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Review Article

基于高分辨率蛋白质结构的血红素分解酶HO和BVR的反应化学认识的最新进展

卷 27, 期 21, 2020

页: [3499 - 3518] 页: 20

弟呕挨: 10.2174/0929867326666181217142715

open access plus

摘要

在哺乳动物中，血红素族的分解代谢对于生命是必不可少的。血红素首先被血红素加氧酶（HO）裂解为线性四吡咯BiliverdinIXα（BV），然后BIV被Biliverdin Reductase（BVR）转化为胆红素。 HO利用NADPH-细胞色素P450氧化还原酶（CPR）提供的三个氧分子（O2）和七个电子来打开血红素环，BVR通过使用NAD（P）H降低BV。 HOs的结构研究，包括底物结合，反应中间物结合和几种特定抑制剂结合形式，揭示了解释底物与HO结合以及特异HO反应进程潜在机制的细节。低温捕获的结构和时间分辨光谱研究检查了远端配体与血红素铁之间的键的光解，证明了HO反应过程中产生的CO如何从反应部位解离，并伴随HO的相应构象变化。包含HO和CPR的复合物结构提供了电子如何转移到血红素-HO复合物中的详细信息。尽管BVR的三级结构及其与NAD +的复合物已经确定了10多年以上，但BVR的催化残基和反应机理仍然未知。最近的晶体学研究，研究了蓝藻BVR与NADP +和底物BV的复合物，为这些问题提供了一些说明。两个BV分子以堆叠的方式结合到BVR，一个BV可以协助另一个BV的还原催化。在这篇综述中，通过生化，光谱学和晶体学研究说明了最近的进展，这些进展详细说明了HO和BVR反应的分子机理的化学基础。

关键词: X射线晶体学，蛋白质结构，氧化还原络合物，血红素代谢，酶促反应，配体识别，堆积的底物结合模式。

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