NADH dehydrogenases: from basic science to biomedicine
Abstract
This review article is concerned with two on-going research projects in our laboratory, both of which are related to the study of the NADH dehydrogenase enzyme complexes in the respiratory chain. The goal of the first project is to decipher the structure and mechanism of action of the proton-translocating NADH-quinone oxidoreductase (NDH-1) from two bacteria, Paracoccus denitrificans and Thermus thermophilus HB-8. These microorganisms are of particular interest because of the close resemblance of the former (P. denitrificans) to a mammalian mitochondria, and because of the thermostability of the enzymes of the latter (T. thermophilus). The NDH-1 enzyme complex of these and other bacteria is composed of 13 to 14 unlike subunits and has a relatively simple structure relative to the mitochondrial proton-translocating NADH-quinone oxidoreductase (complex I), which is composed of at least 42 different subunits. Therefore, the bacterial NDH-I is believed to be a useful model for studying the mitochondrial complex I, which is understood to have the most intricate structure of all the membrane-associated enzyme complexes. Recently, the study of the NADH dehydrogenase complex has taken on new urgency as a result of reports that complex I defects are involved in many human mitochondrial diseases. Thus the goal of the second project is to develop possible gene therapies for mitochondrial diseases caused by complex I defects. This project involves attempting to repair complex I defects in the mammalian system using Saccharomyces cerevisiae NDI1 genes, which code for the internal, rotenone-insensitive NADH-quinone oxidoreductase. In this review, we will discuss our progress and the data generated by these two projects to date. In addition, background information and the significance of various approaches employed to pursue these research objectives will be described.
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Mitochondrial targeting of S. cerevisiae Ndi1 rescues complex I deficiency in human cells.
“Mitochondrial targeting of the S.cerevisiae single subunit NADH oxidase, Ndi1, has been shown to rescue complex I deficiency in human cells [244]”
From Mitochondrial DNA mutations and human disease (2010) · cites this paper as [244]
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Mitochondrial DNA mutations and human disease
Tuppen, H. A. L., Blakely, E. L., Turnbull, D. M., & Taylor, R. W. (2010) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2009.09.005 · Cited by 676 · see citing works
“Mitochondrial targeting of the S.cerevisiae single subunit NADH oxidase, Ndi1, has been shown to rescue complex I de fi ciency in human cells [244] and also protect against neurodegeneration in rats fed with MPTP, a hallucinogen known to cause a form of Parkinson's disease (PD) [245].”
BackgroundMitochondrial respiratory complex I: Structure, function and implication in human diseases
Sharma, L., Lu, J., & Bai, Y. (2009) · Current Medicinal Chemistry · doi:10.2174/092986709787846578 · Cited by 438 · see citing works
- Authors
- Yagi, T., Seo, B. B., Bernardo, S. D., Nakamaru-Ogiso, E., Kao, M.-C., & Matsuno-Yagi, A.
- Affiliations
- Scripps Research Institute (US)
- Corresponding author
- Yagi, Takao
- Venue
- Journal of Bioenergetics and Biomembranes
- Published
- 2001-06
- Volume
- 33
- Issue
- 3
- Pages
- 233-242
- ISSN
- 0145-479X (ISSN-L)
- 1573-6881
- OpenAlex
- W1606704458
- Cited by
- 63
- References
- 97
- Citations by year
- 2025: 1 · 2024: 1 · 2019: 2 · 2016: 2 · 2015: 2 · 2014: 3 · 2013: 2 · 2012: 1
- FWCI
- 2.20
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- Locations
- Journal of Bioenergetics and Biomembranes (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences (R01GM033712)
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK053244)
- National Center for Research Resources (M01RR000833)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Coenzyme Q10 studies and effects
- Keywords
- NADH dehydrogenase, NDH-1, NADH:quinone oxidoreductase, mitochondrial complex I, Paracoccus denitrificans, Thermus thermophilus, enzyme structure and mechanism, proton translocation, mitochondrial disease, gene therapy, NDI1, Saccharomyces cerevisiae, bacterial respiratory chain
- MeSH terms
- Animals, Models, Molecular, NADH, NADPH Oxidoreductases, Paracoccus denitrificans, Saccharomyces cerevisiae, Genetic Therapy, Thermus thermophilus, Protein Subunits, Electron Transport Complex I
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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