Metalloproteins containing cytochrome, iron-sulfur, or copper redox centers.
Metalloproteins containing cytochrome, iron-sulfur, or copper redox centers.
复制标题
DOI：
10.1021/cr400479b
复制
发表时间：
2014-04-23
期刊：
影响因子：
62.1
通讯作者：
Lu, Yi
中科院分区：
文献类型：
--
作者：
Liu, Jing;Chakraborty, Saumen;Hosseinzadeh, Parisa;Yu, Yang;Tian, Shiliang;Petrik, Igor;Bhagi, Ambika;Lu, Yi
氧化还原反应在几乎所有的生物过程中都起着重要的作用，包括光合作用和呼吸作用，这两个过程是维持地球上所有生命的基本能量过程。因此，生物学在这些过程中使用氧化还原活性金属离子也就不足为奇了。很大程度上是氧化还原活性使金属离子具有独特的生物辅助因子资格，并使生物无机酶学既有趣又具有挑战性。尽管大多数金属离子具有氧化还原活性，但生物学中用于电子转移（ET）过程的金属离子数量却非常有限。参与ET过程的氧化还原中心的主要成员包括细胞色素、铁硫簇和铜还毒素。这些中心共同覆盖了生物学中还原电位的整个范围（图1）。由于它们的重要性，关于氧化还原中心（1-77）和细胞色素（8,24,78 -90）铁硫蛋白（91-93）和铜氧还毒素（94-104）的一般性综述已经出现在文献中。在这篇综述中，我们提供了上述氧化还原中心的每个成员的分类和描述，包括天然和设计的蛋白质，以及那些含有这些氧化还原中心组合的蛋白质。通过这篇综述，我们研究了它们氧化还原特性的结构特征，包括从最近的氧化还原中心微调中获得的知识。DFT计算等计算研究在理解结构-功能关系和促进蛋白质中金属辅助因子的ET性质和还原电位的微调方面变得越来越重要。由于这方面在以前（105-110）和本专题问题的其他评论（111,112,113）中已作了广泛的审查，因此这里不再讨论。
Redox reactions play important roles in almost all biological processes, including photosynthesis and respiration, which are two essential energy processes that sustain all life on earth. It is thus not surprising that biology employs redox-active metal ions in these processes. It is largely the redox activity that makes metal ions uniquely qualified as biological cofactors and makes bioinorganic enzymology both fun to explore and challenging to study.Even though most metal ions are redox active, biology employs a surprisingly limited number of them for electron transfer (ET) processes. Prominent members of redox centers involved in ET processes include cytochromes, iron–sulfur clusters, and cupredoxins. Together these centers cover the whole range of reduction potentials in biology (Figure 1). Because of their importance, general reviews about redox centers (1-77) and specific reviews about cytochromes,(8, 24, 78-90) iron–sulfur proteins,(91-93) and cupredoxins (94-104) have appeared in the literature. In this review, we provide both classification and description of each member of the above redox centers, including both native and designed proteins, as well as those proteins that contain a combination of these redox centers. Through this review, we examine structural features responsible for their redox properties, including knowledge gained from recent progress in fine-tuning the redox centers. Computational studies such as DFT calculations become more and more important in understanding the structure–function relationship and facilitating the fine-tuning of the ET properties and reduction potentials of metallocofactors in proteins. Since this aspect has been reviewed extensively before,(105-110) and by other reviews in this thematic issue,(111, 112, 113) it will not be covered here.
登录
查看更多内容
影响因子：
4.3
作者：
Albers, Antonia;Bayer, Thomas;Meyer, Franc
通讯作者：
Meyer, Franc
DOI：
10.1073/pnas.72.12.4854
发表时间：
1975-01-01
影响因子：
11.1
作者：
ADMAN, E;WATENPAUGH, KD;JENSEN, LH
通讯作者：
JENSEN, LH
影响因子：
3.6
作者：
Abreu, IA;Saraiva, LM;Teixeira, M
通讯作者：
Teixeira, M
DOI：
10.1016/0005-2728(84)90247-0
发表时间：
1984-01-01
期刊：
BIOCHIMICA ET BIOPHYSICA ACTA
影响因子：
--
作者：
ALAM, J;SPRINKLE, J;KROGMANN, DW
通讯作者：
KROGMANN, DW
影响因子：
3.9
作者：
Ambler, RP;Meyer, TE;Cusanovich, MA
通讯作者：
Cusanovich, MA