| Year |
Citation |
Score |
| 2018 |
Ohnishi T, Ohnishi ST, Salerno JC. Five decades of research on mitochondrial NADH-quinone oxidoreductase (complex I). Biological Chemistry. PMID 30243012 DOI: 10.1515/Hsz-2018-0164 |
0.629 |
|
| 2016 |
Ohnishi T, Tsuyoshi Ohnishi S, Salerno J. Five Decades of Research on Structure/Function of Complex I (NADH-quinone Oxidoreductase) Biochimica Et Biophysica Acta (Bba) - Bioenergetics. 1857: e43. DOI: 10.1016/J.Bbabio.2016.04.314 |
0.528 |
|
| 2014 |
Ohnishi T, Ohnishi S, Salerno J. Role of protein-associated quinones Q-Nf and Q-Ns in complex I energy coupling Biochimica Et Biophysica Acta (Bba) - Bioenergetics. 1837: e46-e47. DOI: 10.1016/j.bbabio.2014.05.065 |
0.486 |
|
| 2013 |
Ohnishi T, Ohnishi ST. Functional Role of Two Protein-Associated Ubiquinone Molecules (Q-NF and Q-NS) for the Proton-Pumping Mechanism in Bovine Heart Complex I (NADH-Ubiquinone Oxidoreductase) Biophysical Journal. 104: 487a. DOI: 10.1016/J.Bpj.2012.11.2685 |
0.406 |
|
| 2012 |
Ohnishi T, Ohnishi ST, Shinzawa-Itoh K, Yoshikawa S, Weber RT. EPR detection of two protein-associated ubiquinone components (SQ(Nf) and SQ(Ns)) in the membrane in situ and in proteoliposomes of isolated bovine heart complex I. Biochimica Et Biophysica Acta. 1817: 1803-9. PMID 22503829 DOI: 10.1016/J.Bbabio.2012.03.032 |
0.39 |
|
| 2012 |
Sinha PK, Nakamaru-Ogiso E, Torres-Bacete J, Sato M, Castro-Guerrero N, Ohnishi T, Matsuno-Yagi A, Yagi T. Electron transfer in subunit NuoI (TYKY) of Escherichia coli NADH:quinone oxidoreductase (NDH-1). The Journal of Biological Chemistry. 287: 17363-73. PMID 22474289 DOI: 10.1074/Jbc.M111.329649 |
0.36 |
|
| 2010 |
Nakamaru-Ogiso E, Kao MC, Chen H, Sinha SC, Yagi T, Ohnishi T. The membrane subunit NuoL(ND5) is involved in the indirect proton pumping mechanism of Escherichia coli complex I. The Journal of Biological Chemistry. 285: 39070-8. PMID 20826797 DOI: 10.1074/Jbc.M110.157826 |
0.33 |
|
| 2010 |
Ohnishi ST, Salerno JC, Ohnishi T. Possible roles of two quinone molecules in direct and indirect proton pumps of bovine heart NADH-quinone oxidoreductase (complex I). Biochimica Et Biophysica Acta. 1797: 1891-3. PMID 20599678 DOI: 10.1016/J.Bbabio.2010.06.010 |
0.575 |
|
| 2010 |
Ohnishi ST, Shinzawa-Itoh K, Ohta K, Yoshikawa S, Ohnishi T. New insights into the superoxide generation sites in bovine heart NADH-ubiquinone oxidoreductase (Complex I): the significance of protein-associated ubiquinone and the dynamic shifting of generation sites between semiflavin and semiquinone radicals. Biochimica Et Biophysica Acta. 1797: 1901-9. PMID 20513438 DOI: 10.1016/J.Bbabio.2010.05.012 |
0.391 |
|
| 2010 |
Ohnishi T. Structural biology: Piston drives a proton pump. Nature. 465: 428-9. PMID 20505714 DOI: 10.1038/465428A |
0.351 |
|
| 2010 |
Nakamaru-Ogiso E, Han H, Matsuno-Yagi A, Keinan E, Sinha SC, Yagi T, Ohnishi T. The ND2 subunit is labeled by a photoaffinity analogue of asimicin, a potent complex I inhibitor. Febs Letters. 584: 883-8. PMID 20074573 DOI: 10.1016/J.Febslet.2010.01.004 |
0.309 |
|
| 2010 |
Ohnishi T, Nakamaru-Ogiso E, Ohnishi ST. A new hypothesis on thesimultaneous direct and indirect coupling mechanism in NADH–quinone oxidoreductase (Complex I) Biochimica Et Biophysica Acta (Bba) - Bioenergetics. 1797: 10. DOI: 10.1016/J.Bbabio.2010.04.046 |
0.309 |
|
| 2009 |
Fato R, Bergamini C, Bortolus M, Maniero AL, Leoni S, Ohnishi T, Lenaz G. Differential effects of mitochondrial Complex I inhibitors on production of reactive oxygen species. Biochimica Et Biophysica Acta. 1787: 384-92. PMID 19059197 DOI: 10.1016/J.Bbabio.2008.11.003 |
0.365 |
|
| 2008 |
Ohnishi T, Ohnishi ST, Shinzawa-Ito K, Yoshikawa S. Functional role of coenzyme Q in the energy coupling of NADH-CoQ oxidoreductase (Complex I): stabilization of the semiquinone state with the application of inside-positive membrane potential to proteoliposomes. Biofactors (Oxford, England). 32: 13-22. PMID 19096096 DOI: 10.1002/Biof.5520320103 |
0.4 |
|
| 2008 |
Zhang Y, Lyver ER, Nakamaru-Ogiso E, Yoon H, Amutha B, Lee DW, Bi E, Ohnishi T, Daldal F, Pain D, Dancis A. Dre2, a conserved eukaryotic Fe/S cluster protein, functions in cytosolic Fe/S protein biogenesis. Molecular and Cellular Biology. 28: 5569-82. PMID 18625724 DOI: 10.1128/Mcb.00642-08 |
0.381 |
|
| 2008 |
Nakamaru-Ogiso E, Matsuno-Yagi A, Yoshikawa S, Yagi T, Ohnishi T. Iron-sulfur cluster N5 is coordinated by an HXXXCXXCXXXXXC motif in the NuoG subunit of Escherichia coli NADH:quinone oxidoreductase (complex I). The Journal of Biological Chemistry. 283: 25979-87. PMID 18603533 DOI: 10.1074/Jbc.M804015200 |
0.365 |
|
| 2008 |
Ohnishi T, Nakamaru-Ogiso E. Were there any "misassignments" among iron-sulfur clusters N4, N5 and N6b in NADH-quinone oxidoreductase (complex I)? Biochimica Et Biophysica Acta. 1777: 703-10. PMID 18486592 DOI: 10.1016/J.Bbabio.2008.04.032 |
0.363 |
|
| 2008 |
Lin T, Sled VD, Ohnishi T, Brennicke A, Grohmann L. Analysis of the Iron-Sulfur Clusters Within the Complex I (NADH: Ubiquinone Oxidoreductase) Isolated from Potato Tuber Mitochondria European Journal of Biochemistry. 230: 1032-1036. DOI: 10.1111/J.1432-1033.1995.1032G.X |
0.413 |
|
| 2005 |
Ohnishi T, Salerno JC. Conformation-driven and semiquinone-gated proton-pump mechanism in the NADH-ubiquinone oxidoreductase (complex I). Febs Letters. 579: 4555-61. PMID 16098512 DOI: 10.1016/J.Febslet.2005.06.086 |
0.619 |
|
| 2005 |
Cooley JW, Ohnishi T, Daldal F. Binding dynamics at the quinone reduction (Qi) site influence the equilibrium interactions of the iron sulfur protein and hydroquinone oxidation (Qo) site of the cytochrome bc1 complex. Biochemistry. 44: 10520-32. PMID 16060661 DOI: 10.1021/Bi050571+ |
0.394 |
|
| 2005 |
Velazquez I, Nakamaru-Ogiso E, Yano T, Ohnishi T, Yagi T. Amino acid residues associated with cluster N3 in the NuoF subunit of the proton-translocating NADH-quinone oxidoreductase from Escherichia coli. Febs Letters. 579: 3164-8. PMID 15922336 DOI: 10.1016/J.Febslet.2005.05.005 |
0.344 |
|
| 2005 |
Ohnishi ST, Ohnishi T, Muranaka S, Fujita H, Kimura H, Uemura K, Yoshida K, Utsumi K. A possible site of superoxide generation in the complex I segment of rat heart mitochondria. Journal of Bioenergetics and Biomembranes. 37: 1-15. PMID 15906144 DOI: 10.1007/S10863-005-4117-Y |
0.384 |
|
| 2005 |
Yano T, Dunham WR, Ohnishi T. Characterization of the delta muH+-sensitive ubisemiquinone species (SQ(Nf)) and the interaction with cluster N2: new insight into the energy-coupled electron transfer in complex I. Biochemistry. 44: 1744-54. PMID 15683258 DOI: 10.1021/Bi048132I |
0.361 |
|
| 2005 |
Ohnishi T, Johnson JE, Yano T, Lobrutto R, Widger WR. Thermodynamic and EPR studies of slowly relaxing ubisemiquinone species in the isolated bovine heart complex I. Febs Letters. 579: 500-6. PMID 15642366 DOI: 10.1016/J.Febslet.2004.11.107 |
0.371 |
|
| 2005 |
Nakamaru-Ogiso E, Yano T, Yagi T, Ohnishi T. Characterization of the iron-sulfur cluster N7 (N1c) in the subunit NuoG of the proton-translocating NADH-quinone oxidoreductase from Escherichia coli. The Journal of Biological Chemistry. 280: 301-7. PMID 15520003 DOI: 10.1074/Jbc.M410377200 |
0.416 |
|
| 2002 |
Magnitsky S, Toulokhonova L, Yano T, Sled VD, Hägerhäll C, Grivennikova VG, Burbaev DS, Vinogradov AD, Ohnishi T. EPR characterization of ubisemiquinones and iron-sulfur cluster N2, central components of the energy coupling in the NADH-ubiquinone oxidoreductase (complex I) in situ. Journal of Bioenergetics and Biomembranes. 34: 193-208. PMID 12171069 DOI: 10.1023/A:1016083419979 |
0.433 |
|
| 2001 |
Yano T, Ohnishi T. The origin of cluster N2 of the energy-transducing NADH-quinone oxidoreductase: Comparisons of phylogenetically related enzymes Journal of Bioenergetics and Biomembranes. 33: 213-222. PMID 11695831 DOI: 10.1023/A:1010782903144 |
0.393 |
|
| 2000 |
Yano T, Magnitsky S, Ohnishi T. Characterization of the complex I-associated ubisemiquinone species: Toward the understanding of their functional roles in the electron/proton transfer reaction Biochimica Et Biophysica Acta - Bioenergetics. 1459: 299-304. PMID 11004443 DOI: 10.1016/S0005-2728(00)00164-X |
0.379 |
|
| 2000 |
Ohnishi T, Moser CC, Page CC, Dutton PL, Yano T. Simple redox-linked proton-transfer design: new insights from structures of quinol-fumarate reductase. Structure (London, England : 1993). 8: R23-32. PMID 10673443 DOI: 10.1016/S0969-2126(00)00098-8 |
0.309 |
|
| 1999 |
Ohnishi T, Magnitsky S, Toulokhonova L, Yano T, Yagi T, Burbaev DS, Vinogradov AD. EPR studies of the possible binding sites of the cluster N2, semiquinones, and specific inhibitors of the NADH:quinone oxidoreductase (complex I) Biochemical Society Transactions. 27: 586-591. PMID 10917647 DOI: 10.1042/Bst0270586 |
0.328 |
|
| 1999 |
Darrouzet E, Valkova-Valchanova M, Ohnishi T, Daldal F. Structure and function of the bacterial bc1 complex: Domain movement, subunit interactions, and emerging rationale engineering attempts Journal of Bioenergetics and Biomembranes. 31: 275-288. PMID 10591533 DOI: 10.1023/A:1005428014548 |
0.382 |
|
| 1999 |
Yano T, Magnitsky S, Sled' VD, Ohnishi T, Yagi T. Characterization of the putative 2x[4Fe-4S]-binding NQO9 subunit of the proton-translocating NADH-quinone oxidoreductase (NDH-1) of Paracoccus denitrificans. Expression, reconstitution, and EPR characterization Journal of Biological Chemistry. 274: 28598-28605. PMID 10497226 DOI: 10.1074/jbc.274.40.28598 |
0.315 |
|
| 1999 |
Ushakova AV, Grivennikova VG, Ohnishi T, Vinogradov AD. Triton X-100 as a specific inhibitor of the mammalian NADH-ubiquinone oxidoreductase (Complex I) Biochimica Et Biophysica Acta - Bioenergetics. 1409: 143-153. PMID 9878712 DOI: 10.1016/S0005-2728(98)00156-X |
0.322 |
|
| 1998 |
Ohnishi T, Sled VD, Yano T, Yagi T, Burbaev DS, Vinogradov AD. Structure-function studies of iron-sulfur clusters and semiquinones in the NADH-Q oxidoreductase segment of the respiratory chain Biochimica Et Biophysica Acta - Bioenergetics. 1365: 301-308. PMID 9693742 DOI: 10.1016/S0005-2728(98)00082-6 |
0.407 |
|
| 1998 |
Dutton PL, Moser CC, Sled VD, Daldal F, Ohnishi T. A reductant-induced oxidation mechanism for complex I. Biochimica Et Biophysica Acta. 1364: 245-57. PMID 9593917 DOI: 10.1016/S0005-2728(98)00031-0 |
0.399 |
|
| 1998 |
Ohnishi T. Iron-sulfur clusters/semiquinones in Complex I Biochimica Et Biophysica Acta - Bioenergetics. 1364: 186-206. PMID 9593887 DOI: 10.1016/S0005-2728(98)00027-9 |
0.432 |
|
| 1997 |
Brasseur G, Sled V, Liebl U, Ohnishi T, Daldal F. The amino-terminal portion of the rieske iron-sulfur protein contributes to the ubihydroquinone oxidation site catalysis of the Rhodobacter capsulatus bc1 complex Biochemistry. 36: 11685-11696. PMID 9305958 DOI: 10.1021/Bi970777D |
0.387 |
|
| 1997 |
Liebl U, Sled V, Brasseur G, Ohnishi T, Daldal F. Conserved nonliganding residues of the Rhodobacter capsulatus rieske iron-sulfur protein of the bc1 complex are essential for protein structure, properties of the [2Fe-2S] cluster, and communication with the quinone pool Biochemistry. 36: 11675-11684. PMID 9305957 DOI: 10.1021/Bi970776L |
0.392 |
|
| 1997 |
Yano T, Chu SS, Sled' VD, Ohnishi T, Yagi T. The proton-translocating NADH-quinone oxidoreductase (NDH-1) of thermophilic bacterium Thermus thermophilus HB-8. Complete DNA sequence of the gene cluster and thermostable properties of the expressed NQO2 subunit Journal of Biological Chemistry. 272: 4201-4211. PMID 9020134 DOI: 10.1074/Jbc.272.7.4201 |
0.352 |
|
| 1996 |
Zhang H, Carrell CJ, Huang D, Sled V, Ohnishi T, Smith JL, Cramer WA. Characterization and crystallization of the lumen side domain of the chloroplast Rieske iron-sulfur protein Journal of Biological Chemistry. 271: 31360-31366. PMID 8940143 DOI: 10.1074/Jbc.271.49.31360 |
0.412 |
|
| 1996 |
Gurbiel RJ, Doan PE, Gassner GT, Macke TJ, Case DA, Ohnishi T, Fee JA, Ballou DP, Hoffman BM. Active site structure of Rieske-type proteins: electron nuclear double resonance studies of isotopically labeled phthalate dioxygenase from Pseudomonas cepacia and Rieske protein from Rhodobacter capsulatus and molecular modeling studies of a Rieske center. Biochemistry. 35: 7834-45. PMID 8672484 DOI: 10.1021/Bi960380U |
0.389 |
|
| 1996 |
Yano T, Sled VD, Ohnishi T, Yagi T. Expression and characterization of the flavoprotein subcomplex composed of 50-kDa (NQO1) and 25-kDa (NQO2) subunits of the proton-translocating NADH-quinone oxidoreductase of Paracoccus denitrificans Journal of Biological Chemistry. 271: 5907-5913. PMID 8621464 DOI: 10.1074/Jbc.271.10.5907 |
0.421 |
|
| 1996 |
Link TA, Saynovits M, Assmann C, Iwata S, Ohnishi T, Von Jagow G. Isolation, characterisation and crystallisation of a water-soluble fragment of the Rieske iron-sulfur protein of bovine heart mitochondrial bc1 complex European Journal of Biochemistry. 237: 71-75. PMID 8620896 DOI: 10.1111/J.1432-1033.1996.0071N.X |
0.393 |
|
| 1995 |
Ingledew WJ, Ohnishi T, Salerno JC. Studies on a stabilisation of ubisemiquinone by Escherichia coli quinol oxidase, cytochrome bo. European Journal of Biochemistry / Febs. 227: 903-8. PMID 7867653 DOI: 10.1111/J.1432-1033.1995.0903P.X |
0.58 |
|
| 1995 |
Hägerhäll C, Sled' V, Hederstedt L, Ohnishi T. The trinuclear iron-sulfur cluster S3 in Bacillus subtilis succinate:menaquinone reductase; effects of a mutation in the putative cluster ligation motif on enzyme activity and EPR properties Bba - Bioenergetics. 1229: 356-362. PMID 7748886 DOI: 10.1016/0005-2728(95)00023-C |
0.387 |
|
| 1995 |
Vinogradov AD, Sled VD, Burbaev DS, Grivennikova VG, Moroz IA, Ohnishi T. Energy-dependent Complex I-associated ubisemiquinones in submitochondrial particles. Febs Letters. 370: 83-7. PMID 7649309 DOI: 10.1016/0014-5793(95)00803-H |
0.378 |
|
| 1995 |
Yano T, Yagi T, Sled VD, Ohnishi T. Expression and characterization of the 66-kilodalton (NQO3) iron-sulfur subunit of the proton-translocating NADH-quinone oxidoreductase of Paracoccus denitrificans Journal of Biological Chemistry. 270: 18264-18270. PMID 7629145 DOI: 10.1074/Jbc.270.31.18264 |
0.422 |
|
| 1995 |
Gavrikova EV, Grivennikova VG, Sled VD, Ohnishi T, Vinogradov AD. Kinetics of the mitochondrial three-subunit NADH dehydrogenase interaction with hexammineruthenium(III) Bba - Bioenergetics. 1230: 23-30. PMID 7612640 DOI: 10.1016/0005-2728(95)00015-B |
0.378 |
|
| 1995 |
Leif H, Sled VD, Ohnishi T, Weiss H, Friedrich T. Isolation and Characterization of the Proton-translocating NADH:ubiquinone Oxidoreductase from Escherichia coli Febs Journal. 230: 538-548. DOI: 10.1111/J.1432-1033.1995.0538H.X |
0.419 |
|
| 1994 |
Friedrich T, van Heek P, Leif H, Ohnishi T, Forche E, Kunze B, Jansen R, Trowitzsch-Kienast W, Höfle G, Reichenbach H. Two binding sites of inhibitors in NADH: ubiquinone oxidoreductase (complex I). Relationship of one site with the ubiquinone-binding site of bacterial glucose:ubiquinone oxidoreductase. European Journal of Biochemistry / Febs. 219: 691-8. PMID 8307034 DOI: 10.1111/J.1432-1033.1994.Tb19985.X |
0.317 |
|
| 1994 |
Yano T, Sled' VD, Ohnishi T, Yagi T. Expression of the 25-kilodalton iron-sulfur subunit of the energy-transducing NADH-ubiquinone oxidoreductase of Paracoccus denitrificans Biochemistry. 33: 494-499. PMID 8286379 DOI: 10.1021/Bi00168A014 |
0.418 |
|
| 1994 |
Ohnishi T, Sled VD, Rudnitzky NI, Jacobson BW, Fukumori Y, Meinhardt SW, Calhoun MW, Gennis RB, Leif H, Freidrich T, Weiss H. Biophysical and biochemical studies of bacterial NADH:quinone oxidoreductase (NDH-1) Biochemical Society Transactions. 22: 70S. PMID 8206301 DOI: 10.1042/Bst022070S |
0.359 |
|
| 1994 |
Friedrich T, Ohnishi T, Forche E, Kunze B, Jansen R, Trowitzsch W, Höfle G, Reichenbach H, Weiss H. Two binding sites for naturally occurring inhibitors in mitochondrial and bacterial NADH:ubiquinone oxidoreductase (complex I). Biochemical Society Transactions. 22: 226-30. PMID 8206236 DOI: 10.1042/Bst0220226 |
0.302 |
|
| 1994 |
Fecke W, Sled VD, Ohnishi T, Weiss H. Disruption of the gene encoding the NADH-binding subunit of NADH:ubiquinone oxidoreductase in Neurospora crassa - Formation of a partially assembled enzyme without FMN and the iron-sulphur cluster N-3 European Journal of Biochemistry. 220: 551-558. PMID 8125114 DOI: 10.1111/J.1432-1033.1994.Tb18655.X |
0.407 |
|
| 1994 |
Tominaga T, Sato S, Ohnishi T, Ohnishi ST. Electron paramagnetic resonance (EPR) detection of nitric oxide produced during forebrain ischemia of the rat Journal of Cerebral Blood Flow and Metabolism. 14: 715-722. PMID 8063867 DOI: 10.1038/Jcbfm.1994.92 |
0.315 |
|
| 1994 |
Sled VD, Rudnitzky NI, Hatefi Y, Ohnishi T. Thermodynamic analysis of flavin in mitochondrial NADH:Ubiquinone oxidoreductase (complex I) Biochemistry. 33: 10069-10075. PMID 8060976 DOI: 10.1021/Bi00199A034 |
0.427 |
|
| 1994 |
Yano T, Sled VD, Ohnishi T, Yagi T. Identification of amino acid residues associated with the [2Fe-2S] cluster of the 25 kDa (NQO2) subunit of the proton-translocating NADH-quinone oxidoreductase of Paracoccus denitrificans Febs Letters. 354: 160-164. PMID 7957917 DOI: 10.1016/0014-5793(94)01107-9 |
0.333 |
|
| 1994 |
Ohnishi T, Meinhardt SW, von Jagow G, Yagi T, Hatefi Y. Effect of ethoxyformic anhydride on the Rieske iron-sulfur protein of bovine heart ubiquinol: Cytochrome c oxidoreductase Febs Letters. 353: 103-107. PMID 7926009 DOI: 10.1016/0014-5793(94)01021-8 |
0.436 |
|
| 1994 |
Friedrich T, Leif H, Sied V, Ohnishi T, Weiss H. Iron-sulfur clusters in the Escherichia coli proton-pumping NADH:ubiquinone oxido-reductase. Journal of Inorganic Biochemistry. 56: 13. DOI: 10.1016/0162-0134(94)85054-2 |
0.393 |
|
| 1993 |
Sato S, Tominaga T, Ohnishi T, Ohnishi ST. EPR spin-trapping study of nitric oxide formation during bilateral carotid occlusion in the rat Bba - Molecular Basis of Disease. 1181: 195-197. PMID 8386941 DOI: 10.1016/0925-4439(93)90111-D |
0.308 |
|
| 1993 |
Sled' VD, Friedrich T, Leif H, Weiss H, Meinhardt SW, Fukumori Y, Calhoun MW, Gennis RB, Ohnishi T. Bacterial NADH-quinone oxidoreductases: Iron-sulfur clusters and related problems Journal of Bioenergetics and Biomembranes. 25: 347-356. PMID 8226716 DOI: 10.1007/Bf00762460 |
0.409 |
|
| 1992 |
Nehls U, Friedrich T, Schmiede A, Ohnishi T, Weiss H. Characterization of assembly intermediates of NADH: Ubiquinone oxidoreductase (complex I) accumulated in Neurospora mitochondria by gene disruption Journal of Molecular Biology. 227: 1032-1042. PMID 1433284 DOI: 10.1016/0022-2836(92)90519-P |
0.391 |
|
| 1992 |
Weidner U, Nehls U, Schneider R, Fecke W, Leif H, Schmiede A, Friedrich T, Zensen R, Schulte U, Ohnishi T, Weiss H. Molecular genetic studies of complex I in Neurospora crassa, Aspergillus niger and Escherichia coli Biochimica Et Biophysica Acta - Bioenergetics. 1101: 177-180. PMID 1385977 DOI: 10.1016/0005-2728(92)90218-Q |
0.405 |
|
| 1992 |
Schmidt M, Friedrich T, Wallrath J, Ohnishi T, Weiss H. Accumulation of the preassembled membrane arm of NADH:ubiquinone oxidoreductase in mitochondria of manganese-limited grown Neurospora crassa Febs Letters. 313: 8-11. PMID 1330699 DOI: 10.1016/0014-5793(92)81172-I |
0.376 |
|
| 1992 |
Meinhardt SW, Ohnishi T. Determination of the position of the Qi - quinone binding from the protein surface of the cytochrome bc1 complex in Rhodobacter capsulates chromatophores Bba - Bioenergetics. 1100: 67-74. PMID 1314666 DOI: 10.1016/0005-2728(92)90127-N |
0.388 |
|
| 1992 |
Davidson E, Ohnishi T, Tokito M, Daldal F. Rhodobacter capsulatus mutants lacking the Rieske FeS protein form a stable cytochrome bc1 subcomplex with an intact quinone reduction site Biochemistry®. 31: 3351-3358. PMID 1313293 DOI: 10.1021/Bi00128A007 |
0.378 |
|
| 1992 |
Davidson E, Ohnishi T, Atta-Asafo-Adjei E, Daldal F. Potential ligands to the [2Fe-2S] Rieske cluster of the cytochrome bc1 complex of rhodobacter capsulatus probed by site-directed mutagenesis Biochemistry®. 31: 3342-3351. PMID 1313292 DOI: 10.1021/Bi00128A006 |
0.388 |
|
| 1992 |
Hederstedt L, Ohnishi T. Chapter 7 Progress in succinate:quinone oxidoreductase research New Comprehensive Biochemistry. 23: 163-198. DOI: 10.1016/S0167-7306(08)60175-1 |
0.308 |
|
| 1991 |
Wang DC, Meinhardt SW, Sackmann U, Weiss H, Ohnishi T. The iron-sulfur clusters in the two related forms of mitochondrial NADH: ubiquinone oxidoreductase made by Neurospora crassa. European Journal of Biochemistry. 197: 257-64. PMID 1849820 DOI: 10.1111/J.1432-1033.1991.Tb15906.X |
0.411 |
|
| 1991 |
Ohnishi T. Q-band ENDOR spectra of the rieske protein from rhodobactor capsulatus ubiquinol-cytochrome c oxidoreductase show two histidines coordinated to the [2Fe-2S] cluster Biochemistry. 30: 11579-11584. PMID 1660722 DOI: 10.1021/Bi00113A013 |
0.419 |
|
| 1989 |
Meinhardt SW, Gennis RB, Ohnishi T. EPR studies of the cytochrome-d complex of Escherichia coli. Biochimica Et Biophysica Acta. 975: 175-84. PMID 2544229 DOI: 10.1016/S0005-2728(89)80216-6 |
0.312 |
|
| 1989 |
Gatti DL, Meinhardt SW, Ohnishi T, Tzagoloff A. Structure and function of the mitochondrial bc1 complex. A mutational analysis of the yeast Rieske iron-sulfur protein. Journal of Molecular Biology. 205: 421-35. PMID 2538628 DOI: 10.1016/0022-2836(89)90352-5 |
0.399 |
|
| 1989 |
Lorusso M, Cocco T, Boffoli D, Gatti D, Meinhardt S, Ohnishi T, Papa S. Effect of papain digestion on polypeptide subunits and electron-transfer pathways in mitochondrial b-c1 complex. European Journal of Biochemistry. 179: 535-40. PMID 2537722 DOI: 10.1111/J.1432-1033.1989.Tb14580.X |
0.438 |
|
| 1989 |
Ichiki T, Tanaka M, Kobayashi M, Sugiyama N, Suzuki H, Nishikimi M, Ohnishi T, Nonaka I, Wada Y, Ozawa T. Disproportionate deficiency of iron-sulfur clusters and subunits of complex I in mitochondrial encephalomyopathy. Pediatric Research. 25: 194-201. PMID 2493147 DOI: 10.1203/00006450-198902000-00023 |
0.32 |
|
| 1988 |
Yagi T, Hon-Nami K, Ohnishi T. Purification and characterization of two types of NADH-quinone reductase from Thermus thermophilus HB-8. Biochemistry. 27: 2008-2013. PMID 3378042 DOI: 10.1021/Bi00406A030 |
0.396 |
|
| 1988 |
Matsushita K, Ohnishi T, Kaback HR. NADH-ubiquinone oxidoreductases of the Escherichia coli aerobic respiratory chain. Biochemistry. 26: 7732-7. PMID 3122832 DOI: 10.1021/Bi00398A029 |
0.338 |
|
| 1988 |
Ohnishi T, Brandt U, von Jagow G. Studies on the effect of stigmatellin derivatives on cytochrome b and the Rieske iron-sulfur cluster of cytochrome c reductase from bovine heart mitochondria. European Journal of Biochemistry. 176: 385-9. PMID 2843373 DOI: 10.1111/J.1432-1033.1988.Tb14293.X |
0.386 |
|
| 1988 |
Pennoyer JD, Ohnishi T, Trumpower BL. Purification and properties of succinate-ubiquinone oxidoreductase complex from Paracoccus denitrificans. Biochimica Et Biophysica Acta. 935: 195-207. PMID 2843228 DOI: 10.1016/0005-2728(88)90216-2 |
0.391 |
|
| 1987 |
Telser J, Hoffman BM, LoBrutto R, Ohnishi T, Tsai AL, Simpkin D, Palmer G. Evidence for N coordination to Fe in the [2Fe-2S] center in yeast mitochondrial complex III Comparison with similar findings for analogous bacterial [2Fe-2S] proteins Febs Letters. 214: 117-121. PMID 3032676 DOI: 10.1016/0014-5793(87)80024-8 |
0.41 |
|
| 1986 |
von Jagow G, Link TA, Ohnishi T. Organization and function of cytochrome b and ubiquinone in the cristae membrane of beef heart mitochondria Journal of Bioenergetics and Biomembranes. 18: 157-179. PMID 2426249 DOI: 10.1007/Bf00743462 |
0.35 |
|
| 1985 |
Ohnishi T, Harmon HJ, Waring AJ. Electron-paramagnetic-resonance studies on the spatial relationship of redox components in cytochrome oxidase. Biochemical Society Transactions. 13: 607-11. PMID 2993072 DOI: 10.1042/Bst0130607 |
0.31 |
|
| 1985 |
von Jagow G, Ohnishi T. The chromone inhibitor stigmatellin--binding to the ubiquinol oxidation center at the C-side of the mitochondrial membrane. Febs Letters. 185: 311-5. PMID 2987042 DOI: 10.1016/0014-5793(85)80929-7 |
0.362 |
|
| 1984 |
Moreadith RW, Batshaw ML, Ohnishi T, Kerr D, Knox B, Jackson D, Hruban R, Olson J, Reynafarje B, Lehninger AL. Deficiency of the iron-sulfur clusters of mitochondrial reduced nicotinamide-adenine dinucleotide-ubiquinone oxidoreductase (complex I) in an infant with congenital lactic acidosis. The Journal of Clinical Investigation. 74: 685-97. PMID 6432847 DOI: 10.1172/JCI111484 |
0.311 |
|
| 1984 |
Lin CI, Ohnishi T, Clejan L, Beattie DS. The presence of the iron-sulfur protein (subunit V) of complex III in mitochondria of heme-deficient yeast cells lacking iron-sulfur clusters detectable by electron paramagnetic resonance. European Journal of Biochemistry. 137: 179-83. PMID 6317381 DOI: 10.1111/J.1432-1033.1983.Tb07812.X |
0.44 |
|
| 1982 |
Capeillere-Blandin C, Ohnishi T. Investigation of the iron-sulfur clusters in some mitochondrial mutants of Saccharomyces cerevisiae. A possible correlation between Rieske's iron-sulfur cluster and cytochrome b. European Journal of Biochemistry. 122: 403-13. PMID 6277636 DOI: 10.1111/J.1432-1033.1982.Tb05895.X |
0.428 |
|
| 1981 |
Blum H, Poole RK, Ohnishi T. The orientation of iron-sulphur clusters in membrane multilayers prepared from aerobically-grown Escherichia coli K12 and a cytochrome-deficient mutant. The Biochemical Journal. 190: 385-93. PMID 6258566 DOI: 10.1042/Bj1900385 |
0.355 |
|
| 1980 |
Salerno JC, Ohnishi T. Studies on the stabilized ubisemiquinone species in the succinate-cytochrome c reductase segment of the intact mitochondrial membrane system. The Biochemical Journal. 192: 769-81. PMID 6263261 DOI: 10.1042/Bj1920769 |
0.597 |
|
| 1980 |
Ohnishi T, Lloyd D, Lindmark DG, Müller M. Respiration of Tritrichomonas foetus: components detected in hydrogenosomes and in intact cells by electron paramagnetic resonance spectrometry. Molecular and Biochemical Parasitology. 2: 39-50. PMID 6258070 DOI: 10.1016/0166-6851(80)90047-X |
0.392 |
|
| 1980 |
Blum H, Leigh JS, Ohnishi T. Effect of dysprosium on the spin-lattice relaxation time of cytochrome c and cytochrome a. Biochimica Et Biophysica Acta. 626: 31-40. PMID 6257306 DOI: 10.1016/0005-2795(80)90194-4 |
0.532 |
|
| 1980 |
Thayer WS, Ohnishi T, Rubin E. Characterization of iron-sulfur clusters in rat liver submitochondrial particles by electron paramagnetic resonance spectroscopy. Alterations produced by chronic ethanol consumption. Biochimica Et Biophysica Acta. 591: 22-36. PMID 6248107 DOI: 10.1016/0005-2728(80)90217-0 |
0.378 |
|
| 1980 |
Ingledew WJ, Reid GA, Poole RK, Blum H, Ohnishi T. The iron-sulphur centres of aerobically-grown escherichia coli K12. An electron paramagnetic resonance study Febs Letters. 111: 223-227. PMID 6244182 DOI: 10.1016/0014-5793(80)80798-8 |
0.347 |
|
| 1979 |
Blum H, Salerno JC, Rich PR, Ohnishi T. Exchange integral for a variety of tetranuclear ferredoxins. Biochimica Et Biophysica Acta. 548: 139-46. PMID 226131 DOI: 10.1016/0005-2728(79)90194-4 |
0.594 |
|
| 1979 |
Salerno JC, Blum H, Ohnishi T. The orientation of iron-sulfur clusters and a spin-coupled ubiquinone pair in the mitochondrial membrane. Biochimica Et Biophysica Acta. 547: 270-81. PMID 223637 DOI: 10.1016/0005-2728(79)90010-0 |
0.622 |
|
| 1979 |
Ohnishi T, King TE. EPR and other properties of succinate dehydrogenase. Methods in Enzymology. 53: 483-95. PMID 213687 DOI: 10.1016/S0076-6879(78)53051-6 |
0.352 |
|
| 1978 |
Blum H, Leigh JS, Salerno JC, Ohnishi T. The orientation of bovine adrenal cortex cytochrome P-450 in submitochondrial particle multilayers. Archives of Biochemistry and Biophysics. 187: 153-7. PMID 207224 DOI: 10.1016/0003-9861(78)90017-6 |
0.647 |
|
| 1977 |
Adar F, Blum H, Leigh JS, Ohnishi T, Salerno J, Kimura T. Anti-ferromagnetic exchange in beef adrenodoxin as measured by resonance raman spectroscopy Febs Letters. 84: 214-216. PMID 598498 DOI: 10.1016/0014-5793(77)80690-X |
0.625 |
|
| 1977 |
Salerno JC, Harmon HJ, Blum H, Leigh JS, Ohnishi T. A transmembrane quinone pair in the succinate dehydrogenase--cytochrome b region. Febs Letters. 82: 179-82. PMID 199459 DOI: 10.1016/0014-5793(77)80579-6 |
0.635 |
|
| 1977 |
Blum H, Salerno JC, Prince RC, Leigh JS, Ohnishi T. Electron paramagnetic resonance determination of a low-lying excited state in Chromatium vinosum high-potential iron protein. Biophysical Journal. 20: 23-31. PMID 198036 DOI: 10.1016/S0006-3495(77)85534-3 |
0.668 |
|
| 1977 |
Salerno JC, Ohnishi T, Blum H, Leigh JS. Determination of the exchange integral in binuclear iron-sulfur clusters in proteins of varying complexity. Biochimica Et Biophysica Acta. 494: 191-7. PMID 198006 DOI: 10.1016/0005-2795(77)90147-7 |
0.694 |
|
| 1977 |
Salerno JC, Ohnishi T. Spin coupling between electron carriers in the dehydrogenase segments of the respiratory chain. Biochemical and Biophysical Research Communications. 75: 618-24. PMID 193495 DOI: 10.1016/0006-291X(77)91517-0 |
0.61 |
|
| 1977 |
Case GD, Ohnishi T, Leigh JS. Intramitochondrial positions of ubiquinone and iron-sulphur centres determined by dipolar interactions with paramagnetic ions. The Biochemical Journal. 160: 785-95. PMID 189759 DOI: 10.1042/Bj1600785 |
0.588 |
|
| 1977 |
Salerno JC, Harmon HJ, Blum H, Leigh JS, Ohnishi T. A transmembrane quinone pair in the succinate dehydrogenase-cytochrome b region Febs Letters. 82: 179-182. DOI: 10.1016/0014-5793(77)80579-6 |
0.61 |
|
| 1976 |
Salerno JC, Ohnishi T. Tetranuclear and binuclear iron-sulfur clusters in succinate dehydrogenase: a method of iron quantitation by formation of paramagnetic complexes. Biochemical and Biophysical Research Communications. 73: 833-40. PMID 188423 DOI: 10.1016/0006-291X(76)90884-6 |
0.616 |
|
| 1976 |
Salerno JC, Ohnishi T. Effects of ethanol and acetaldehyde on iron-sulfure centers in the mitochondrial respiratory chain. Archives of Biochemistry and Biophysics. 176: 757-65. PMID 185968 DOI: 10.1016/0003-9861(76)90220-4 |
0.604 |
|
| 1976 |
Ingledew WJ, Salerno JC, Ohnishi T. Thermodynamic resolution of cytochrome P450 and characterization of an iron-sulfur center in rat liver microsomal preparations. Archives of Biochemistry and Biophysics. 174: 298-304. PMID 180896 DOI: 10.1016/0003-9861(76)90348-9 |
0.589 |
|
| 1976 |
Ohnishi T. Studies on the mechanism of site I energy conservation. European Journal of Biochemistry. 64: 91-103. PMID 179811 DOI: 10.1111/J.1432-1033.1976.Tb10277.X |
0.345 |
|
| 1976 |
Ohnishi T, Ingledew WJ, Shiraishi S. Resolution and functional characterization of two mitochondrial iron sulphur centres of the 'high potential iron sulphur protein' type Biochemical Journal. 153: 39-48. PMID 176999 DOI: 10.1042/Bj1530039 |
0.398 |
|
| 1976 |
Ingledew WJ, Salerno JC, Ohnishi T. Studies on electron paramagnetic resonance spectra manifested by a respiratory chain hydrogen carrier. Archives of Biochemistry and Biophysics. 177: 176-84. PMID 11748 DOI: 10.1016/0003-9861(76)90427-6 |
0.6 |
|
| 1975 |
Ohnishi T. Thermodynamic and EPR characterization of iron-sulfur centers in the NADH-ubiquinone segment of the mitochondrial respiratory chain in pigeon heart. Biochimica Et Biophysica Acta. 387: 475-90. PMID 166670 DOI: 10.1016/0005-2728(75)90087-0 |
0.331 |
|
| 1975 |
Ingledew WJ, Ohnishi T. Properties of the S-3 iron-sulphur centre of succinate dehydrogenase in the intact respiratory chain of beef heart mitochondria. Febs Letters. 54: 167-71. PMID 165977 DOI: 10.1016/0014-5793(75)80067-6 |
0.414 |
|
| 1975 |
Ohnishi T, Ingledew WJ, Shiraishi S. Existence of two distinct hipip-type iron-sulfur centers in mitochondria Biochemical and Biophysical Research Communications. 63: 894-899. PMID 165818 DOI: 10.1016/0006-291X(75)90652-X |
0.395 |
|
| 1974 |
Ohnishi T, Leigh JS, Ian Ragan C, Racker E. Low temperature electron paramagnetic resonance studies on iron-sulfur centers in cardiac NADH dehydrogenase Biochemical and Biophysical Research Communications. 56: 775-782. PMID 4151193 DOI: 10.1016/0006-291X(74)90672-X |
0.6 |
|
| 1973 |
Ohnishi T, Hemington JG, LaNoue KF, Morris HP, Williamson JR. Electron paramagnetic resonance studies of iron-sulfur centers in mitochondria prepared from three morris hepatomas with different growth rates Biochemical and Biophysical Research Communications. 55: 372-381. PMID 4358400 DOI: 10.1016/0006-291X(73)91097-8 |
0.375 |
|
| 1972 |
Ohnishi T, Asakura T, Wilson DF, Chance B. The oxidation-reduction potentials of iron-sulfur centers in the site I region of the respiratory chain in C. utilis submitochondrial particles. Febs Letters. 21: 59-62. PMID 11946475 DOI: 10.1016/0014-5793(72)80163-7 |
0.348 |
|
| 1972 |
Ohnishi T, Panebianco P, Chance B. Studies on site I phosphorylation, EPR detectable iron-sulfur proteins and piericidin A sensitivity in the in vivo induction system of Candida utilis cells. Biochemical and Biophysical Research Communications. 49: 99-106. PMID 4342729 DOI: 10.1016/0006-291X(72)90014-9 |
0.325 |
|
| 1972 |
Ohnishi T, Wilson DF, Asakura T, Chance B. Studies on iron-sulfur proteins in the site I region of the respiratory chain in pigeon heart mitochondria and submitochondrial particles. Biochemical and Biophysical Research Communications. 46: 1631-8. PMID 4335622 DOI: 10.1016/0006-291X(72)90796-6 |
0.396 |
|
| 1969 |
Ohnishi T, Schleyer H, Chance B. Studies on non-heme iron proteins and the piericidin A binding site of submitochondrial particles from Candida utilis cells grown in media of varying iron concentrations. Biochemical and Biophysical Research Communications. 36: 487-93. PMID 4309785 DOI: 10.1016/0006-291X(69)90591-9 |
0.386 |
|
| 1967 |
Chance B, Ernster L, Garland PB, Lee CP, Light PA, Ohnishi T, Ragan CI, Wong D. Flavoproteins of the mitochondrial respiratory chain. Proceedings of the National Academy of Sciences of the United States of America. 57: 1498-505. PMID 4292153 DOI: 10.1073/pnas.57.5.1498 |
0.397 |
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