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dc.contributor.authorNguyen, Diep M. N.
dc.contributor.authorSchut, Gerrit J.
dc.contributor.authorZadvornyy, Oleg A.
dc.contributor.authorTokmina-Lukaszewska, Monika
dc.contributor.authorPoudel, Saroj
dc.contributor.authorLipscomb, Gina L.
dc.contributor.authorAdams, Leslie A.
dc.contributor.authorDinsmore, Jessica T.
dc.contributor.authorNixon, William J.
dc.contributor.authorBoyd, Eric S.
dc.contributor.authorBothner, Brian
dc.contributor.authorPeters, John W.
dc.contributor.authorAdams, Michael W. W.
dc.date.accessioned2017-09-20T15:45:12Z
dc.date.available2017-09-20T15:45:12Z
dc.date.issued2017-07
dc.identifier.citationNguyen, Diep M. N. , Gerrit J. Schut, Oleg A. Zadvornyy, Monika Tokmina-Lukaszewska, Saroj Poudel, Gina L. Lipscomb, Leslie A. Adams, Jessica T. Dinsmore, William J. Nixon, Eric S. Boyd, Brian Bothner, John W. Peters, and Michael W. W. Adams. "Two functionally distinct NADP(+)-dependent ferredoxin oxidoreductases maintain the primary redox balance of Pyrococcus furiosus." Journal of Biological Chemistry 292, no. 35 (July 2017): 14603-14616. DOI: 10.1074/jbc.M117.794172.en_US
dc.identifier.issn0021-9258
dc.identifier.urihttps://scholarworks.montana.edu/xmlui/handle/1/13717
dc.description.abstractElectron bifurcation has recently gained acceptance as the third mechanism of energy conservation in which energy is conserved through the coupling of exergonic and endergonic reactions. A structure-based mechanism of bifurcation has been elucidated recently for the flavin-based enzyme NADH-dependent ferredoxin NADP+ oxidoreductase I (NfnI) from the hyperthermophillic archaeon Pyrococcus furiosus. NfnI is thought to be involved in maintaining the cellular redox balance, producing NADPH for biosynthesis by recycling the two other primary redox carriers, NADH and ferredoxin. The P. furiosus genome encodes an NfnI paralog termed NfnII, and the two are differentially expressed depending on the growth conditions. In this study, we show that deletion of the genes encoding either NfnI or NfnII affects the cellular concentrations of NAD(P)H and particularly NADPH. This results in a moderate to severe growth phenotype in deletion mutants, demonstrating a key role for each enzyme in maintaining redox homeostasis. Despite their similarity in primary sequence and cofactor content, crystallographic, kinetic, and mass spectrometry analyses reveal that there are fundamental structural differences between the two enzymes and NfnII does not catalyze the NfnI bifurcating reaction. Instead it exhibits non-bifurcating ferredoxin NADP oxidoreductase-type activity. NfnII is therefore proposed to be a bifunctional enzyme and to also catalyze a bifurcating reaction, although its third substrate, in addition to ferredoxin and NADP(H), is as yet unknown.en_US
dc.description.sponsorshipBiological Electron Transfer and Catalysis Energy Frontier Research Center (DE-SC0012518)en_US
dc.titleTwo functionally distinct NADP(+)-dependent ferredoxin oxidoreductases maintain the primary redox balance of Pyrococcus furiosusen_US
mus.citation.extentfirstpage14603en_US
mus.citation.extentlastpage14616en_US
mus.citation.issue35en_US
mus.citation.journaltitleJournal of Biological Chemistryen_US
mus.citation.volume292en_US
mus.identifier.categoryChemical & Material Sciencesen_US
mus.identifier.categoryLife Sciences & Earth Sciencesen_US
mus.identifier.doi10.1074/jbc.M117.794172en_US
mus.relation.collegeCollege of Letters & Scienceen_US
mus.relation.departmentChemistry & Biochemistry.en_US
mus.relation.departmentMicrobiology & Immunology.en_US
mus.relation.universityMontana State University - Bozemanen_US
mus.data.thumbpage7en_US
mus.contributor.orcidBothner, Brian|0000-0003-1295-9609en_US
mus.contributor.orcidPeters, John W.|0000-0001-9117-9568en_US
mus.contributor.orcidZadvornyy, Oleg A.|0000-0002-5374-6856en_US
mus.contributor.orcidTokmina-Lukaszewska, Monika|0000-0003-3298-8298en_US


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