Three-dimensional structure of NADH-dehydrogenase from Neurospora crassa by electron microscopy and conical tilt reconstruction

Guénebaut, Vincent; Vincentelli, Renaud; Mills, Deryck J.; Weiss, Hanns; Leonard, Kevin

doi:10.1006/jmbi.1996.0753

Cited by 143 publications

(95 citation statements)

References 19 publications

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“…Both arms of the complex had roughly the same length, as in our earlier model (20). However, the peripheral arm was much broader, especially the linkage between the membrane arm and the peripheral arm, which was in consensus with other models from negatively stained mitochondrial complexes (18,19,21,23). The discrepancies between the old and the new model of the E. coli complex I could have been due to a better preservation of the complex in gold thioglucose together with a more efficient embedding in the staining medium.…”

Section: Discussionsupporting

confidence: 87%

A Novel, Enzymatically Active Conformation of the Escherichia coli NADH:Ubiquinone Oxidoreductase (Complex I)

Böttcher

Scheide

Hesterberg

et al. 2002

Journal of Biological Chemistry

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Electron microscopy has demonstrated the unusual L-shaped structure of the respiratory complex I consisting of two arms, which are arranged perpendicular to each other. We found that the Escherichia coli complex I has an additional stable conformation, with the two arms arranged side by side, resulting in a horseshoeshaped structure. The structure of both conformations was determined by means of electron microscopy of gold thioglucose-stained single particles. They were distinguished from each other by titration of the complex with polyethylene glycol and by means of analytical ultracentrifugation. The transition between the two conformations is induced by the ionic strength of the buffer and is reversible. Only the horseshoe-shaped complex I exhibits enzyme activity in detergent solution, which is abolished by the addition of salt. Therefore, it is proposed that this structure is the native conformation of the complex in the membrane.

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Section: Discussionsupporting

confidence: 87%

A Novel, Enzymatically Active Conformation of the Escherichia coli NADH:Ubiquinone Oxidoreductase (Complex I)

Böttcher

Scheide

Hesterberg

et al. 2002

Journal of Biological Chemistry

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“…The complex has an L shape, whereby the base of the L (containing the hydrophobic domain) is considered to reside in the mitochondrial inner membrane, whereas the stalk of the L (containing the hydrophilic domain) sticks out into the matrix space. This has also been found for the mitochondrial enzymes from Neurospora crassa (32 subunits) (Leonard et al 1987;Hofhaus et al 1991;Guénebaut et al 1997) and Yarrowia lipolytica (40 subunits) (Djafarzadeh et al 2000;Radermacher et al 2006), and for the bacterial enzymes from Escherichia coli (13 subunits) (Guénebaut et al 1998;Morgan and Sazanov 2008) and Aquifex aeolicus (14 subunits) (Peng et al 2003). As expected from the number of subunits, the detailed contours of the stalk and base part of the L-shaped molecule differ among the enzymes (Zickermann et al 2009;Clason et al 2010).…”

Section: Introductionsupporting

confidence: 60%

The reaction of NADPH with bovine mitochondrial NADH:ubiquinone oxidoreductase revisited

Albracht

2010

J Bioenerg Biomembr

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Bovine NADH:ubiquinone oxidoreductase (Complex I) is the first complex in the mitochondrial respiratory chain. It has long been assumed that it contained only one FMN group. However, as demonstrated in 2003, the intact enzyme contains two FMN groups. The second FMN was proposed to be located in a conserved flavodoxin fold predicted to be present in the PSST subunit. The longknown reaction of Complex I with NADPH differs in many aspects from that with NADH. It was proposed that the second flavin group was specifically involved in the reaction with NADPH. The X-ray structure of the hydrophilic domain of Complex I from Thermus thermophilus (Sazanov and Hinchliffe 2006, Science 311, 1430-1436 disclosed the positions of all redox groups of that enzyme and of the subunits holding them. The PSST subunit indeed contains the predicted flavodoxin fold although it did not contain FMN. Inspired by this structure, the present paper describes a re-evaluation of the enigmatic reactions of the bovine enzyme with NADPH. Published data, as well as new freeze-quench kinetic data presented here, are incompatible with the general opinion that NADPH and NADH react at the same site. Instead, it is proposed that these pyridine nucleotides react at opposite ends of the 90Å long chain of prosthetic groups in Complex I. Ubiquinone is proposed to react with the Fe-S clusters in the TYKY subunit deep inside the hydrophilic domain. A new model for electron transfer in Complex I is proposed. In the accompanying paper this model is compared with the one advocated in current literature.

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“…Low resolution electron microscopy analyses [3][4][5][6][7][8][9][10] show that complex I is structurally organized in two major domains: a membrane spanning segment and a peripheral arm, which protrudes into the mitochondrial matrix (or the bacterial cytosol). Sazanov and Hinchliffe reported the crystal structure of the hydrophilic domain of complex I from the bacterium Thermus (T) thermophilus at 3.3 Å resolution [11].…”

Section: Introductionmentioning

confidence: 99%

EXAFS reveals a structural zinc binding site in the bovine NADH‐Q oxidoreductase

et al. 2007

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The metal content of bovine NADH-Q oxidoreductase determined by inductively-coupled plasma atomic-emission spectroscopy reveals the presence of about one atom of zinc per molecule of flavin mononucleotide. We applied Zn K-edge extended X-ray absorption fine structure spectroscopy (EXAFS) to investigate the local structure of the bound zinc ion and to identify the nature of the coordinating residues. The EXAFS spectrum is consistent with a structured zinc binding site. By combining information from first-shell analysis and from metalloprotein data bases putative binding clusters have been built and fitted to the experimental spectrum using ab initio simulations. The best fitting binding cluster is formed by two histidine and two cysteine residues arranged in a tetrahedral geometry.

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Three-dimensional structure of NADH-dehydrogenase from Neurospora crassa by electron microscopy and conical tilt reconstruction

Cited by 143 publications

References 19 publications

A Novel, Enzymatically Active Conformation of the Escherichia coli NADH:Ubiquinone Oxidoreductase (Complex I)

A Novel, Enzymatically Active Conformation of the Escherichia coli NADH:Ubiquinone Oxidoreductase (Complex I)

The reaction of NADPH with bovine mitochondrial NADH:ubiquinone oxidoreductase revisited

EXAFS reveals a structural zinc binding site in the bovine NADH‐Q oxidoreductase

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