期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 116, 期 28, 页码 13964-13969出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1901471116
关键词
carboxylases; enzyme mechanisms; carbon dioxide; CO2 fixation; RuBisCO
资金
- European Research Council [637675]
- Max-Planck-Society Partnergroup Program
- SYNMIKRO fellowship
- NSF Science and Technology Centers Grant [NSF-1231306]
- U.S. Department of Energy (DOE) Office of Science, Biological and Environmental Research
- Stanford Precourt Institute
- SLAC Laboratory Directed Research and Development
- DOE Office of Science User Facility [DE-AC02-05CH11231]
- European Research Council (ERC) [637675] Funding Source: European Research Council (ERC)
Carboxylases are biocatalysts that capture and convert carbon dioxide (CO2) under mild conditions and atmospheric concentrations at a scale of more than 400 Gt annually. However, how these enzymes bind and control the gaseous CO2 molecule during catalysis is only poorly understood. One of the most efficient classes of carboxylating enzymes are enoyl-CoA carboxylases/reductases (Ecrs), which outcompete the plant enzyme RuBisCO in catalytic efficiency and fidelity by more than an order of magnitude. Here we investigated the interactions of CO2 within the active site of Ecr from Kitasatospora setae. Combining experimental biochemistry, protein crystallography, and advanced computer simulations we show that 4 amino acids, N81, F170, E171, and H365, are required to create a highly efficient CO2 -fixing enzyme. Together, these 4 residues anchor and position the CO2 molecule for the attack by a reactive enolate created during the catalytic cycle. Notably, a highly ordered water molecule plays an important role in an active site that is otherwise carefully shielded from water, which is detrimental to CO2 fixation. Altogether, our study reveals unprecedented molecular details of selective CO2 binding and C-C-bond formation during the catalytic cycle of nature's most efficient CO2 -fixing enzyme. This knowledge provides the basis for the future development of catalytic frameworks for the capture and conversion of CO2 in biology and chemistry.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据