dc.contributor.author | Pierce, Elizabeth | |
dc.contributor.author | Can, Mehmet | |
dc.contributor.author | Ragsdale, Stephen W. | |
dc.contributor.author | Gibson, Marcus Ian | |
dc.contributor.author | Brignole, Edward J. | |
dc.contributor.author | Drennan, Catherine L. | |
dc.date.accessioned | 2016-10-26T19:22:50Z | |
dc.date.available | 2016-10-26T19:22:50Z | |
dc.date.issued | 2015-06 | |
dc.date.submitted | 2015-06 | |
dc.identifier.issn | 0006-2960 | |
dc.identifier.issn | 1520-4995 | |
dc.identifier.uri | http://hdl.handle.net/1721.1/105101 | |
dc.description.abstract | Thiamine pyrophosphate (TPP), a derivative of vitamin B[subfield 1], is a versatile and ubiquitous cofactor. When coupled with [4Fe-4S] clusters in microbial 2-oxoacid:ferredoxin oxidoreductases (OFORs), TPP is involved in catalyzing low-potential redox reactions that are important for the synthesis of key metabolites and the reduction of N[subfield 2], H[superscript +], and CO[subfield 2]. We have determined the high-resolution (2.27 Å) crystal structure of the TPP-dependent oxalate oxidoreductase (OOR), an enzyme that allows microbes to grow on oxalate, a widely occurring dicarboxylic acid that is found in soil and freshwater and is responsible for kidney stone disease in humans. OOR catalyzes the anaerobic oxidation of oxalate, harvesting the low-potential electrons for use in anaerobic reduction and fixation of CO[subfield 2]. We compare the OOR structure to that of the only other structurally characterized OFOR family member, pyruvate:ferredoxin oxidoreductase. This side-by-side structural analysis highlights the key similarities and differences that are relevant for the chemistry of this entire class of TPP-utilizing enzymes. | en_US |
dc.description.sponsorship | National Institutes of Health (U.S.) (grant NIH GM069857) | en_US |
dc.description.sponsorship | National Science Foundation (U.S.) (Graduate Research Fellowship, Grant 1122374) | en_US |
dc.description.sponsorship | Martin Family Society of Fellows for Sustainability | en_US |
dc.description.sponsorship | Howard Hughes Medical Institute (Investigator) | en_US |
dc.language.iso | en_US | |
dc.publisher | American Chemical Society (ACS) | en_US |
dc.relation.isversionof | http://dx.doi.org/10.1021/acs.biochem.5b00521 | en_US |
dc.rights | Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use. | en_US |
dc.source | ACS | en_US |
dc.title | The Structure of an Oxalate Oxidoreductase Provides Insight into Microbial 2-Oxoacid Metabolism | en_US |
dc.type | Article | en_US |
dc.identifier.citation | Gibson, Marcus I., Edward J. Brignole, Elizabeth Pierce, Mehmet Can, Stephen W. Ragsdale, and Catherine L. Drennan. "The Structure of an Oxalate Oxidoreductase Provides Insight into Microbial 2-Oxoacid Metabolism." Biochemistry 54:26 (2015), pp. 4112-4120. © 2015 American Chemical Society. | en_US |
dc.contributor.department | Massachusetts Institute of Technology. Department of Biology | en_US |
dc.contributor.department | Massachusetts Institute of Technology. Department of Chemistry | en_US |
dc.contributor.mitauthor | Gibson, Marcus Ian | |
dc.contributor.mitauthor | Brignole, Edward J. | |
dc.contributor.mitauthor | Drennan, Catherine L. | |
dc.relation.journal | Biochemistry | en_US |
dc.eprint.version | Final published version | en_US |
dc.type.uri | http://purl.org/eprint/type/JournalArticle | en_US |
eprint.status | http://purl.org/eprint/status/PeerReviewed | en_US |
dspace.orderedauthors | Gibson, Marcus I.; Brignole, Edward J.; Pierce, Elizabeth; Can, Mehmet; Ragsdale, Stephen W.; Drennan, Catherine L. | en_US |
dspace.embargo.terms | N | en_US |
dc.identifier.orcid | https://orcid.org/0000-0001-5486-2755 | |
dspace.mitauthor.error | true | |
mit.license | PUBLISHER_POLICY | en_US |
mit.metadata.status | Complete | |