的中间体,并优化ATP合成中的能量利用.
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