| Name | complex I |
|---|---|
| Synonyms | 39kD; CI 39kD; Complex I; Complex I 39kD; NADH dehydrogenase (ubiquinone) Fe S protein 2 like; NADH ubiquinone oxidoreductase 39 kDa subunit mitochondrial; NADH ubiquinone oxidoreductase 39 kDa subunit; NDUFA 9… |
| Name | sulfur |
|---|---|
| CAS | sulfur |
| PubMed | Abstract | RScore(About this table) | |
|---|---|---|---|
| 20091229 | Baymann F, Nitschke W: Heliobacterial Rieske/cytb complex. . Photosynth Res. 2010 Jan 21. They indicate that the complex is related to the b (6) f complex in agreement with the phylogenetic position of the organism. |
1(0,0,0,1) | Details |
| 20133838 | Roessler MM, King MS, Robinson AJ, Armstrong FA, Harmer J, Hirst J: Direct assignment of EPR spectra to structurally defined iron-sulfur clusters in complex I by double electron-electron resonance. Proc Natl Acad Sci U S A. 2010 Feb 2;107(5):1930-5. Epub 2010 Jan 19. Complex I contains a to oxidize and an unusually long series of iron-sulfur (FeS) clusters, in several subunits, to transfer the electrons to |
92(1,1,2,7) | Details |
| 19752196 | Sheftel AD, Stehling O, Pierik AJ, Netz DJ, Kerscher S, Elsasser HP, Wittig I, Balk J, Brandt U, Lill R: Human ind1, an iron-sulfur cluster assembly factor for respiratory complex I. Mol Cell Biol. 2009 Nov;29(22):6059-73. Epub 2009 Sep 14. |
18(0,0,2,8) | Details |
| 19445896 | Couch VA, Medvedev ES, Stuchebrukhov AA: Electrostatics of the FeS clusters in respiratory complex I. . Biochim Biophys Acta. 2009 Oct;1787(10):1266-71. Epub 2009 May 13. We present accurate electrostatic interaction energies for the iron-sulfur (FeS) clusters of complex I to facilitate the development of models and the interpretation of experiments in connection to electron transfer (ET) in this enzyme. |
84(1,1,1,4) | Details |
| 19682435 | Zerzankova L, Suchankova T, Vrana O, Farrell NP, Brabec V, Kasparkova J: Conformation and recognition of DNA modified by a new antitumor dinuclear PtII complex resistant to decomposition by sulfur nucleophiles. Biochem Pharmacol. 2010 Jan 15;79(2):112-21. Epub 2009 Aug 12. This new, long-chain bifunctional dinuclear Pt (II) complex is resistant to metabolic decomposition by sulfur-containing nucleophiles. |
81(1,1,1,1) | Details |
| 19842617 | Lyubenova S, Maly T, Zwicker K, Brandt U, Ludwig B, Prisner T: Multifrequency pulsed electron paramagnetic resonance on metalloproteins. Acc Chem Res. 2010 Feb 16;43(2):181-9. Hyperfine sublevel correlation spectroscopy (HYSCORE) was used to study the ligand sphere of iron-sulfur clusters in complex I of the mitochondrial respiratory chain and substrate binding to the enzyme polysulfide reductase. |
37(0,1,2,2) | Details |
| 20117074 | Tocilescu MA, Fendel U, Zwicker K, Drose S, Kerscher S, Brandt U: The role of a conserved in the 49-kDa subunit of complex I for binding and reduction. Biochim Biophys Acta. 2010 Feb 1. This places the substrate in an ideal distance to its electron donor iron-sulfur cluster N2 for efficient electron transfer during the catalytic cycle of complex I. |
36(0,1,1,6) | Details |
| 20025615 | Hirst J: Towards the molecular mechanism of respiratory complex I. . Biochem J. 2009 Dec 23;425(2):327-39. Thus energy transduction by complex I comprises oxidation by a intramolecular electron transfer from the flavin to bound along a chain of iron-sulfur clusters, reduction and translocation. |
35(0,1,1,5) | Details |
| 19366602 | Maly T, Zwicker K, Cernescu A, Brandt U, Prisner TF: New pulsed EPR methods and their application to characterize mitochondrial complex I. Biochim Biophys Acta. 2009 Jun;1787(6):584-92. Epub 2009 Feb 12. Here we give an overview of the use of pulsed EPR spectroscopy to study the iron-sulfur clusters of NADH:ubiquinone oxidoreductase (complex I). |
6(0,0,1,1) | Details |
| 19635800 | Berrisford JM, Sazanov LA: Structural basis for the mechanism of respiratory complex I. . J Biol Chem. 2009 Oct 23;284(43):29773-83. Epub 2009 Jul 27. |
5(0,0,0,5) | Details |
| 19366614 | Zickermann V, Kerscher S, Zwicker K, Tocilescu MA, Radermacher M, Brandt U: Architecture of complex I and its implications for electron transfer and pumping. Biochim Biophys Acta. 2009 Jun;1787(6):574-83. Epub 2009 Feb 7. The reduction site close to iron-sulfur cluster N2 at the interface of the 49-kDa and PSST subunits has been mapped by extensive site directed mutagenesis. |
4(0,0,0,4) | Details |
| 19961238 | Shinzawa-Itoh K, Seiyama J, Terada H, Nakatsubo R, Naoki K, Nakashima Y, Yoshikawa S: Bovine heart NADH-ubiquinone oxidoreductase contains one molecule of with ten isoprene units as one of the cofactors. Biochemistry. 2010 Jan 26;49(3):487-92. NADH-ubiquinone oxidoreductase (Complex I) is located at the entrance of the mitochondrial electron transfer chain and transfers electrons from to with 10 isoprene units (Q (10)) coupled with pumping. An improved purification method including solubilization of mitochondrial membrane with followed by gradient centrifugation and anion-exchange column chromatography provided reproducibly a heme-free preparation containing 1 Q (10), 70 atoms of phospholipids, 1 1 FMN, 30 inorganic sulfur ions, and 30 iron atoms as the intrinsic constituents. |
4(0,0,0,4) | Details |
| 19507904 | Wittekindt C, Schwarz M, Friedrich T, Koslowski T: Aromatic amino acids as stepping stones in charge transfer in respiratory complex I: an unusual mechanism deduced from atomistic theory and bioinformatics. J Am Chem Soc. 2009 Jun 17;131(23):8134-40. |
3(0,0,0,3) | Details |
| 19348891 | Stehling O, Sheftel AD, Lill R: Chapter 12 Controlled expression of iron-sulfur cluster assembly components for respiratory chain complexes in mammalian cells. Methods Enzymol. 2009;456:209-31. Impaired function of the mitochondria-located Fe/S cluster (ISC) assembly machinery affects all cellular Fe/S proteins, including enzymes of the respiratory chain, oxidoreductase (complex I; eight Fe/S clusters), oxidoreductase (complex II; three Fe/S clusters), and cytochrome bc (1) complex (complex III; one Fe/S cluster). |
2(0,0,0,2) | Details |
| 19577535 | Schultze M, Forberich B, Rexroth S, Dyczmons NG, Roegner M, Appel J: Localization of cytochrome b6f complexes implies an incomplete respiratory chain in cytoplasmic membranes of the cyanobacterium Synechocystis sp. Biochim Biophys Acta. 2009 Dec;1787(12):1479-85. Epub 2009 Jul 3. The cytochrome b (6) f complex is an integral part of the photosynthetic and respiratory electron transfer chain of oxygenic photosynthetic bacteria. |
2(0,0,0,2) | Details |
| 20163106 | Semeniuc RF, Reamer TJ, Blitz JP, Wheeler KA, Smith MD: Functionalized O-alkyldithiocarbonates: a new class of ligands designed for luminescent heterometallic materials. Inorg Chem. 2010 Mar 15;49(6):2624-9. The ligand coordinates to a [(bipy) Re (CO)(3)](+) center in a monodentate fashion through one of its soft sulfur atoms, leaving the hard terminus free for further coordination chemistry. Using a Ni (II) dithiophosphonate linker, the heterometallic {[CH (3) OCH (2) CH (2) OP (An) S (2)](2) Ni}[4-PyCH (2) OCS (2) Re (bipy)(CO)(3)](2) complex is obtained, through the coordination of two groups to the Ni (II) center. |
1(0,0,0,1) | Details |
| 19780620 | Reger DL, Elgin JD, Foley EA, Smith MD, Grandjean F, Long GJ: Structural, magnetic, and Mossbauer spectral study of the electronic spin-state transition in [Fe{HC (3-Mepz) 2 (5-Mepz)}2](BF4) 2. Inorg Chem. 2009 Oct 5;48(19):9393-401. At 294 K the complex is predominately high-spin with Fe-N bond distances averaging 2.14 A, distances that are somewhat shorter than expected for a purely high-spin iron (II) complex because of the presence of an admixture of about 80% high-spin and 20% low-spin iron (II). |
1(0,0,0,1) | Details |
| 20075289 | Tinsley N, Iqbal M, Pumford NR, Lassiter K, Ojano-Dirain C, Wing T, Bottje W: Investigation of mitochondrial protein expression and oxidation in heart muscle in low and high feed efficient male broilers in a single genetic line. Poult Sci. 2010 Feb;89(2):349-52. The expression of 6 electron transport chain proteins [complex II, 70S subunit (CII 70S); iron-sulfur-containing protein (ISP), cytochrome b (Cyt b), cytochrome (Cyt c1) (of complex III); and cytochrome oxidase subunit II (COX II) (of complex IV)] and adenine nucleotide translocator 1 (ANT1) were higher in low feed efficiency heart mitochondria, but 1 protein [NAD subunit 6c (NAD6c) (complex I)] was higher in high feed efficiency birds. |
1(0,0,0,1) | Details |
| 19542287 | Cromie GA: Phylogenetic ubiquity and shuffling of the bacterial RecBCD and AddAB recombination complexes. J Bacteriol. 2009 Aug;191(16):5076-84. Epub 2009 Jun 19. Examination of the phylogenetic distribution of AddAB and RecBCD revealed that one or the other complex is present in most sequenced bacteria. Finally, it appears that two sequence motifs, the Walker A box involved in ATP binding and an iron-sulfur- cluster, are present only in subsets of AddB proteins, suggesting the existence of mechanistically distinct classes of AddB. |
1(0,0,0,1) | Details |
| 19821612 | Reyda MR, Fugate CJ, Jarrett JT: A complex between synthase and the iron-sulfur cluster assembly chaperone HscA that enhances in vivo cluster assembly. Biochemistry. 2009 Nov 17;48(45):10782-92. BioB binds to HscA in an ATP/ADP-independent manner, and a high-affinity complex is also formed with a truncated form of HscA that lacks the nucleotide binding domain. |
1(0,0,0,1) | Details |
| 20023300 | Lhee S, Kolling DR, Nair SK, Dikanov SA, Crofts AR: Modifications of protein environment of the [2Fe-2S] cluster of the bc1 complex: effects on the biophysical properties of the rieske iron-sulfur protein and on the kinetics of the complex. J Biol Chem. 2010 Mar 19;285(12):9233-48. Epub 2009 Dec 20. The rate-determining step in the overall turnover of the bc (1) complex is electron transfer from to the Rieske iron-sulfur protein (ISP) at the Q (o)-site. |
1(0,0,0,1) | Details |
| 19808020 | Chan SY, Zhang YY, Hemann C, Mahoney CE, Zweier JL, Loscalzo J: MicroRNA-210 controls mitochondrial metabolism during hypoxia by repressing the iron-sulfur cluster assembly proteins ISCU1/2. Cell Metab. 2009 Oct;10(4):273-84. In turn, by repressing ISCU1/2 during hypoxia, miR-210 decreases the activity of prototypical iron-sulfur proteins controlling mitochondrial metabolism, including Complex I and aconitase. |
1(0,0,0,1) | Details |
| 20080550 | Grawert T, Span I, Eisenreich W, Rohdich F, Eppinger J, Bacher A, Groll M: Probing the reaction mechanism of IspH protein by x-ray structure analysis. Proc Natl Acad Sci U S A. 2010 Jan 19;107(3):1077-81. Epub 2009 Dec 28. This conversion is catalyzed by IspH protein comprising a central iron-sulfur cluster as electron transfer cofactor in the active site. The resulting alkoxide complex is coupled to a -bonding network, which serves as reservoir via a Thr167 relay. |
1(0,0,0,1) | Details |