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dc.contributor.authorMeuser, Jonathan E.
dc.contributor.authorD'Adamo, S.
dc.contributor.authorJinkerson, R. E.
dc.contributor.authorMus, Florence
dc.contributor.authorYang, Wenqiang
dc.contributor.authorGhirardi, ML
dc.contributor.authorSeibert, M.
dc.contributor.authorGrossman, A. R.
dc.contributor.authorPosewitz, Matthew C.
dc.date.accessioned2017-02-02T22:21:35Z
dc.date.available2017-02-02T22:21:35Z
dc.date.issued2012-01
dc.identifier.citationMeuser JE, D’Adamo S, Jinkerson RE, Mus F, Yang W, Ghirardi ML, Seibert M, Grossman AR, Posewitz MC, "Genetic disruption of both Chlamydomonas reinhardtii [FeFe]-hydrogenases: Insight into the role of HYDA2 in H2 production," Biochemical and Biophysical Research Communications, January 2012 417(2):704–709en_US
dc.identifier.issn0006-291X
dc.identifier.urihttps://scholarworks.montana.edu/xmlui/handle/1/12539
dc.description.abstractChlamydomonas reinhardtii (Chlamydomonas throughout) encodes two [FeFe]-hydrogenases, designated HYDA1 and HYDA2. While HYDA1 is considered the dominant hydrogenase, the role of HYDA2 is unclear. To study the individual functions of each hydrogenase and provide a platform for future bioengineering, we isolated the Chlamydomonas hydA1-1, hydA2-1 single mutants and the hydA1-1 hydA2-1 double mutant. A reverse genetic screen was used to identify a mutant with an insertion in HYDA2, followed by mutagenesis of the hydA2-1 strain coupled with a H2 chemosensor phenotypic screen to isolate the hydA1-1 hydA2-1 mutant. Genetic crosses of the hydA1-1 hydA2-1 mutant to wild-type cells allowed us to also isolate the single hydA1-1 mutant. Fermentative, photosynthetic, and in vitro hydrogenase activities were assayed in each of the mutant genotypes. Surprisingly, analyses of the hydA1-1 and hydA2-1 single mutants, as well as the HYDA1 and HYDA2 rescued hydA1-1 hydA2-1 mutant demonstrated that both hydrogenases are able to catalyze H2 production from either fermentative or photosynthetic pathways. The physiology of both mutant and complemented strains indicate that the contribution of HYDA2 to H2 photoproduction is approximately 25% that of HYDA1, which corresponds to similarly low levels of in vitro hydrogenase activity measured in the hydA1-1 mutant. Interestingly, enhanced in vitro and fermentative H2 production activities were observed in the hydA1-1 hydA2-1 strain complemented with HYDA1, while maximal H2-photoproduction rates did not exceed those of wild-type cells.en_US
dc.titleGenetic disruption of both Chlamydomonas reinhardtii [FeFe]-hydrogenases: Insight into the role of HYDA2 in H2 productionen_US
dc.typeArticleen_US
mus.citation.extentfirstpage704en_US
mus.citation.extentlastpage709en_US
mus.citation.issue2en_US
mus.citation.journaltitleBiochemical and Biophysical Research Communicationsen_US
mus.citation.volume417en_US
mus.identifier.categoryChemical & Material Sciencesen_US
mus.identifier.categoryEngineering & Computer Scienceen_US
mus.identifier.categoryLife Sciences & Earth Sciencesen_US
mus.identifier.doi10.1016/j.bbrc.2011.12.002en_US
mus.relation.collegeCollege of Agricultureen_US
mus.relation.collegeCollege of Engineeringen_US
mus.relation.collegeCollege of Letters & Scienceen_US
mus.relation.departmentCenter for Biofilm Engineering.en_US
mus.relation.departmentChemical & Biological Engineering.en_US
mus.relation.departmentChemistry & Biochemistry.en_US
mus.relation.departmentGenetics.en_US
mus.relation.departmentMicrobiology & Immunology.en_US
mus.relation.universityMontana State University - Bozemanen_US
mus.relation.researchgroupCenter for Biofilm Engineering.en_US
mus.data.thumbpage5en_US
mus.contributor.orcidMus, Florence|0000-0002-1655-1267en_US


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