Structure of the respiratory NADH:ubiquinone oxidoreductase (complex I)

Grigorieff, Nikolaus

doi:10.1016/s0959-440x(99)80067-0

Cited by 97 publications

(52 citation statements)

References 109 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The NADH dehydrogenase site of CI, which is also the site of electron leakage, is located in the matrix side of the inner mitochondrial membrane [8]. Thus, oxidant production from CI is directed into the mitochondrial matrix where oxidative damage to mitochondrial proteins may occur.…”

Section: Introductionmentioning

confidence: 99%

Age-related alterations in oxidatively damaged proteins of mouse heart mitochondrial electron transport chain complexes

Choksi

Papaconstantinou

2008

Free Radical Biology and Medicine

View full text Add to dashboard Cite

Mitochondrial generated ROS increases with age and is a major factor that damages proteins by oxidative modification. Accumulation of oxidatively damaged proteins has been implicated as a causal factor in the age-associated decline in tissue function. Mitochondrial electron transport chain (ETC) complexes I and III are the principle sites of ROS production, and oxidative modifications to their complex subunits inhibit their in vitro activity. We hypothesize that mitochondrial complex subunits may be primary targets for modification by ROS which may impair normal complex activity. This study of heart mitochondria from young, middle-aged and old mice reveals that there is an agerelated decline in complex I and V activities that correlate with increased oxidative modification to their subunits. The data also show a specificity for modifications of the ETC complex subunits, i.e., several proteins have more than one type of adduct. We postulate that the electron leakage from ETC complexes causes specific damage to their subunits and increased ROS generation as oxidative damage accumulates, leading to further mitochondrial dysfunction, a cyclical process that underlies the progressive decline in physiologic function of aged mouse heart.

show abstract

Section: Introductionmentioning

confidence: 99%

Age-related alterations in oxidatively damaged proteins of mouse heart mitochondrial electron transport chain complexes

Choksi

Papaconstantinou

2008

Free Radical Biology and Medicine

View full text Add to dashboard Cite

show abstract

“…NADH:ubiquinone oxidoreductase (complex I) from the inner membrane of bovine heart mitochondria is a multisubunit, membrane-bound, L-shaped assembly with a molecular mass of over 900 kDa (1)(2)(3). Complex I catalyzes the first step in the electron transport chain (4,5), the transfer of two electrons from NADH to ubiquinone, coupled to the translocation of four protons across the membrane (6).…”

mentioning

confidence: 99%

Definition of the Nuclear Encoded Protein Composition of Bovine Heart Mitochondrial Complex I

Carroll

Shannon

Fearnley

et al. 2002

Journal of Biological Chemistry

148

120

View full text Add to dashboard Cite

Mitochondrial NADH:ubiquinone oxidoreductase (complex I) from bovine heart is a complicated multisubunit, membrane-bound assembly. Seven subunits are encoded by mitochondrial DNA, and the sequences of 36 nuclear encoded subunits have been described. The subunits of complex I and two subcomplexes (I␣ and I␤) were resolved on one-and two-dimensional gels and by reverse-phase high performance liquid chromatography. Mass spectrometric analysis revealed two previously unknown subunits in complex I, named B14.7 and ESSS, one in each subcomplex. Coding sequences for each protein were identified in data bases and were confirmed by cDNA cloning and sequencing. Subunit B14.7 has an acetylated N terminus, no presequence, and contains four potential transmembrane helices. It is homologous to subunit 21.3b from complex I in Neurospora crassa and is related to Tim17, Tim22, and Tim23, which are involved in protein translocation across the inner membrane. Subunit ESSS has a cleaved mitochondrial import sequence and one potential transmembrane helix. A total of 45 different subunits of bovine complex I have now been characterized.

show abstract

“…The complex (Figure 1.9a) has an L-shape with two major sub-units, one predominantly within the membrane and the other protruding into the inner mitochondrial space containing the NADH reaction site [12][13][14][15]. The NADH-CoQ reductase complex is the most complex and largest of the proton pumping enzymes in the mitochondrion and is made up of about 30 separate sub-units; it is also, because of this complexity, the least well understood.…”

Section: The Nadh-coq Reductase Complexmentioning

confidence: 99%

“…At present there is not a crystal structure for the NADH-CoQ reductase complex and the precise pathway of electron transfer within the complex and the mechanism and stoichiometry of proton transport are currently not well established, although a crystal structure of the hydrophilic domain of complex I from Thermus thermoplilus has recently been obtained [17]. For further details of the NADH-CoQ reductase complex, readers are directed to several recent reviews [13,[18][19][20][21].…”

Section: The Nadh-coq Reductase Complexmentioning

confidence: 99%

Bioenergetics and Biological Electron Transport

Bartlett

2008

Bioelectrochemistry

View full text Add to dashboard Cite

Structure of the respiratory NADH:ubiquinone oxidoreductase (complex I)

Cited by 97 publications

References 109 publications

Age-related alterations in oxidatively damaged proteins of mouse heart mitochondrial electron transport chain complexes

Age-related alterations in oxidatively damaged proteins of mouse heart mitochondrial electron transport chain complexes

Definition of the Nuclear Encoded Protein Composition of Bovine Heart Mitochondrial Complex I

Bioenergetics and Biological Electron Transport

Contact Info

Product

Resources

About