Show simple item record

dc.contributor.authorMus, Florence
dc.contributor.authorEilers, Brian J.
dc.contributor.authorAlleman, Alexander B.
dc.contributor.authorKabasakal, Burak V.
dc.contributor.authorWells, Jennifer N.
dc.contributor.authorMurray, James W.
dc.contributor.authorNocek, Boguslaw P.
dc.contributor.authorDuBois, Jennifer L.
dc.contributor.authorPeters, John W.
dc.date.accessioned2018-04-26T16:55:43Z
dc.date.available2018-04-26T16:55:43Z
dc.date.issued2017-08
dc.identifier.citationMus, Florence, Brian J. Eilers, Alexander B. Alleman, Burak V. Kabasakal, Jennifer N. Wells, James W. Murray, Boguslaw P. Nocek, Jennifer L. DuBois, and John W. Peters. "Structural Basis for the Mechanism of ATP-Dependent Acetone Carboxylation." Scientific Reports 7 (August 2017): 1-10. DOI: 10.1038/s41598-017-06973-8.en_US
dc.identifier.issn2045-2322
dc.identifier.urihttps://scholarworks.montana.edu/xmlui/handle/1/14521
dc.description.abstractMicroorganisms use carboxylase enzymes to form new carbon-carbon bonds by introducing carbon dioxide gas (CO2) or its hydrated form, bicarbonate (HCO3 −), into target molecules. Acetone carboxylases (ACs) catalyze the conversion of substrates acetone and HCO3 − to form the product acetoacetate. Many bicarbonate-incorporating carboxylases rely on the organic cofactor biotin for the activation of bicarbonate. ACs contain metal ions but not organic cofactors, and use ATP to activate substrates through phosphorylation. How the enzyme coordinates these phosphorylation events and new C-C bond formation in the absence of biotin has remained a mystery since these enzymes were discovered. The first structural rationale for acetone carboxylation is presented here, focusing on the 360 kDa (αβγ)2 heterohexameric AC from Xanthobacter autotrophicus in the ligand-free, AMP-bound, and acetate coordinated states. These structures suggest successive steps in a catalytic cycle revealing that AC undergoes large conformational changes coupled to substrate activation by ATP to perform C-C bond ligation at a distant Mn center. These results illustrate a new chemical strategy for the conversion of CO2 into biomass, a process of great significance to the global carbon cycle.en_US
dc.description.sponsorshipUS Department of Energy (DE-FG02-04ER15563)en_US
dc.rightsCC BY 4.0en_US
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/legalcodeen_US
dc.titleStructural Basis for the Mechanism of ATP-Dependent Acetone Carboxylationen_US
dc.typeArticleen_US
mus.citation.journaltitleScientific Reportsen_US
mus.citation.volume7en_US
mus.identifier.categoryLife Sciences & Earth Sciencesen_US
mus.identifier.doi10.1038/s41598-017-06973-8en_US
mus.relation.collegeCollege of Letters & Scienceen_US
mus.relation.departmentChemistry & Biochemistry.en_US
mus.relation.universityMontana State University - Bozemanen_US
mus.data.thumbpage3en_US
mus.contributor.orcidPeters, John W.|0000-0001-9117-9568en_US
mus.contributor.orcidMus, Florence|0000-0002-1655-1267en_US


Files in this item

Thumbnail

This item appears in the following Collection(s)

Show simple item record

CC BY 4.0
Except where otherwise noted, this item's license is described as CC BY 4.0