| Year |
Citation |
Score |
| 2019 |
Lengalova A, Fojtikova-Proskova V, Vavra J, Martínek V, Stranava M, Shimizu T, Martinkova M. Kinetic analysis of a globin-coupled diguanylate cyclase, YddV: Effects of heme iron redox state, axial ligands, and heme distal mutations on catalysis. Journal of Inorganic Biochemistry. 201: 110833. PMID 31520879 DOI: 10.1016/j.jinorgbio.2019.110833 |
0.3 |
|
| 2014 |
Anzenbacher P, Marchal S, Palacký J, Anzenbacherová E, Domaschke T, Lange R, Shimizu T, Kitanishi K, Stranava M, Stiborová M, Martinkova M. Pressure effects reveal that changes in the redox states of the heme iron complexes in the sensor domains of two heme-based oxygen sensor proteins, EcDOS and YddV, have profound effects on their flexibility. The Febs Journal. 281: 5208-19. PMID 25238584 DOI: 10.1111/febs.13060 |
0.305 |
|
| 2012 |
Takahashi H, Sekimoto M, Tanaka M, Tanaka A, Igarashi J, Shimizu T. Hydrogen sulfide stimulates the catalytic activity of a heme-regulated phosphodiesterase from Escherichia coli (Ec DOS). Journal of Inorganic Biochemistry. 109: 66-71. PMID 22387619 DOI: 10.1016/J.Jinorgbio.2012.01.001 |
0.376 |
|
| 2012 |
Uchida T, Sagami I, Shimizu T, Ishimori K, Kitagawa T. Effects of the bHLH domain on axial coordination of heme in the PAS-A domain of neuronal PAS domain protein 2 (NPAS2): conversion from His119/Cys170 coordination to His119/His171 coordination. Journal of Inorganic Biochemistry. 108: 188-95. PMID 22245004 DOI: 10.1016/J.Jinorgbio.2011.12.005 |
0.358 |
|
| 2012 |
Nakajima K, Kitanishi K, Kobayashi K, Kobayashi N, Igarashi J, Shimizu T. Leu65 in the heme distal side is critical for the stability of the Fe(II)-O2 complex of YddV, a globin-coupled oxygen sensor diguanylate cyclase. Journal of Inorganic Biochemistry. 108: 163-70. PMID 22005448 DOI: 10.1016/J.Jinorgbio.2011.09.019 |
0.378 |
|
| 2011 |
Kitanishi K, Kobayashi K, Uchida T, Ishimori K, Igarashi J, Shimizu T. Identification and functional and spectral characterization of a globin-coupled histidine kinase from Anaeromyxobacter sp. Fw109-5. The Journal of Biological Chemistry. 286: 35522-34. PMID 21852234 DOI: 10.1074/Jbc.M111.274811 |
0.382 |
|
| 2011 |
Igarashi J, Sasaki T, Kobayashi N, Yoshioka S, Matsushita M, Shimizu T. Autophosphorylation of heme-regulated eukaryotic initiation factor 2α kinase and the role of the modification in catalysis. The Febs Journal. 278: 918-28. PMID 21223507 DOI: 10.1111/J.1742-4658.2011.08007.X |
0.378 |
|
| 2011 |
Hayasaka K, Kitanishi K, Igarashi J, Shimizu T. Heme-binding characteristics of the isolated PAS-B domain of mouse Per2, a transcriptional regulatory factor associated with circadian rhythms. Biochimica Et Biophysica Acta. 1814: 326-33. PMID 20887817 DOI: 10.1016/J.Bbapap.2010.09.007 |
0.402 |
|
| 2010 |
Kitanishi K, Kobayashi K, Kawamura Y, Ishigami I, Ogura T, Nakajima K, Igarashi J, Tanaka A, Shimizu T. Important roles of Tyr43 at the putative heme distal side in the oxygen recognition and stability of the Fe(II)-O2 complex of YddV, a globin-coupled heme-based oxygen sensor diguanylate cyclase. Biochemistry. 49: 10381-93. PMID 21067162 DOI: 10.1021/Bi100733Q |
0.313 |
|
| 2010 |
Kobayashi K, Tanaka A, Takahashi H, Igarashi J, Ishitsuka Y, Yokota N, Shimizu T. Catalysis and oxygen binding of Ec DOS: a haem-based oxygen-sensor enzyme from Escherichia coli. Journal of Biochemistry. 148: 693-703. PMID 20861024 DOI: 10.1093/Jb/Mvq103 |
0.366 |
|
| 2010 |
Giroud C, Moreau M, Sagami I, Shimizu T, Frapart Y, Mansuy D, Boucher JL. Comparison of wild type neuronal nitric oxide synthase and its Tyr588Phe mutant towards various l-arginine analogues Journal of Inorganic Biochemistry. 104: 1043-1050. PMID 20630600 DOI: 10.1016/J.Jinorgbio.2010.06.001 |
0.423 |
|
| 2010 |
Kitanishi K, Nakajima K, Ogura T, Igarashi J, Shimizu T. 2P111 Characterization of YddV, a heme-based oxygen sensor diguanylate cyclase enzyme : Catalytic and spectroscopic studies(The 48th Annual Meeting of the Biophysical Society of Japan) Seibutsu Butsuri. 50. DOI: 10.2142/Biophys.50.S101_5 |
0.317 |
|
| 2009 |
Ito S, Igarashi J, Shimizu T. The FG loop of a heme-based gas sensor enzyme, Ec DOS, functions in heme binding, autoxidation and catalysis. Journal of Inorganic Biochemistry. 103: 1380-5. PMID 19712978 DOI: 10.1016/j.jinorgbio.2009.07.012 |
0.312 |
|
| 2008 |
Tanaka A, Shimizu T. Ligand binding to the Fe(III)-protoporphyrin IX complex of phosphodiesterase from Escherichia coli (Ec DOS) markedly enhances catalysis of cyclic di-GMP: roles of Met95, Arg97, and Phe113 of the putative heme distal side in catalytic regulation and ligand binding. Biochemistry. 47: 13438-46. PMID 19053256 DOI: 10.1021/bi8012017 |
0.321 |
|
| 2008 |
Ishitsuka Y, Araki Y, Tanaka A, Igarashi J, Ito O, Shimizu T. Arg97 at the heme-distal side of the isolated heme-bound PAS domain of a heme-based oxygen sensor from Escherichia coli (Ec DOS) plays critical roles in autoxidation and binding to gases, particularly O2. Biochemistry. 47: 8874-84. PMID 18672892 DOI: 10.1021/Bi800248C |
0.422 |
|
| 2008 |
El-Mashtoly SF, Nakashima S, Tanaka A, Shimizu T, Kitagawa T. Roles of Arg-97 and Phe-113 in regulation of distal ligand binding to heme in the sensor domain of Ec DOS protein. Resonance Raman and mutation study. The Journal of Biological Chemistry. 283: 19000-10. PMID 18450754 DOI: 10.1074/Jbc.M801262200 |
0.412 |
|
| 2008 |
Igarashi J, Murase M, Iizuka A, Pichierri F, Martinkova M, Shimizu T. Elucidation of the heme binding site of heme-regulated eukaryotic initiation factor 2alpha kinase and the role of the regulatory motif in heme sensing by spectroscopic and catalytic studies of mutant proteins. The Journal of Biological Chemistry. 283: 18782-91. PMID 18450746 DOI: 10.1074/Jbc.M801400200 |
0.41 |
|
| 2008 |
Zakariassen H, Cederkvist FH, Harbitz E, Shimizu T, Lange R, Mayer B, Gorren AC, Andersson KK, Sørlie M. Thermodynamic analysis of L-arginine and N omega-hydroxy-L-arginine binding to nitric oxide synthase. Biochimica Et Biophysica Acta. 1784: 806-10. PMID 18371313 DOI: 10.1016/J.Bbapap.2008.02.016 |
0.32 |
|
| 2008 |
Igarashi J, Murase M, Iwashita J, Sasaki T, Shimizu T. O8. NO-induced activation of a heme-sensor, eIF2α kinase, in association with binding to cysteine and heme Nitric Oxide. 19: 21-22. DOI: 10.1016/J.Niox.2008.06.009 |
0.313 |
|
| 2007 |
Martinkova M, Igarashi J, Shimizu T. Eukaryotic initiation factor 2alpha kinase is a nitric oxide-responsive mercury sensor enzyme: potent inhibition of catalysis by the mercury cation and reversal by nitric oxide. Febs Letters. 581: 4109-14. PMID 17689536 DOI: 10.1016/J.Febslet.2007.07.055 |
0.326 |
|
| 2007 |
Hirai K, Martinkova M, Igarashi J, Saiful I, Yamauchi S, El-Mashtoly S, Kitagawa T, Shimizu T. Identification of Cys385 in the isolated kinase insertion domain of heme-regulated eIF2 alpha kinase (HRI) as the heme axial ligand by site-directed mutagenesis and spectral characterization. Journal of Inorganic Biochemistry. 101: 1172-9. PMID 17597215 DOI: 10.1016/J.Jinorgbio.2007.05.004 |
0.408 |
|
| 2007 |
El-Mashtoly SF, Takahashi H, Shimizu T, Kitagawa T. Ultraviolet resonance Raman evidence for utilization of the heme 6-propionate hydrogen-bond network in signal transmission from heme to protein in Ec DOS protein. Journal of the American Chemical Society. 129: 3556-63. PMID 17335280 DOI: 10.1021/Ja0669777 |
0.388 |
|
| 2007 |
Murase M, Hirai K, Miksanova M, Tanaka A, Igarashi J, Shimizu T. 3P089 Site-directed mutagenesis study to identify the heme binding site in a heme-regulated eukaryotic initiation factor 2α kinase, HRI(Hemeproteins,Poster Presentations) Seibutsu Butsuri. 47. DOI: 10.2142/Biophys.47.S225_2 |
0.337 |
|
| 2006 |
Miksanova M, Igarashi J, Minami M, Sagami I, Yamauchi S, Kurokawa H, Shimizu T. Characterization of heme-regulated eIF2alpha kinase: roles of the N-terminal domain in the oligomeric state, heme binding, catalysis, and inhibition. Biochemistry. 45: 9894-905. PMID 16893190 DOI: 10.1021/Bi060556K |
0.413 |
|
| 2006 |
Yokota N, Araki Y, Kurokawa H, Ito O, Igarashi J, Shimizu T. Critical roles of Leu99 and Leu115 at the heme distal side in auto-oxidation and the redox potential of a heme-regulated phosphodiesterase from Escherichia coli. The Febs Journal. 273: 1210-23. PMID 16519686 DOI: 10.1111/j.1742-4658.2006.05145.x |
0.333 |
|
| 2006 |
Hirai K, Miksanova M, Igarashi J, Shimizu T. 1P150 Spectroscopic Studies of the Putative Heme-binding Domain of Heme-regulated eIF2αKinase(5. Heme protein,Poster Session,Abstract,Meeting Program of EABS & BSJ 2006) Seibutsu Butsuri. 46. DOI: 10.2142/Biophys.46.S184_2 |
0.387 |
|
| 2006 |
Takahashi H, Shimizu T. Phosphodiesterase Activity of Ec DOS, a Heme-regulated Enzyme from Escherichia coli, toward 3′,5′-Cyclic Diguanylic Acid Is Obviously Enhanced by O2 and CO Binding Chemistry Letters. 35: 970-971. DOI: 10.1246/Cl.2006.970 |
0.359 |
|
| 2005 |
Yoshimura-Suzuki T, Sagami I, Yokota N, Kurokawa H, Shimizu T. DOS(Ec), a heme-regulated phosphodiesterase, plays an important role in the regulation of the cyclic AMP level in Escherichia coli. Journal of Bacteriology. 187: 6678-82. PMID 16166529 DOI: 10.1128/Jb.187.19.6678-6682.2005 |
0.316 |
|
| 2005 |
Sasakura Y, Kanda K, Yoshimura-Suzuki T, Matsui T, Fukuzono S, Shimizu T. Investigation of the relationship between protein-protein interaction and catalytic activity of a heme-regulated phosphodiesterase from Escherichia coli (Ec DOS) by protein microarray. Biochemistry. 44: 9598-605. PMID 16008345 DOI: 10.1021/Bi050406U |
0.395 |
|
| 2005 |
Uchida T, Sato E, Sato A, Sagami I, Shimizu T, Kitagawa T. CO-dependent activity-controlling mechanism of heme-containing CO-sensor protein, neuronal PAS domain protein 2. The Journal of Biological Chemistry. 280: 21358-68. PMID 15797872 DOI: 10.1074/jbc.M412350200 |
0.315 |
|
| 2005 |
El-Mashtoly S, Kurokawa H, Shimizu T, Kitagawa T. 3P083 Protein Conformational Changes in the EC DOS Protein upon Redox Change or Ligand Binding Probed by UV Resonance Raman Spectroscopy Seibutsu Butsuri. 45. DOI: 10.2142/Biophys.45.S224_3 |
0.34 |
|
| 2005 |
Kurokawa H, Suzuki-Yoshimura T, Sasakura Y, Watanabe M, Hirata S, Taguchi S, Igarashi J, Sagami I, Shimizu T. Structure and Function Relationships of a Redox-Sensor Protein, Heme-Regulated Phosphodiesterase Seibutsu Butsuri. 45: 84-89. DOI: 10.2142/Biophys.45.84 |
0.373 |
|
| 2005 |
Bengea SN, Araki Y, Ito O, Igarashi J, Kurokawa H, Shimizu T. Dual Effects of the Substrate and Pterins on the Kinetics of CO Binding to Neuronal Nitric Oxide Synthase: A Laser Flash Photolysis Study Chemistry Letters. 34: 752-753. DOI: 10.1246/Cl.2005.752 |
0.363 |
|
| 2004 |
Sato E, Sagami I, Uchida T, Sato A, Kitagawa T, Igarashi J, Shimizu T. SOUL in mouse eyes is a new hexameric heme-binding protein with characteristic optical absorption, resonance Raman spectral, and heme-binding properties. Biochemistry. 43: 14189-98. PMID 15518569 DOI: 10.1021/Bi048742I |
0.394 |
|
| 2004 |
Watanabe M, Kurokawa H, Yoshimura-Suzuki T, Sagami I, Shimizu T. Critical roles of Asp40 at the haem proximal side of haem-regulated phosphodiesterase from Escherichia coli in redox potential, auto-oxidation and catalytic control. European Journal of Biochemistry / Febs. 271: 3937-42. PMID 15373839 DOI: 10.1111/J.1432-1033.2004.04331.X |
0.419 |
|
| 2004 |
Bengea S, Araki Y, Ito O, Igarashi J, Sagami I, Shimizu T. Analysis of the kinetics of CO binding to neuronal nitric oxide synthase by flash photolysis: dual effects of substrates, inhibitors, and tetrahydrobiopterin. Journal of Inorganic Biochemistry. 98: 1210-6. PMID 15219987 DOI: 10.1016/J.Jinorgbio.2004.04.009 |
0.353 |
|
| 2004 |
Moreau M, Takahashi H, Sari MA, Boucher JL, Sagami I, Shimizu T, Mansuy D. Importance of valine 567 in substrate recognition and oxidation by neuronal nitric oxide synthase Journal of Inorganic Biochemistry. 98: 1200-1209. PMID 15219986 DOI: 10.1016/J.Jinorgbio.2004.03.015 |
0.406 |
|
| 2004 |
Kurokawa H, Lee DS, Watanabe M, Sagami I, Mikami B, Raman CS, Shimizu T. A redox-controlled molecular switch revealed by the crystal structure of a bacterial heme PAS sensor. The Journal of Biological Chemistry. 279: 20186-93. PMID 14982921 DOI: 10.1074/Jbc.M314199200 |
0.358 |
|
| 2004 |
Igarashi J, Sato A, Kitagawa T, Yoshimura T, Yamauchi S, Sagami I, Shimizu T. Activation of heme-regulated eukaryotic initiation factor 2alpha kinase by nitric oxide is induced by the formation of a five-coordinate NO-heme complex: optical absorption, electron spin resonance, and resonance raman spectral studies. The Journal of Biological Chemistry. 279: 15752-62. PMID 14752110 DOI: 10.1074/Jbc.M310273200 |
0.399 |
|
| 2004 |
Sato Y, Sagami I, Shimizu T. Identification of caveolin-1-interacting sites in neuronal nitric-oxide synthase. Molecular mechanism for inhibition of NO formation. The Journal of Biological Chemistry. 279: 8827-36. PMID 14681230 DOI: 10.1074/Jbc.M310327200 |
0.426 |
|
| 2004 |
Taguchi S, Matsui T, Igarashi J, Sasakura Y, Araki Y, Ito O, Sugiyama S, Sagami I, Shimizu T. Binding of oxygen and carbon monoxide to a heme-regulated phosphodiesterase from Escherichia coli. Kinetics and infrared spectra of the full-length wild-type enzyme, isolated PAS domain, and Met-95 mutants. The Journal of Biological Chemistry. 279: 3340-7. PMID 14612459 DOI: 10.1074/Jbc.M301013200 |
0.424 |
|
| 2004 |
Sagami I, Sato E, Uchida T, Sato A, Kitagawa T, Igarashi J, Shimizu T. 2P061 Characterization of SOUL in Mouse Eyes : Optical Absorption, Resonance Raman Spectral and Heme Binding Properties Seibutsu Butsuri. 44. DOI: 10.2142/Biophys.44.S125_1 |
0.302 |
|
| 2004 |
Hirata S, Kurokawa H, Sagami I, Shimizu T. Fluorescence Spectra of Trp53Phe and Trp110Ile Mutants of a Heme-regulated Phosphodiesterase from Escherichia coli Chemistry Letters. 33: 870-871. DOI: 10.1246/Cl.2004.870 |
0.334 |
|
| 2003 |
Hirata S, Matsui T, Sasakura Y, Sugiyama S, Yoshimura T, Sagami I, Shimizu T. Characterization of Met95 mutants of a heme-regulated phosphodiesterase from Escherichia coli. Optical absorption, magnetic circular dichroism, circular dichroism, and redox potentials. European Journal of Biochemistry / Febs. 270: 4771-9. PMID 14622266 DOI: 10.1046/J.1432-1033.2003.03879.X |
0.375 |
|
| 2003 |
Yoshimura T, Sagami I, Sasakura Y, Shimizu T. Relationships between heme incorporation, tetramer formation, and catalysis of a heme-regulated phosphodiesterase from Escherichia coli: a study of deletion and site-directed mutants. The Journal of Biological Chemistry. 278: 53105-11. PMID 14551206 DOI: 10.1074/Jbc.M304408200 |
0.429 |
|
| 2003 |
Sorlie M, Gorren AC, Marchal S, Shimizu T, Lange R, Andersson KK, Mayer B. Single-turnover of nitric-oxide synthase in the presence of 4-amino-tetrahydrobiopterin: proposed role for tetrahydrobiopterin as a proton donor. The Journal of Biological Chemistry. 278: 48602-10. PMID 14514694 DOI: 10.1074/Jbc.M305682200 |
0.407 |
|
| 2003 |
Igarashi J, Sato A, Kitagawa T, Sagami I, Shimizu T. CO binding study of mouse heme-regulated eIF-2α kinase: kinetics and resonance Raman spectra Biochimica Et Biophysica Acta. 1650: 99-104. PMID 12922173 DOI: 10.1016/S1570-9639(03)00205-X |
0.376 |
|
| 2003 |
Yadav J, Sagami I, Shimizu T. Cyanide binding study of neuronal nitric oxide synthase: effects of inhibitors and mutations at the substrate binding site. Journal of Inorganic Biochemistry. 95: 25-30. PMID 12706538 DOI: 10.1016/S0162-0134(03)00089-8 |
0.414 |
|
| 2003 |
Bengea S, Sagami I, Shimizu T. CO binding to the isolated oxygenase domain of neuronal nitric oxide synthase: effects of inhibitors and mutations at the substrate-binding site. Journal of Inorganic Biochemistry. 94: 343-347. PMID 12667705 DOI: 10.1016/S0162-0134(03)00026-6 |
0.416 |
|
| 2003 |
Takahashi H, Sato Y, Moreau M, Sari MA, Boucher JL, Mansuy D, Sagami I, Shimizu T. Critical Role of Val567 in Substrate Recognition by Neuronal Nitric Oxide Synthase for NO Formation Activity Chemistry Letters. 32: 998-999. DOI: 10.1246/Cl.2003.998 |
0.373 |
|
| 2003 |
Yoshimura T, Sagami I, Sasakura Y, Shimizu T. Relationships between tetramer formation, heme incorporation and catalysis of a heme-regulated phosphodiesterase from Escherichia coli: A study of deletion mutants Journal of Inorganic Biochemistry. 96: 257. DOI: 10.1016/S0162-0134(03)80812-7 |
0.341 |
|
| 2003 |
Igarashi J, Sagami I, Shimizu T, Sato A, Kitagawa T. CO binding study of mouse heme-regulated eIF-2a kinase: Kinetics and resonance Raman spectra Journal of Inorganic Biochemistry. 96: 156. DOI: 10.1016/S0162-0134(03)80654-2 |
0.311 |
|
| 2002 |
Watanabe M, Matsui T, Sasakura Y, Sagami I, Shimizu T. Unusual cyanide bindings to a heme-regulated phosphodiesterase from Escherichia coli: effect of Met95 mutations. Biochemical and Biophysical Research Communications. 299: 169-172. PMID 12437964 DOI: 10.1016/S0006-291X(02)02621-9 |
0.388 |
|
| 2002 |
Fuziwara S, Sagami I, Rozhkova E, Craig D, Noble MA, Munro AW, Chapman SK, Shimizu T. Catalytically functional flavocytochrome chimeras of P450 BM3 and nitric oxide synthase. Journal of Inorganic Biochemistry. 91: 515-26. PMID 12237219 DOI: 10.1016/S0162-0134(02)00478-6 |
0.623 |
|
| 2002 |
Sasakura Y, Hirata S, Sugiyama S, Suzuki S, Taguchi S, Watanabe M, Matsui T, Sagami I, Shimizu T. Characterization of a direct oxygen sensor heme protein from Escherichia coli. Effects of the heme redox states and mutations at the heme-binding site on catalysis and structure. Journal of Biological Chemistry. 277: 23821-23827. PMID 11970957 DOI: 10.1074/Jbc.M202738200 |
0.433 |
|
| 2002 |
Rozhkova EA, Fujimoto N, Sagami I, Daff SN, Shimizu T. Interactions between the isolated oxygenase and reductase domains of neuronal nitric-oxide synthase: assessing the role of calmodulin. The Journal of Biological Chemistry. 277: 16888-94. PMID 11884406 DOI: 10.1074/Jbc.M200642200 |
0.626 |
|
| 2002 |
Sagami I, Sato Y, Noguchi T, Miyajima M, Rozhkova E, Daff S, Shimizu T. Electron transfer in nitric-oxide synthase Coordination Chemistry Reviews. 226: 179-186. DOI: 10.1016/S0010-8545(01)00446-5 |
0.627 |
|
| 2001 |
Sato Y, Sagami I, Shimizu T. Critical role of the neuronal nitric-oxide synthase heme proximal side residue, Arg418, in catalysis and electron transfer Journal of Inorganic Biochemistry. 87: 261-266. PMID 11744064 DOI: 10.1016/S0162-0134(01)00334-8 |
0.429 |
|
| 2001 |
Kobayashi K, Tagawa S, Daff S, Sagami I, Shimizu T. Rapid Calmodulin-dependent Interdomain Electron Transfer in Neuronal Nitric-oxide Synthase Measured by Pulse Radiolysis Journal of Biological Chemistry. 276: 39864-39871. PMID 11518705 DOI: 10.1074/Jbc.M102537200 |
0.354 |
|
| 2001 |
Sagami I, Daff S, Shimizu T. Intra-subunit and inter-subunit electron transfer in neuronal nitric-oxide synthase: effect of calmodulin on heterodimer catalysis. Journal of Biological Chemistry. 276: 30036-30042. PMID 11395516 DOI: 10.1074/Jbc.M104123200 |
0.394 |
|
| 2001 |
Daff S, Noble MA, Craig DH, Rivers SL, Chapman SK, Munro AW, Fujiwara S, Rozhkova E, Sagami I, Shimizu T. Control of electron transfer in neuronal NO synthase. Biochemical Society Transactions. 29: 147-52. PMID 11356143 DOI: 10.1042/Bst0290147 |
0.647 |
|
| 2001 |
Noguchi T, Sagami I, Daff S, Shimizu T. Important Role of Tetrahydrobiopterin in NO Complex Formation and Interdomain Electron Transfer in Neuronal Nitric-Oxide Synthase Biochemical and Biophysical Research Communications. 282: 1092-1097. PMID 11302726 DOI: 10.1006/Bbrc.2001.4697 |
0.434 |
|
| 2001 |
Sato Y, Sagami I, Matsui T, Shimizu T. Unusual Role of Tyr588 of Neuronal Nitric Oxide Synthase in Controlling Substrate Specificity and Electron Transfer Biochemical and Biophysical Research Communications. 281: 621-626. PMID 11237702 DOI: 10.1006/Bbrc.2001.4356 |
0.394 |
|
| 2001 |
Sagami I, Sato Y, Noguchi T, Miyajima M, Shimizu T. Electron-Transfer Mechanisms of Nitric-Oxide Synthase. Seibutsu Butsuri. 41: 137-141. DOI: 10.2142/Biophys.41.137 |
0.41 |
|
| 2000 |
Yumoto T, Sagami I, Daff S, Shimizu T. Roles of the heme proximal side residues tryptophan409 and tryptophan421 of neuronal nitric oxide synthase in the electron transfer reaction. Journal of Inorganic Biochemistry. 82: 163-170. PMID 11132623 DOI: 10.1016/S0162-0134(00)00142-2 |
0.457 |
|
| 2000 |
Miyajima M, Sagami I, Daff S, Migita CT, Shimizu T. Azo reduction of methyl red by neuronal nitric oxide synthase: the important role of FMN in catalysis. Biochemical and Biophysical Research Communications. 275: 752-758. PMID 10973794 DOI: 10.1006/Bbrc.2000.3367 |
0.428 |
|
| 2000 |
Sagami I, Sato Y, Daff S, Shimizu T. Aromatic Residues and Neighboring Arg414 in the (6R)-5,6,7,8-Tetrahydro-l-Biopterin Binding Site of Full-length Neuronal Nitric-oxide Synthase Are Crucial in Catalysis and Heme Reduction with NADPH Journal of Biological Chemistry. 275: 26150-26157. PMID 10846172 DOI: 10.1074/Jbc.M000534200 |
0.433 |
|
| 1999 |
Noble MA, Munro AW, Rivers SL, Robledo L, Daff SN, Yellowlees LJ, Shimizu T, Sagami I, Guillemette JG, Chapman SK. Potentiometric analysis of the flavin cofactors of neuronal nitric oxide synthase. Biochemistry. 38: 16413-8. PMID 10600101 DOI: 10.1021/Bi992150W |
0.385 |
|
| 1999 |
Daff S, Sagami I, Shimizu T. The 42-Amino Acid Insert in the FMN Domain of Neuronal Nitric-oxide Synthase Exerts Control over Ca2+/Calmodulin-dependent Electron Transfer Journal of Biological Chemistry. 274: 30589-30595. PMID 10521442 DOI: 10.1074/Jbc.274.43.30589 |
0.384 |
|
| 1999 |
Shimanuki T, Sato H, Daff S, Sagami I, Shimizu T. Crucial Role of Lys423 in the Electron Transfer of Neuronal Nitric-oxide Synthase Journal of Biological Chemistry. 274: 26956-26961. PMID 10480907 DOI: 10.1074/Jbc.274.38.26956 |
0.446 |
|
| 1998 |
Sato H, Sagami I, Daff S, Shimizu T. Autoxidation Rates of Neuronal Nitric Oxide Synthase: Effects of the Substrates, Inhibitors, and Modulators Biochemical and Biophysical Research Communications. 253: 845-849. PMID 9918817 DOI: 10.1006/Bbrc.1998.9851 |
0.314 |
|
| 1998 |
Yanagita K, Sagami I, Daff S, Shimizu T. Marked Enhancement in the Reductive Dehalogenation of Hexachloroethane by a Thr319Ala Mutation of Cytochrome P450 1A2 Biochemical and Biophysical Research Communications. 249: 678-682. PMID 9731196 DOI: 10.1006/Bbrc.1998.9084 |
0.32 |
|
| 1998 |
Nakano K, Sagami I, Daff S, Shimizu T. Chiral Recognition At The Heme Active Site Of Nitric Oxide Synthase Is Markedly Enhanced By L-Arginine And 5,6,7,8-Tetrahydrobiopterin Biochemical and Biophysical Research Communications. 248: 767-772. PMID 9704002 DOI: 10.1006/Bbrc.1998.8893 |
0.36 |
|
| 1998 |
Sato H, Nomura S, Sagami I, Ito O, Daff S, Shimizu T. CO binding studies of nitric oxide synthase: effects of the substrate, inhibitors and tetrahydrobiopterin. Febs Letters. 430: 377-380. PMID 9688574 DOI: 10.1016/S0014-5793(98)00699-1 |
0.339 |
|
| 1998 |
Sagami I, Shimizu T. The Crucial Roles of Asp-314 and Thr-315 in the Catalytic Activation of Molecular Oxygen by Neuronal Nitric-oxide Synthase A SITE-DIRECTED MUTAGENESIS STUDY Journal of Biological Chemistry. 273: 2105-2108. PMID 9442050 DOI: 10.1074/Jbc.273.4.2105 |
0.45 |
|
| 1997 |
Shibata Y, Sato H, Sagami I, Shimizu T. Interaction of Angeli's salt with cytochrome P450 1A2 distal mutants: an optical absorption spectral study Biochimica Et Biophysica Acta. 1343: 67-75. PMID 9428660 DOI: 10.1016/S0167-4838(97)00104-0 |
0.375 |
|
| 1997 |
Yanagita K, Sagami I, Shimizu T. Distal site and surface mutations of cytochrome P450 1A2 markedly enhance dehalogenation of chlorinated hydrocarbons. Archives of Biochemistry and Biophysics. 346: 269-276. PMID 9343374 DOI: 10.1006/Abbi.1997.0301 |
0.376 |
|
| 1997 |
Sano H, Sato H, Sagami I, Shimizu T. Nitric Oxide Synthesis Capabilities Of Cytochrome P450 1A2 And Nadph-Cytochrome P450 Reductase From Ng-Hydroxy-L-Arginine Chemistry Letters. 1997: 759-760. DOI: 10.1246/Cl.1997.759 |
0.345 |
|
| 1997 |
Umeno M, Yanagita K, Sagami I, Shimizu T. Azo reduction catalyzed by cytochrome P450 1A2 and NADPH-cytochrome P450 reductase Journal of Inorganic Biochemistry. 67: 379. DOI: 10.1016/S0162-0134(97)80245-0 |
0.319 |
|
| 1996 |
Nakano R, Sato H, Shimizu T. Tris(2,2′-bipyridyl) ruthernium(II)-mediated photoinduced electron transfer of engineered cytochrome P450 1A2 Journal of Photochemistry and Photobiology B-Biology. 32: 171-176. PMID 8622181 DOI: 10.1016/1011-1344(95)07230-6 |
0.336 |
|
| 1996 |
Nakano R, Sato H, Watanabe A, Ito O, Shimizu T. Conserved Glu318 at the cytochrome P450 1A2 distal site is crucial in the nitric oxide complex stability. Journal of Biological Chemistry. 271: 8570-8574. PMID 8621484 DOI: 10.1074/Jbc.271.15.8570 |
0.412 |
|
| 1995 |
Nakano R, Konami H, Sato H, Ito O, Shimizu T. Marked detergents effects on safranine T-mediated photo-induced electron transfer in cytochrome P-450 1A2 Biochimica Et Biophysica Acta. 1252: 245-250. PMID 7578230 DOI: 10.1016/0167-4838(95)00143-I |
0.347 |
|
| 1995 |
Sato H, Shimizu T. Marked Effects of Alcohols and Imidazoles on the Cumyl Hydroperoxide Reaction with the Wild-Type Cytochrome-P450 1A2 Archives of Biochemistry and Biophysics. 322: 277-283. PMID 7574687 DOI: 10.1006/Abbi.1995.1463 |
0.306 |
|
| 1994 |
Mayuzumi H, Shimizu T, Sambongi C, Hiroya K, Hatano M. Essential Role Of His163 Of Cytochrome P450 1A2 In Catalytic Functions Associated With Cytochrome B5 Archives of Biochemistry and Biophysics. 310: 367-372. PMID 8179321 DOI: 10.1006/Abbi.1994.1180 |
0.372 |
|
| 1994 |
Hiroya K, Murakami Y, Shimizu T, Hatano M, Ortiz de Montellano PR. Differential roles of Glu318 and Thr319 in cytochrome P450 1A2 catalysis supported by NADPH-cytochrome P450 reductase and tert-butyl hydroperoxide. Archives of Biochemistry and Biophysics. 310: 397-401. PMID 7910007 DOI: 10.1006/Abbi.1994.1184 |
0.395 |
|
| 1994 |
Sato H, Shimizu T, Murakami Y, Hatano M. Remarkable enhancement of 7-ethoxycoumarin O-deethylation by Lys250, Arg251 and Lys253 mutations of cytochrome P450 1A2 Chemistry Letters. 1994: 311-314. DOI: 10.1246/Cl.1994.311 |
0.344 |
|
| 1993 |
Mayuzumi H, Sambongi C, Hiroya K, Shimizu T, Tateishi T, Hatano M. Effect of mutations of ionic amino acids of cytochrome P450 1A2 on catalytic activities toward 7-ethoxycoumarin and methanol. Biochemistry. 32: 5622-5628. PMID 8504082 DOI: 10.1021/Bi00072A018 |
0.389 |
|
| 1993 |
Krainev AG, Shimizu T, Ishigooka M, Hiroya K, Hatano M. Chiral recognition at cytochrome P450 1A2 active site: effects of mutations at the putative distal site on the bindings of asymmetrical axial ligands. Biochemistry. 32: 1951-1957. PMID 8448154 DOI: 10.1021/Bi00059A011 |
0.31 |
|
| 1993 |
Tuck SF, Hiroya K, Shimizu T, Hatano M, Ortiz de Montellano PR. The cytochrome P450 1A2 active site: topology and perturbations caused by glutamic acid-318 and threonine-319 mutations. Biochemistry. 32: 2548-53. PMID 8095402 DOI: 10.1021/Bi00061A012 |
0.365 |
|
| 1992 |
Krainev AG, Shimizu T, Hiroya K, Hatano M. Effect of mutations at Lys250, Arg251, and Lys253 of cytochrome P450 1A2 on the catalytic activities and the bindings of bifunctional axial ligands. Archives of Biochemistry and Biophysics. 298: 198-203. PMID 1524428 DOI: 10.1016/0003-9861(92)90113-B |
0.415 |
|
| 1992 |
Hiroya K, Ishigooka M, Shimizu T, Hatano M. Role of Glu318 and Thr319 in the catalytic function of cytochrome P450d (P4501A2): effects of mutations on the methanol hydroxylation. The Faseb Journal. 6: 749-751. PMID 1347023 DOI: 10.1096/Fasebj.6.2.1347023 |
0.335 |
|
| 1992 |
Ishigooka M, Shimizu T, Hiroya K, Hatano M. Role of Glu318 at the putative distal site in the catalytic function of cytochrome P450d. Biochemistry. 31: 1528-1531. PMID 1346571 DOI: 10.1021/Bi00120A033 |
0.364 |
|
| 1991 |
Shimizu T, Ito O, Hatano M, Fujii-Kuriyama Y. CO binding studies of engineered cytochrome P-450ds: effects of mutations at putative distal sites in the presence of polycyclic hydrocarbons. Biochemistry. 30: 4659-4662. PMID 2029514 DOI: 10.1021/Bi00233A004 |
0.382 |
|
| 1991 |
Shimizu T, Sadeque AJM, Sadeque GN, Hatano M, Fujii-Kuriyama Y. Ligand binding studies of engineered cytochrome P-450d wild type, proximal mutants, and distal mutants. Biochemistry. 30: 1490-1496. PMID 1993167 DOI: 10.1021/Bi00220A007 |
0.391 |
|
| 1991 |
Krainev AG, Shimizu T, Ishigooka M, Hiroya K, Hatano M, Fujii-Kuriyama Y. Absorption spectral study of cytochrome P450d-phenyl isocyanide complexes: effects of mutations at the putative distal site on the conformational stability. Biochemistry. 30: 11206-11211. PMID 1958658 DOI: 10.1021/Bi00111A003 |
0.34 |
|
| 1991 |
Hiroya K, Shimizu T, Hatano M, Fujii-Kuriyama Y. Remarkable Changes in Catalytic Activity toward Testosterone of Engineered Cytochrome P-450d by Mutations at Putative Distal Site Chemistry Letters. 20: 973-976. DOI: 10.1246/Cl.1991.973 |
0.338 |
|
| 1990 |
Furuya H, Shimizu T, Hirano K, Hatano M, Fujii-Kuriyama Y, Raag R, Poulos TL. Site-directed mutageneses of rat liver cytochrome P-450d: catalytic activities toward benzphetamine and 7-ethoxycoumarin. Biochemistry. 28: 6848-57. PMID 2819037 DOI: 10.1021/Bi00443A011 |
0.379 |
|
| 1990 |
Ogoma Y, Kobayashi H, Fujii T, Kondo Y, Hachimori A, Shimizu T, Hatano M. 19F-n.m.r. study of trifluoperazine-S100 protein interaction: effects of Ca2+ and Zn2+. International Journal of Biological Macromolecules. 12: 185-188. PMID 2271488 DOI: 10.1016/0141-8130(90)90030-E |
0.31 |
|
| 1990 |
Sotokawa H, Shimizu T, Furuya H, Sadeque AJM, Hatano M, Ohba Y, Iwaizumi M, Fujii-Kuriyama Y. Electron spin resonance studies of wild-type and mutant cytochromes P-450d: effects of mutations at proximal, aromatic and distal sites on g values. Biochimica Et Biophysica Acta. 1037: 122-128. PMID 2153026 DOI: 10.1016/0167-4838(90)90110-2 |
0.365 |
|
| 1989 |
Furuya H, Shimizu T, Hatano M, Fujii-Kuriyama Y. Mutations at the distal and proximal sites of cytochrome P-450d changed regio-specificity of acetanilide hydroxylations Biochemical and Biophysical Research Communications. 160: 669-676. PMID 2719689 DOI: 10.1016/0006-291X(89)92485-6 |
0.381 |
|
| 1989 |
Shimizu T, Sadeque AJM, Hatano M, Fujii-Kuriyama Y. Bindings of axial ligands to cytochrome P-450d mutants: a difference absorption spectral study. Biochimica Et Biophysica Acta. 995: 116-121. PMID 2649155 DOI: 10.1016/0167-4838(89)90069-1 |
0.351 |
|
| 1988 |
Shimizu T, Hatano M. 43Ca nuclear magnetic resonance of Ca2+–calmodulin solutions: Effects of trifluoperazine and peptides Inorganica Chimica Acta. 152: 257-260. DOI: 10.1016/S0020-1693(00)91478-6 |
0.312 |
|
| 1988 |
Sadeque AJ, Shimizu T, Hirano K, Hatano M, Fujii-Kuriyama Y. Interaction of fluoroaniline with cytochrome P-450d mutants: Difference absorption spectral studies Inorganica Chimica Acta. 153: 161-164. DOI: 10.1016/S0020-1693(00)86308-2 |
0.391 |
|
| 1988 |
Sadeque AJM, Shimizu T, Hatano M. Interaction of fluoroaniline with cytochrome P-450scc and myoglobin: temperature and pH dependence studies Inorganica Chimica Acta. 151: 49-54. DOI: 10.1016/S0020-1693(00)83483-0 |
0.336 |
|
| 1987 |
Sakurada J, Takahashi S, Shimizu T, Hatano M, Nakamura S, Hosoya T. Proton and iodine-127 nuclear magnetic resonance studies on the binding of iodide by lactoperoxidase. Biochemistry. 26: 6478-6483. PMID 2827729 DOI: 10.1021/Bi00394A028 |
0.328 |
|
| 1987 |
Sadeque AJM, Shimizu T, Hatano M. Thiol-coordinated heme octapeptides of cytochrome c; Model compounds of cytochrome P-450 Inorganica Chimica Acta. 135: 109-113. DOI: 10.1016/S0020-1693(00)83272-7 |
0.346 |
|
| 1985 |
Sakurada J, Hosoya T, Shimizu T, Hatano M. 127I Nuclear Magnetic Resonance Studies On The Interaction Of Iodide Ion With Horseradish Peroxidase Chemistry Letters. 14: 211-214. DOI: 10.1246/Cl.1985.211 |
0.303 |
|
| 1985 |
Shimizu T, Sotokawa H, Hatano M. 1H nuclear magnetic resonance and magnetic circular dichroism studies of ferric low-spin cytochrome P-450scc Inorganica Chimica Acta. 108: 195-199. DOI: 10.1016/S0020-1693(00)84539-9 |
0.321 |
|
| 1985 |
Sotokawa H, Shimizu T, Hatano M. Interaction of naphthalene-d8 with cytochromes P-450: a 2H nuclear magnetic resonance study Inorganica Chimica Acta. 108: 67-70. DOI: 10.1016/S0020-1693(00)84326-1 |
0.353 |
|
| 1982 |
Shimizu T, Nozawa T, Hatano M. Deuterium nuclear magnetic resonance spectroscopy of deuterated pyridine-iron(III) porphyrin complexes. Locations and relaxation times of bound deuterated pyridine resonances. Journal of Biochemistry. 91: 1951-1958. PMID 7118856 DOI: 10.1093/Oxfordjournals.Jbchem.A133889 |
0.303 |
|
| 1982 |
Shimizu T, Kodaka M, Hatano M. 67Zn and 1H NMR studies of Zn2+-imidazole and carboxylate complexes. Biochemical and Biophysical Research Communications. 106: 988-993. PMID 7115389 DOI: 10.1016/0006-291X(82)91808-3 |
0.302 |
|
| 1982 |
Shimizu T, Hatano M. 43Ca and 67Zn NMR study of Ca2+, Zn2+-thermolysin complexes Biochemical and Biophysical Research Communications. 104: 1356-1362. PMID 7073747 DOI: 10.1016/0006-291X(82)91399-7 |
0.317 |
|
| 1979 |
Shimizu T, Nozawa T, Hatano M, Satake H, Imai Y, Hashimoto C, Sato R. Circular dichroism spectra of purified cytochromes P-450 from rabbit liver microsomes Biochimica Et Biophysica Acta. 579: 122-133. PMID 465524 DOI: 10.1016/0005-2795(79)90092-8 |
0.3 |
|
| 1978 |
Nozawa T, Shimizu T, Hatano M, Shimada H, Iizuka T, Ishimura Y. Magnetic circular dichroism of Pseudomonas putida cytochrome P-450 in near infrared region. Biochimica Et Biophysica Acta. 534: 285-294. PMID 667105 DOI: 10.1016/0005-2795(78)90011-9 |
0.335 |
|
| 1976 |
Shimizu T, Nozawa T, Hatano M. Magnetic circular dichroism of heme-isocyanide complex in aqueous media. Bioinorganic Chemistry. 6: 1-9. PMID 953042 DOI: 10.1016/S0006-3061(00)80046-0 |
0.311 |
|
| 1976 |
Shimizu T, Nozawa T, Hatano M. Magnetic circular dichroism of myoglobin-thiolate complexes Biochimica Et Biophysica Acta. 434: 126-136. PMID 7306 DOI: 10.1016/0005-2795(76)90042-8 |
0.307 |
|
| 1975 |
Shimizu T, Nozawa T, Hatano M, Imai Y, Sato R. Magnetic circular dichroism studies of hepatic microsomal cytochrome P-450. Biochemistry. 14: 4172-4178. PMID 1182096 DOI: 10.1021/Bi00690A004 |
0.346 |
|
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