The enigmatic reaction of flavins with oxygen

被引：200

作者：

Chaiyen, Pimchai ^{[2
,3
]}

Fraaije, Marco W. ^{[4
]}

Mattevi, Andrea ^{[1
]}

机构：

[1] Univ Pavia, Dept Biol & Biotechnol, I-27100 Pavia, Italy

[2] Mahidol Univ, Fac Sci, Dept Biochem, Bangkok 10400, Thailand

[3] Mahidol Univ, Fac Sci, Ctr Excellence Prot Struct & Funct, Bangkok 10400, Thailand

[4] Univ Groningen, Groningen Biomol Sci & Biotechnol Inst, Biochem Lab, NL-9747 AG Groningen, Netherlands

来源：

TRENDS IN BIOCHEMICAL SCIENCES | 2012年 / 37卷 / 09期

关键词：

reactive oxygen species; biocatalysis; oxidase; monooxygenase; oxidative damage; flavin; mechanism; PYRANOSE; 2-OXIDASE; ACTIVE-SITE; MYCOBACTERIUM-TUBERCULOSIS; DEPENDENT MONOOXYGENASE; FLAVOPROTEIN OXIDASES; ACTIVATION SITE; O-2; REACTIVITY; MECHANISM; C4A-HYDROPEROXYFLAVIN; IDENTIFICATION;

D O I：

10.1016/j.tibs.2012.06.005

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

070307 [化学生物学]; 071010 [生物化学与分子生物学];

摘要：

The reaction of flavoenzymes with oxygen remains a fascinating area of research because of its relevance for reactive oxygen species (ROS) generation. Several exciting recent studies provide consistent mechanistic clues about the specific functional and structural properties of the oxidase and monooxygenase flavoenzymatic systems. Specifically, the spatial arrangement of the reacting oxygen that is in direct contact with the flavin group is emerging as a crucial factor that differentiates between oxidase and monooxygenase enzymes. A challenge for the future will be to use these emerging concepts to rationally engineer flavoenzymes, paving the way to new research avenues with far-reaching implications for oxidative biocatalysis and metabolic engineering.

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收藏

页码：373 / 380

页数：8

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