Physiological relevance, localization and substrate specificity of the alternative (type II) mitochondrial NADH dehydrogenases of Ogataea parapolymorpha
Mitochondria from Ogataea parapolymorpha harbor a branched electron-transport chain containing a proton-pumping Complex I NADH dehydrogenase and three Type II NADH dehydrogenases (NDH-2). To investigate the physiological role, localization and substrate specificity of these enzymes, the growth of va...
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Frontiers Media S.A.
2024-12-01
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| Online Access: | https://www.frontiersin.org/articles/10.3389/fmicb.2024.1473869/full |
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| author | Hannes Juergens Álvaro Mielgo-Gómez Albert Godoy-Hernández Jolanda ter Horst Janine M. Nijenhuis Duncan G. G. McMillan Duncan G. G. McMillan Robert Mans |
| author_facet | Hannes Juergens Álvaro Mielgo-Gómez Albert Godoy-Hernández Jolanda ter Horst Janine M. Nijenhuis Duncan G. G. McMillan Duncan G. G. McMillan Robert Mans |
| author_sort | Hannes Juergens |
| collection | DOAJ |
| description | Mitochondria from Ogataea parapolymorpha harbor a branched electron-transport chain containing a proton-pumping Complex I NADH dehydrogenase and three Type II NADH dehydrogenases (NDH-2). To investigate the physiological role, localization and substrate specificity of these enzymes, the growth of various NADH dehydrogenase knockout mutants was quantitatively characterized in shake-flask and chemostat cultures, followed by oxygen-uptake experiments with isolated mitochondria. NAD(P)H:quinone oxidoreduction of the three NDH-2 were individually assessed. Our findings reveal that the O. parapolymorpha respiratory chain contains an internal NADH-accepting NDH-2 (Ndh2-1/OpNdi1), at least one external NAD(P)H-accepting enzyme, and likely additional mechanisms for respiration-linked oxidation of cytosolic NADH. Metabolic regulation appears to prevent competition between OpNdi1 and Complex I for mitochondrial NADH. With the exception of OpNdi1, the respiratory chain of O. parapolymorpha exhibits metabolic redundancy and tolerates deletion of multiple NADH-dehydrogenase genes without compromising fully respiratory metabolism. |
| format | Article |
| id | doaj-art-292e3268ebd84adcb436ccc64ef1d5cd |
| institution | OA Journals |
| issn | 1664-302X |
| language | English |
| publishDate | 2024-12-01 |
| publisher | Frontiers Media S.A. |
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| series | Frontiers in Microbiology |
| spelling | doaj-art-292e3268ebd84adcb436ccc64ef1d5cd2025-08-20T02:34:32ZengFrontiers Media S.A.Frontiers in Microbiology1664-302X2024-12-011510.3389/fmicb.2024.14738691473869Physiological relevance, localization and substrate specificity of the alternative (type II) mitochondrial NADH dehydrogenases of Ogataea parapolymorphaHannes Juergens0Álvaro Mielgo-Gómez1Albert Godoy-Hernández2Jolanda ter Horst3Janine M. Nijenhuis4Duncan G. G. McMillan5Duncan G. G. McMillan6Robert Mans7Department of Biotechnology, Delft University of Technology, Delft, NetherlandsDepartment of Biotechnology, Delft University of Technology, Delft, NetherlandsDepartment of Biotechnology, Delft University of Technology, Delft, NetherlandsDepartment of Biotechnology, Delft University of Technology, Delft, NetherlandsDepartment of Biotechnology, Delft University of Technology, Delft, NetherlandsDepartment of Biotechnology, Delft University of Technology, Delft, NetherlandsSchool of Biological Sciences, University of Reading, Reading, United KingdomDepartment of Biotechnology, Delft University of Technology, Delft, NetherlandsMitochondria from Ogataea parapolymorpha harbor a branched electron-transport chain containing a proton-pumping Complex I NADH dehydrogenase and three Type II NADH dehydrogenases (NDH-2). To investigate the physiological role, localization and substrate specificity of these enzymes, the growth of various NADH dehydrogenase knockout mutants was quantitatively characterized in shake-flask and chemostat cultures, followed by oxygen-uptake experiments with isolated mitochondria. NAD(P)H:quinone oxidoreduction of the three NDH-2 were individually assessed. Our findings reveal that the O. parapolymorpha respiratory chain contains an internal NADH-accepting NDH-2 (Ndh2-1/OpNdi1), at least one external NAD(P)H-accepting enzyme, and likely additional mechanisms for respiration-linked oxidation of cytosolic NADH. Metabolic regulation appears to prevent competition between OpNdi1 and Complex I for mitochondrial NADH. With the exception of OpNdi1, the respiratory chain of O. parapolymorpha exhibits metabolic redundancy and tolerates deletion of multiple NADH-dehydrogenase genes without compromising fully respiratory metabolism.https://www.frontiersin.org/articles/10.3389/fmicb.2024.1473869/fullmitochondriaNADH dehydrogensaseOgataea parapolymorphabioenergeticsyeast engineering |
| spellingShingle | Hannes Juergens Álvaro Mielgo-Gómez Albert Godoy-Hernández Jolanda ter Horst Janine M. Nijenhuis Duncan G. G. McMillan Duncan G. G. McMillan Robert Mans Physiological relevance, localization and substrate specificity of the alternative (type II) mitochondrial NADH dehydrogenases of Ogataea parapolymorpha Frontiers in Microbiology mitochondria NADH dehydrogensase Ogataea parapolymorpha bioenergetics yeast engineering |
| title | Physiological relevance, localization and substrate specificity of the alternative (type II) mitochondrial NADH dehydrogenases of Ogataea parapolymorpha |
| title_full | Physiological relevance, localization and substrate specificity of the alternative (type II) mitochondrial NADH dehydrogenases of Ogataea parapolymorpha |
| title_fullStr | Physiological relevance, localization and substrate specificity of the alternative (type II) mitochondrial NADH dehydrogenases of Ogataea parapolymorpha |
| title_full_unstemmed | Physiological relevance, localization and substrate specificity of the alternative (type II) mitochondrial NADH dehydrogenases of Ogataea parapolymorpha |
| title_short | Physiological relevance, localization and substrate specificity of the alternative (type II) mitochondrial NADH dehydrogenases of Ogataea parapolymorpha |
| title_sort | physiological relevance localization and substrate specificity of the alternative type ii mitochondrial nadh dehydrogenases of ogataea parapolymorpha |
| topic | mitochondria NADH dehydrogensase Ogataea parapolymorpha bioenergetics yeast engineering |
| url | https://www.frontiersin.org/articles/10.3389/fmicb.2024.1473869/full |
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