The structure-based reaction mechanism of urease, a nickel dependent enzyme: tale of a long debate

被引:110
|
作者
Mazzei, Luca [1 ]
Musiani, Francesco [1 ]
Ciurli, Stefano [1 ]
机构
[1] Univ Bologna, Dept Pharm & Biotechnol, Lab Bioinorgan Chem, Viale G Fanin 40, I-40127 Bologna, Italy
来源
关键词
Nickel; Urease; Catalytic mechanism; Crystal structure; Sporosarcina pasteurii; Klebsiella aerogenes; Helicobacter pylori; JACK-BEAN UREASE; KLEBSIELLA-AEROGENES UREASE; BACILLUS-PASTEURII UREASE; SITE-DIRECTED MUTAGENESIS; X-RAY DATA; ACTIVE-SITE; HELICOBACTER-PYLORI; BETA-MERCAPTOETHANOL; EC; 3.5.1.5; FLUORIDE INHIBITION;
D O I
10.1007/s00775-020-01808-w
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
This review is an attempt to retrace the chronicle that starts from the discovery of the role of nickel as the essential metal ion in urease for the enzymatic catalysis of urea, a key step in the biogeochemical cycle of nitrogen on Earth, to the most recent progress in understanding the chemistry of this historical enzyme. Data and facts are presented through the magnifying lenses of the authors, using their best judgment to filter and elaborate on the many facets of the research carried out on this metalloenzyme over the years. The tale is divided in chapters that discuss and describe the results obtained in the subsequent leaps in the knowledge that led from the discovery of a biological role for Ni to the most recent advancements in the comprehension of the relationship between the structure and function of urease. This review is intended not only to focus on the bioinorganic chemistry of this beautiful metal-based catalysis, but also, and maybe primarily, to evoke inspiration and motivation to further explore the realm of bio-based coordination chemistry.
引用
收藏
页码:829 / 845
页数:17
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