Crystallographic Characterization of the Carbonylated A-Cluster in Carbon Monoxide Dehydrogenase/Acetyl-CoA Synthase

被引：33

作者：

Cohen, Steven E. ^{[1
]}

Can, Mehmet ^{[2
]}

Wittenborn, Elizabeth C. ^{[1
]}

Hendrickson, Rachel A. ^{[3
]}

Ragsdale, Stephen W. ^{[2
]}

Drennan, Catherine L. ^{[1
,3
,4
,5
]}

机构：

[1] MIT, Dept Chem, Cambridge, MA 02139 USA

[2] Univ Michigan, Sch Med, Dept Biol Chem, Ann Arbor, MI 04109 USA

[3] MIT, Dept Biol, 77 Massachusetts Ave, Cambridge, MA 02139 USA

[4] Howard Hughes Med Inst, Cambridge, MA 02139 USA

[5] Canadian Inst Adv Res, Bioinspired Solar Energy Program, Toronto, ON M5G 1M1, Canada

来源：

ACS CATALYSIS | 2020年 / 10卷 / 17期

关键词：

CODH; ACS; Wood-Ljungdahl; acetogenesis; metalloenzymes; carbon monoxide; acetyl coenzyme A; X-ray crystallography; ACETYL-COENZYME-A; CLOSTRIDIUM-THERMOACETICUM; MULTIENZYME COMPLEX; C-BOND; NICKEL; MECHANISM; TUNNEL; MODEL; END;

D O I：

10.1021/acscatal.0c03033

中图分类号：

O64 [物理化学（理论化学）、化学物理学];

学科分类号：

070304 ; 081704 ;

摘要：

The Wood-Ljungdahl pathway allows for autotrophic bacterial growth on carbon dioxide, with the last step in acetyl-CoA synthesis catalyzed by the bifunctional enzyme carbon monoxide dehydrogenase/acetyl-CoA synthase (CODH/ACS). ACS uses a complex Ni-Fe-S metallocluster termed the A-cluster to assemble acetyl-CoA from carbon monoxide, a methyl moiety and coenzyme A. Here, we report the crystal structure of CODH/ACS from Moorella thermoacetica with substrate carbon monoxide bound at the A-cluster, a state previously uncharacterized by crystallography. Direct structural characterization of this state highlights the role of second sphere residues and conformational dynamics in acetyl-CoA assembly, the biological equivalent of the Monsanto process.

引用

页码：9741 / 9746

页数：6

共 35 条

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