| Year |
Citation |
Score |
| 2020 |
Takahashi S, Nambu S, Matsui T, Fujii H, Ishikawa H, Mizutani Y, Tsumoto K, Ikeda-Saito M. Unique Electronic Structures of the Highly Ruffled Hemes in Heme-Degrading Enzymes of , IsdG and IsdI, by Resonance Raman and Electron Paramagnetic Resonance Spectroscopies. Biochemistry. 59: 3918-3928. PMID 32988197 DOI: 10.1021/acs.biochem.0c00731 |
0.364 |
|
| 2018 |
Matsui T, Sugiyama R, Sakanashi K, Tamura Y, Iida M, Nambu Y, Higuchi T, Suematsu M, Ikeda-Saito M. Hydrogen sulfide bypasses the rate-limiting oxygen activation of heme oxygenase. The Journal of Biological Chemistry. PMID 30237172 DOI: 10.1074/Jbc.Ra118.004641 |
0.465 |
|
| 2018 |
Ikeda-Saito M, Matsui T. Heme degradation in Mycobacterium tuberculosis Free Radical Biology and Medicine. 120. DOI: 10.1016/J.Freeradbiomed.2018.04.048 |
0.43 |
|
| 2017 |
Chen M, Asai SI, Narai S, Nambu S, Omura N, Sakaguchi Y, Suzuki T, Ikeda-Saito M, Watanabe K, Yao M, Shigi N, Tanaka Y. Biochemical and structural characterization of oxygen-sensitive 2-thiouridine synthesis catalyzed by an iron-sulfur protein TtuA. Proceedings of the National Academy of Sciences of the United States of America. PMID 28439027 DOI: 10.1073/Pnas.1615585114 |
0.388 |
|
| 2016 |
Bacchi M, Veinberg E, Field MJ, Niklas J, Matsui T, Tiede DM, Poluektov OG, Ikeda-Saito M, Fontecave M, Artero V. Artificial Hydrogenases Based on Cobaloximes and Heme Oxygenase. Chempluschem. 81: 1083-1089. PMID 31964078 DOI: 10.1002/Cplu.201600218 |
0.403 |
|
| 2016 |
Suenaga T, Watanabe-Matsui M, Uejima T, Shima H, Matsui T, Ikeda-Saito M, Shirouzu M, Igarashi K, Murayama K. Charge-state-distribution analysis of Bach2 intrinsically disordered heme binding region. Journal of Biochemistry. PMID 27206783 DOI: 10.1093/Jb/Mvw035 |
0.354 |
|
| 2016 |
Matsui T, Nambu S, Goulding CW, Takahashi S, Fujii H, Ikeda-Saito M. Unique coupling of mono- and dioxygenase chemistries in a single active site promotes heme degradation. Proceedings of the National Academy of Sciences of the United States of America. PMID 27006503 DOI: 10.1073/Pnas.1523333113 |
0.429 |
|
| 2016 |
Kitatsuji C, Izumi K, Nambu S, Kurogochi M, Uchida T, Nishimura S, Iwai K, O'Brian MR, Ikeda-Saito M, Ishimori K. Protein oxidation mediated by heme-induced active site conversion specific for heme-regulated transcription factor, iron response regulator. Scientific Reports. 6: 18703. PMID 26729068 DOI: 10.1038/Srep18703 |
0.457 |
|
| 2015 |
Watanabe-Matsui M, Matsumoto T, Matsui T, Ikeda-Saito M, Muto A, Murayama K, Igarashi K. Heme binds to an intrinsically disordered region of Bach2 and alters its conformation. Archives of Biochemistry and Biophysics. 565: 25-31. PMID 25444856 DOI: 10.1016/J.Abb.2014.11.005 |
0.345 |
|
| 2014 |
Wilks A, Ikeda-Saito M. Heme utilization by pathogenic bacteria: not all pathways lead to biliverdin. Accounts of Chemical Research. 47: 2291-8. PMID 24873177 DOI: 10.1021/Ar500028N |
0.462 |
|
| 2014 |
Matsui T, Nambu S, Ikeda-Saito M. 1P095 Unique reaction mechanism of MhuD, a heme-degrading enzyme from Mycobacterial tuberculosis(02. Heme proteins,Poster,The 52nd Annual Meeting of the Biophysical Society of Japan(BSJ2014)) Seibutsu Butsuri. 54. DOI: 10.2142/Biophys.54.S156_5 |
0.334 |
|
| 2013 |
Unno M, Ardèvol A, Rovira C, Ikeda-Saito M. Structures of the substrate-free and product-bound forms of HmuO, a heme oxygenase from corynebacterium diphtheriae: x-ray crystallography and molecular dynamics investigation. The Journal of Biological Chemistry. 288: 34443-58. PMID 24106279 DOI: 10.1074/Jbc.M113.486936 |
0.48 |
|
| 2013 |
Matsui T, Nambu S, Ono Y, Goulding CW, Tsumoto K, Ikeda-Saito M. Heme degradation by Staphylococcus aureus IsdG and IsdI liberates formaldehyde rather than carbon monoxide. Biochemistry. 52: 3025-7. PMID 23600533 DOI: 10.1021/Bi400382P |
0.38 |
|
| 2013 |
Nambu S, Matsui T, Goulding CW, Takahashi S, Ikeda-Saito M. A new way to degrade heme: the Mycobacterium tuberculosis enzyme MhuD catalyzes heme degradation without generating CO. The Journal of Biological Chemistry. 288: 10101-9. PMID 23420845 DOI: 10.1074/Jbc.M112.448399 |
0.415 |
|
| 2012 |
Unno M, Matsui T, Ikeda-Saito M. Crystallographic studies of heme oxygenase complexed with an unstable reaction intermediate, verdoheme. Journal of Inorganic Biochemistry. 113: 102-9. PMID 22673156 DOI: 10.1016/J.Jinorgbio.2012.04.012 |
0.398 |
|
| 2012 |
Uchida T, Sekine Y, Matsui T, Ikeda-Saito M, Ishimori K. A heme degradation enzyme, HutZ, from Vibrio cholerae. Chemical Communications (Cambridge, England). 48: 6741-3. PMID 22627893 DOI: 10.1039/C2Cc31147J |
0.436 |
|
| 2011 |
Unno M, Shinohara M, Takayama K, Tanaka H, Teruya K, Doh-ura K, Sakai R, Sasaki M, Ikeda-Saito M. Binding and selectivity of the marine toxin neodysiherbaine A and its synthetic analogues to GluK1 and GluK2 kainate receptors. Journal of Molecular Biology. 413: 667-83. PMID 21893069 DOI: 10.1016/J.Jmb.2011.08.043 |
0.329 |
|
| 2010 |
Lai W, Chen H, Matsui T, Omori K, Unno M, Ikeda-Saito M, Shaik S. Enzymatic ring-opening mechanism of verdoheme by the heme oxygenase: a combined X-ray crystallography and QM/MM study. Journal of the American Chemical Society. 132: 12960-70. PMID 20806922 DOI: 10.1021/Ja104674Q |
0.443 |
|
| 2010 |
Du Z, Unno M, Matsui T, Ikeda-Saito M, La Mar GN. Solution 1H NMR characterization of substrate-free C. diphtheriae heme oxygenase: pertinence for determining magnetic axes in paramagnetic substrate complexes. Journal of Inorganic Biochemistry. 104: 1063-70. PMID 20655112 DOI: 10.1016/J.Jinorgbio.2010.06.003 |
0.397 |
|
| 2010 |
Matsui T, Iwasaki M, Sugiyama R, Unno M, Ikeda-Saito M. Dioxygen activation for the self-degradation of heme: reaction mechanism and regulation of heme oxygenase. Inorganic Chemistry. 49: 3602-9. PMID 20380462 DOI: 10.1021/Ic901869T |
0.463 |
|
| 2010 |
Matsui T, Unno M, Ikeda-Saito M. Heme oxygenase reveals its strategy for catalyzing three successive oxygenation reactions. Accounts of Chemical Research. 43: 240-7. PMID 19827796 DOI: 10.1021/Ar9001685 |
0.485 |
|
| 2010 |
Matsui T, Unno M, Ikeda-Saito M. 3P104 Ring Opening Mechanism of Verdoheme Catalyzed by Heme Oxygenase(Heme proteins,The 48th Annual Meeting of the Biophysical Society of Japan) Seibutsu Butsuri. 50. DOI: 10.2142/Biophys.50.S163_1 |
0.301 |
|
| 2009 |
Ito Y, Nakagawa S, Komagata A, Ikeda-Saito M, Shiro Y, Nakamura H. Heme-dependent autophosphorylation of a heme sensor kinase, ChrS, from Corynebacterium diphtheriae reconstituted in proteoliposomes. Febs Letters. 583: 2244-8. PMID 19505463 DOI: 10.1016/J.Febslet.2009.06.001 |
0.333 |
|
| 2008 |
Chen H, Ikeda-Saito M, Shaik S. Nature of the Fe-O2 bonding in oxy-myoglobin: effect of the protein. Journal of the American Chemical Society. 130: 14778-90. PMID 18847206 DOI: 10.1021/Ja805434M |
0.418 |
|
| 2008 |
Matsui T, Omori K, Jin H, Ikeda-Saito M. Alkyl peroxides reveal the ring opening mechanism of verdoheme catalyzed by heme oxygenase. Journal of the American Chemical Society. 130: 4220-1. PMID 18331037 DOI: 10.1021/Ja710495Z |
0.44 |
|
| 2008 |
Yokoi N, Ueno T, Unno M, Matsui T, Ikeda-Saito M, Watanabe Y. Ligand design for the improvement of stability of metal complex.protein hybrids. Chemical Communications (Cambridge, England). 229-31. PMID 18092096 DOI: 10.1039/B713468A |
0.345 |
|
| 2007 |
Unno M, Chen H, Kusama S, Shaik S, Ikeda-Saito M. Structural characterization of the fleeting ferric peroxo species in myoglobin: experiment and theory. Journal of the American Chemical Society. 129: 13394-5. PMID 17929929 DOI: 10.1021/Ja076108X |
0.301 |
|
| 2007 |
Hira S, Tomita T, Matsui T, Igarashi K, Ikeda-Saito M. Bach1, a heme-dependent transcription factor, reveals presence of multiple heme binding sites with distinct coordination structure. Iubmb Life. 59: 542-51. PMID 17701549 DOI: 10.1080/15216540701225941 |
0.401 |
|
| 2007 |
Unno M, Matsui T, Ikeda-Saito M. Structure and catalytic mechanism of heme oxygenase. Natural Product Reports. 24: 553-70. PMID 17534530 DOI: 10.1039/B604180A |
0.487 |
|
| 2007 |
Garcia-Serres R, Davydov RM, Matsui T, Ikeda-Saito M, Hoffman BM, Huynh BH. Distinct reaction pathways followed upon reduction of oxy-heme oxygenase and oxy-myoglobin as characterized by Mössbauer spectroscopy. Journal of the American Chemical Society. 129: 1402-12. PMID 17263425 DOI: 10.1021/Ja067209I |
0.473 |
|
| 2007 |
Ikeda-Saito M, Unno M, Matsui T. S14I3 Substrate and product interactions with heme oxygenase and their implication for the heme degradation activity(Protein-Ligand Interactions) Biophysics. 47. DOI: 10.2142/Biophys.47.S20_3 |
0.316 |
|
| 2007 |
Garcia-Serres R, Davydov RM, Matsui T, Ikeda-Saito M, Hoffman aBM, Huynh BH. Distinct Reaction Pathways Followed upon Reduction of Oxy-Heme Oxygenase and Oxy-Myoglobin as Characterized by Mössbauer Spectroscopy [J. Am. Chem. Soc. 2007, 129, 1402−1412]. Journal of the American Chemical Society. 129: 6662-6662. DOI: 10.1021/Ja0724285 |
0.322 |
|
| 2006 |
Ueno T, Yokoi N, Unno M, Matsui T, Tokita Y, Yamada M, Ikeda-Saito M, Nakajima H, Watanabe Y. Design of metal cofactors activated by a protein-protein electron transfer system. Proceedings of the National Academy of Sciences of the United States of America. 103: 9416-21. PMID 16769893 DOI: 10.1073/Pnas.0510968103 |
0.384 |
|
| 2006 |
Matsui T, Kim SH, Jin H, Hoffman BM, Ikeda-Saito M. Compound I of heme oxygenase cannot hydroxylate its heme meso-carbon. Journal of the American Chemical Society. 128: 1090-1. PMID 16433521 DOI: 10.1021/Ja057578Z |
0.393 |
|
| 2006 |
Unno M, Ikeda-Saito M. 1P158 Crystal structure of the heme oxygenase complexed with α-meso hydroxyheme, a high reactive intermediate(5. Heme protein,Poster Session,Abstract,Meeting Program of EABS & BSJ 2006) Seibutsu Butsuri. 46. DOI: 10.2142/Biophys.46.S186_2 |
0.338 |
|
| 2005 |
Matsui T, Nakajima A, Fujii H, Matera KM, Migita CT, Yoshida T, Ikeda-Saito M. O(2)- and H(2)O(2)-dependent verdoheme degradation by heme oxygenase: reaction mechanisms and potential physiological roles of the dual pathway degradation. The Journal of Biological Chemistry. 280: 36833-40. PMID 16115896 DOI: 10.1074/Jbc.M503529200 |
0.479 |
|
| 2005 |
Matsui T, Furukawa M, Unno M, Tomita T, Ikeda-Saito M. Roles of distal Asp in heme oxygenase from Corynebacterium diphtheriae, HmuO: A water-driven oxygen activation mechanism. The Journal of Biological Chemistry. 280: 2981-9. PMID 15528205 DOI: 10.1074/Jbc.M410263200 |
0.42 |
|
| 2004 |
Bulteau AL, O'Neill HA, Kennedy MC, Ikeda-Saito M, Isaya G, Szweda LI. Frataxin acts as an iron chaperone protein to modulate mitochondrial aconitase activity. Science (New York, N.Y.). 305: 242-5. PMID 15247478 DOI: 10.1126/Science.1098991 |
0.377 |
|
| 2004 |
Unno M, Matsui T, Chu GC, Couture M, Yoshida T, Rousseau DL, Olson JS, Ikeda-Saito M. Crystal structure of the dioxygen-bound heme oxygenase from Corynebacterium diphtheriae: implications for heme oxygenase function. The Journal of Biological Chemistry. 279: 21055-61. PMID 14966119 DOI: 10.1074/Jbc.M400491200 |
0.694 |
|
| 2004 |
Hirotsu S, Chu GC, Unno M, Lee DS, Yoshida T, Park SY, Shiro Y, Ikeda-Saito M. The crystal structures of the ferric and ferrous forms of the heme complex of HmuO, a heme oxygenase of Corynebacterium diphtheriae. The Journal of Biological Chemistry. 279: 11937-47. PMID 14645223 DOI: 10.1074/Jbc.M311631200 |
0.71 |
|
| 2003 |
Davydov R, Matsui T, Fujii H, Ikeda-Saito M, Hoffman BM. Kinetic isotope effects on the rate-limiting step of heme oxygenase catalysis indicate concerted proton transfer/heme hydroxylation. Journal of the American Chemical Society. 125: 16208-9. PMID 14692760 DOI: 10.1021/Ja038923S |
0.445 |
|
| 2003 |
Bulteau AL, Ikeda-Saito M, Szweda LI. Redox-dependent modulation of aconitase activity in intact mitochondria. Biochemistry. 42: 14846-55. PMID 14674759 DOI: 10.1021/Bi0353979 |
0.417 |
|
| 2003 |
Zhang X, Fujii H, Matera KM, Migita CT, Sun D, Sato M, Ikeda-Saito M, Yoshida T. Stereoselectivity of each of the three steps of the heme oxygenase reaction: hemin to meso-hydroxyhemin, meso-hydroxyhemin to verdoheme, and verdoheme to biliverdin. Biochemistry. 42: 7418-26. PMID 12809497 DOI: 10.1021/Bi027173G |
0.382 |
|
| 2003 |
Coyle CM, Vogel KM, Rush TS, Kozlowski PM, Williams R, Spiro TG, Dou Y, Ikeda-Saito M, Olson JS, Zgierski MZ. FeNO structure in distal pocket mutants of myoglobin based on resonance Raman spectroscopy. Biochemistry. 42: 4896-903. PMID 12718530 DOI: 10.1021/Bi026395B |
0.392 |
|
| 2003 |
Voegtle HL, Sono M, Adak S, Pond AE, Tomita T, Perera R, Goodin DB, Ikeda-Saito M, Stuehr DJ, Dawson JH. Spectroscopic characterization of five- and six-coordinate ferrous-NO heme complexes. Evidence for heme Fe-proximal cysteinate bond cleavage in the ferrous-NO adducts of the Trp-409Tyr/Phe proximal environment mutants of neuronal nitric oxide synthase. Biochemistry. 42: 2475-84. PMID 12600215 DOI: 10.1021/Bi0271502 |
0.455 |
|
| 2003 |
Li Y, Syvitski RT, Chu GC, Ikeda-Saito M, La Mar GN. Solution 1H NMR investigation of the active site molecular and electronic structures of substrate-bound, cyanide-inhibited HmuO, a bacterial heme oxygenase from Corynebacterium diphtheriae Journal of Biological Chemistry. 278: 6651-6663. PMID 12480929 DOI: 10.1074/Jbc.M211249200 |
0.654 |
|
| 2002 |
Denisov IG, Ikeda-Saito M, Yoshida T, Sligar SG. Cryogenic absorption spectra of hydroperoxo-ferric heme oxygenase, the active intermediate of enzymatic heme oxygenation. Febs Letters. 532: 203-6. PMID 12459490 DOI: 10.1016/S0014-5793(02)03674-8 |
0.407 |
|
| 2002 |
Gonzalez G, Dioum EM, Bertolucci CM, Tomita T, Ikeda-Saito M, Cheesman MR, Watmough NJ, Gilles-Gonzalez MA. Nature of the displaceable heme-axial residue in the EcDos protein, a heme-based sensor from Escherichia coli. Biochemistry. 41: 8414-21. PMID 12081490 DOI: 10.1021/Bi025845X |
0.435 |
|
| 2002 |
Tomita T, Gonzalez G, Chang AL, Ikeda-Saito M, Gilles-Gonzalez MA. A comparative resonance Raman analysis of heme-binding PAS domains: heme iron coordination structures of the BjFixL, AxPDEA1, EcDos, and MtDos proteins. Biochemistry. 41: 4819-26. PMID 11939776 DOI: 10.1021/Bi0158831 |
0.449 |
|
| 2002 |
Davydov R, Kofman V, Fujii H, Yoshida T, Ikeda-Saito M, Hoffman BM. Catalytic mechanism of heme oxygenase through EPR and ENDOR of cryoreduced oxy-heme oxygenase and its Asp 140 mutants. Journal of the American Chemical Society. 124: 1798-808. PMID 11853459 DOI: 10.1021/Ja0122391 |
0.459 |
|
| 2001 |
Tomita T, Haruta N, Aki M, Kitagawa T, Ikeda-Saito M. UV resonance raman detection of a ligand vibration on ferric nitrosyl heme proteins Journal of the American Chemical Society. 123: 2666-2667. PMID 11456938 DOI: 10.1021/Ja001431K |
0.335 |
|
| 2001 |
Fujii H, Zhang X, Tomita T, Ikeda-Saito M, Yoshida T. A role for highly conserved carboxylate, aspartate-140, in oxygen activation and heme degradation by heme oxygenase-1 Journal of the American Chemical Society. 123: 6475-6484. PMID 11439033 DOI: 10.1021/ja010490a |
0.358 |
|
| 2001 |
Lesnefsky EJ, Gudz TI, Migita CT, Ikeda-Saito M, Hassan OM, Turkaly PJ, Hoppel CL. Ischemic injury to mitochondrial electron transport in the aging heart: Damage to the iron-sulfur protein subunit of electron transport complex III Archives of Biochemistry and Biophysics. 385: 117-128. PMID 11361007 DOI: 10.1006/Abbi.2000.2066 |
0.323 |
|
| 2001 |
Lesnefsky EJ, Gudz TI, Moghaddas S, Migita CT, Ikeda-Saito M, Turkaly PJ, Hoppel CL. Aging decreases electron transport complex III activity in heart interfibrillar mitochondria by alteration of the cytochrome c binding site Journal of Molecular and Cellular Cardiology. 33: 37-47. PMID 11133221 DOI: 10.1006/Jmcc.2000.1273 |
0.322 |
|
| 2000 |
Hori H, Masuya F, Dou Y, Ikeda-Saito M. EPR studies on the photoinduced intermediates of NO complexes in recombinant ferric-Mb trapped at low temperatures Journal of Inorganic Biochemistry. 82: 181-187. PMID 11132625 DOI: 10.1016/S0162-0134(00)00143-4 |
0.365 |
|
| 2000 |
Chu GC, Katakura K, Tomita T, Zhang X, Sun D, Sato M, Sasahara M, Kayama T, Ikeda-Saito M, Yoshida T. Histidine 20, the crucial proximal axial heme ligand of bacterial heme oxygenase Hmu O from Corynebacterium diphtheriae. The Journal of Biological Chemistry. 275: 17494-500. PMID 10751393 DOI: 10.1074/Jbc.M000830200 |
0.697 |
|
| 2000 |
Chu GC, Couture M, Yoshida T, Rousseau DL, Ikeda-Saito M. Axial ligation states of five-coordinate heme oxygenase proximal histidine mutants, as revealed by EPR and resonance raman spectroscopy Journal of the American Chemical Society. 122: 12612-12613. DOI: 10.1021/Ja0017209 |
0.609 |
|
| 1999 |
Chu GC, Tomita T, Sönnichsen FD, Yoshida T, Ikeda-Saito M. The heme complex of Hmu O, a bacterial heme degradation enzyme from Corynebacterium diphtheriae. Structure of the catalytic site. The Journal of Biological Chemistry. 274: 24490-6. PMID 10455111 DOI: 10.1074/Jbc.274.35.24490 |
0.704 |
|
| 1999 |
Chu GC, Katakura K, Zhang X, Yoshida T, Ikeda-Saito M. Heme degradation as catalyzed by a recombinant bacterial heme oxygenase (Hmu O) from Corynebacterium diphtheriae. The Journal of Biological Chemistry. 274: 21319-25. PMID 10409691 DOI: 10.1074/Jbc.274.30.21319 |
0.701 |
|
| 1999 |
Chu GC, Park SY, Shiro Y, Yoshida T, Ikeda-Saito M. Crystallization and preliminary X-ray diffraction analysis of a recombinant bacterial heme oxygenase (Hmu O) from Corynebacterium diphtheriae. Journal of Structural Biology. 126: 171-4. PMID 10388628 DOI: 10.1006/Jsbi.1999.4122 |
0.683 |
|
| 1999 |
Pond AE, Roach MP, Sono M, Rux AH, Franzen S, Hu R, Thomas MR, Wilks A, Dou Y, Ikeda-Saito M, Ortiz de Montellano PR, Woodruff WH, Boxer SG, Dawson JH. Assignment of the heme axial ligand(s) for the ferric myoglobin (H93G) and heme oxygenase (H25A) cavity mutants as oxygen donors using magnetic circular dichroism. Biochemistry. 38: 7601-8. PMID 10360958 DOI: 10.1021/Bi9825448 |
0.393 |
|
| 1999 |
Kholodenko Y, Gooding EA, Dou Y, Ikeda-Saito M, Hochstrasser RM. Heme protein dynamics revealed by geminate nitric oxide recombination in mutants of iron and cobalt myoglobin. Biochemistry. 38: 5918-24. PMID 10231545 DOI: 10.1021/Bi983022V |
0.397 |
|
| 1998 |
Martásek P, Miller RT, Liu Q, Roman LJ, Salerno JC, Migita CT, Raman CS, Gross SS, Ikeda-Saito M, Masters BS. The C331A mutant of neuronal nitric-oxide synthase is defective in arginine binding. The Journal of Biological Chemistry. 273: 34799-805. PMID 9857005 DOI: 10.1074/Jbc.273.52.34799 |
0.311 |
|
| 1998 |
Sugimoto T, Unno M, Shiro Y, Dou Y, Ikeda-Saito M. Myoglobin mutants giving the largest geminate yield in CO rebinding in the nanosecond time domain Biophysical Journal. 75: 2188-2194. PMID 9788913 DOI: 10.1016/S0006-3495(98)77662-3 |
0.346 |
|
| 1998 |
Tada T, Watanabe YH, Matsuoka A, Ikeda-Saito M, Imai K, Ni-Hei Y, Shikama K. African elephant myoglobin with an unusual autoxidation behavior: Comparison with the H64Q mutant of sperm whale myoglobin Biochimica Et Biophysica Acta - Protein Structure and Molecular Enzymology. 1387: 165-176. PMID 9748556 DOI: 10.1016/S0167-4838(98)00118-6 |
0.301 |
|
| 1998 |
Ishikawa K, Matera KM, Zhou H, Fujii H, Sato M, Yoshimura T, Ikeda-Saito M, Yoshida T. Identification of histidine 45 as the axial heme iron ligand of heme oxygenase-2 Journal of Biological Chemistry. 273: 4317-4322. PMID 9468479 DOI: 10.1074/Jbc.273.8.4317 |
0.452 |
|
| 1998 |
Migita CT, Matera KM, Ikeda-Saito M, Olson JS, Fujii H, Yoshimura T, Zhou H, Yoshida T. The oxygen and carbon monoxide reactions of heme oxygenase. The Journal of Biological Chemistry. 273: 945-9. PMID 9422754 DOI: 10.1074/Jbc.273.2.945 |
0.475 |
|
| 1998 |
Fujii H, Dou Y, Zhou H, Yoshida T, Ikeda-Saito M. Cobalt porphyrin heme oxygenase complex. EPR evidences for the distal heme pocket hydrogen bonding [4] Journal of the American Chemical Society. 120: 8251-8252. DOI: 10.1021/Ja973925W |
0.365 |
|
| 1998 |
Fujii H, Matera KM, Takahashi S, Migita CT, Zhou H, Yoshida T, Ikeda-Saito M. Heme Degradation Mechanism by Heme Oxygenase: Conversion of α-meso-Hydroxyheme to Verdoheme IXα The Keio Journal of Medicine. 45: 315-321. DOI: 10.1007/978-4-431-68476-3_39 |
0.416 |
|
| 1997 |
Migita CT, Salerno JC, Masters BS, Martasek P, McMillan K, Ikeda-Saito M. Substrate binding-induced changes in the EPR spectra of the ferrous nitric oxide complexes of neuronal nitric oxide synthase. Biochemistry. 36: 10987-92. PMID 9283090 DOI: 10.1021/Bi970823+ |
0.403 |
|
| 1997 |
Matera KM, Zhou H, Migita CT, Hobert SE, Ishikawa K, Katakura K, Maeshima H, Yoshida T, Ikeda-Saito M. Histidine-132 does not stabilize a distal water ligand and is not an important residue for the enzyme activity in heme oxygenase-1 Biochemistry. 36: 4909-4915. PMID 9125512 DOI: 10.1021/Bi962321M |
0.405 |
|
| 1997 |
Takahashi S, Matera KM, Fujii H, Zhou H, Ishikawa K, Yoshida T, Ikeda-Saito M, Rousseau DL. Resonance Raman spectroscopic characterization of α-hydroxyheme and verdoheme complexes of heme oxygenase Biochemistry. 36: 1402-1410. PMID 9063888 DOI: 10.1021/Bi962361Q |
0.46 |
|
| 1996 |
Brucker EA, Olson JS, Phillips GN, Dou Y, Ikeda-Saito M. High resolution crystal structures of the deoxy, oxy, and aquomet forms of cobalt myoglobin. The Journal of Biological Chemistry. 271: 25419-22. PMID 8810310 DOI: 10.1074/Jbc.271.41.25419 |
0.41 |
|
| 1996 |
Matera KM, Takahashi S, Fujii H, Zhou H, Ishikawa K, Yoshimura T, Rousseau DL, Yoshida T, Ikeda-Saito M. Oxygen and one reducing equivalent are both required for the conversion of alpha-hydroxyhemin to verdoheme in heme oxygenase. The Journal of Biological Chemistry. 271: 6618-24. PMID 8636077 DOI: 10.1074/Jbc.271.12.6618 |
0.402 |
|
| 1995 |
Ishikawa K, Takeuchi N, Takahashi S, Matera KM, Sato M, Shibahara S, Rousseau DL, Ikeda-Saito M, Yoshida T. Heme oxygenase-2: Properties of the heme complex of the purified tryptic fragment of recombinant human heme oxygenase-2 Journal of Biological Chemistry. 270: 6345-6350. PMID 7890772 DOI: 10.1074/Jbc.270.11.6345 |
0.462 |
|
| 1995 |
Quillin ML, Li T, Olson JS, Phillips GN, Dou Y, Ikeda-Saito M, Regan R, Carlson M, Gibson QH, Li H. Structural and functional effects of apolar mutations of the distal valine in myoglobin. Journal of Molecular Biology. 245: 416-36. PMID 7837273 DOI: 10.1006/Jmbi.1994.0034 |
0.394 |
|
| 1995 |
Dou Y, Admiraal SJ, Ikeda-Saito M, Krzywda S, Wilkinson AJ, Li T, Olson JS, Prince RC, Pickering IJ, George GN. Alteration of axial coordination by protein engineering in myoglobin. Bisimidazole ligation in the His64-->Val/Val68-->His double mutant. The Journal of Biological Chemistry. 270: 15993-6001. PMID 7608158 DOI: 10.1074/Jbc.270.27.15993 |
0.456 |
|
| 1995 |
Shibayama N, Ikeda-Saito M, Hori H, Itaroku K, Morimoto H, Saigo S. Oxygen equilibrium and electron paramagnetic resonance studies on copper(II)-iron(II) hybrid hemoglobins at room temperature Febs Letters. 372: 126-130. PMID 7556632 DOI: 10.1016/0014-5793(95)00965-C |
0.329 |
|
| 1995 |
Sono M, Stuehr DJ, Ikeda-Saito M, Dawson JH. Identification of nitric oxide synthase as a thiolate-ligated heme protein using magnetic circular dichroism spectroscopy. Comparison with cytochrome P-450-CAM and chloroperoxidase. The Journal of Biological Chemistry. 270: 19943-8. PMID 7544348 DOI: 10.1074/Jbc.270.34.19943 |
0.377 |
|
| 1995 |
Takahashi S, Ishikawa K, Takeuchi N, Ikeda-Saito M, Yoshida T, Rousseau DL. Oxygen-bound heme-heme oxygenase complex: Evidence for a highly bent structure of the coordinated oxygen Journal of the American Chemical Society. 117: 6002-6006. DOI: 10.1021/Ja00127A013 |
0.513 |
|
| 1994 |
Takahashi S, Wang J, Rousseau DL, Ishikawa K, Yoshida T, Host JR, Ikeda-Saito M. Heme-heme oxygenase complex: Structure of the catalytic site and its implication for oxygen activation Journal of Biological Chemistry. 269: 1010-1014. PMID 8288555 |
0.385 |
|
| 1994 |
Takahashi S, Wang J, Rousseau DL, Ishikawa K, Yoshida T, Takeuchi N, Ikeda-Saito M. Heme-heme oxygenase complex: structure and properties of the catalytic site from resonance Raman scattering. Biochemistry. 33: 5531-8. PMID 8180175 DOI: 10.1021/Bi00184A023 |
0.467 |
|
| 1994 |
Hargrove MS, Krzywda S, Wilkinson AJ, Dou Y, Ikeda-Saito M, Olson JS. Stability of myoglobin: a model for the folding of heme proteins. Biochemistry. 33: 11767-75. PMID 7918393 DOI: 10.1021/Bi00205A012 |
0.35 |
|
| 1994 |
Felsch JS, Horvath MP, Gursky S, Hobaugh MR, Goudreau PN, Fee JA, Morgan WT, Admiraal SJ, Ikeda-Saito M, Fujiwara T. Probing protein-cofactor interactions in the terminal oxidases by second derivative spectroscopy: study of bacterial enzymes with cofactor substitutions and heme A model compounds. Protein Science : a Publication of the Protein Society. 3: 2097-103. PMID 7703856 DOI: 10.1002/Pro.5560031123 |
0.409 |
|
| 1993 |
Ikeda-Saito M, Dou Y, Yonetani T, Olson JS, Li T, Regan R, Gibson QH. Ligand diffusion in the distal heme pocket of myoglobin. A primary determinant of geminate rebinding. The Journal of Biological Chemistry. 268: 6855-7. PMID 8463211 |
0.307 |
|
| 1993 |
Wang J, Stuehr DJ, Ikeda-Saito M, Rousseau DL. Heme coordination and structure of the catalytic site in nitric oxide synthase Journal of Biological Chemistry. 268: 22255-22258. PMID 7693663 |
0.367 |
|
| 1992 |
Ikeda-Saito M, Hori H, Andersson LA, Prince RC, Pickering IJ, George GN, Sanders CR, Lutz RS, McKelvey EJ, Mattera R. Coordination structure of the ferric heme iron in engineered distal histidine myoglobin mutants Journal of Biological Chemistry. 267: 22843-22852. PMID 1429633 |
0.335 |
|
| 1992 |
Stuehr DJ, Ikeda-Saito M. Spectral characterization of brain and macrophage nitric oxide synthases: Cytochrome P-450-like hemeproteins that contain a flavin semiquinone radical Journal of Biological Chemistry. 267: 20547-20550. PMID 1383204 |
0.336 |
|
| 1991 |
Lee HC, Booth KS, Caughey WS, Ikeda-Saito M. Interaction of halides with the cyanide complex of myeloperoxidase: a model for substrate binding to compound I Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 1076: 317-320. PMID 1847831 DOI: 10.1016/0167-4838(91)90285-8 |
0.411 |
|
| 1991 |
Sono M, Bracete AM, Huff AM, Ikeda-Saito M, Dawson JH. Evidence that a formyl-substituted iron porphyrin is the prosthetic group of myeloperoxidase: magnetic circular dichroism similarity of the peroxidase to Spirographis heme-reconstituted myoglobin. Proceedings of the National Academy of Sciences of the United States of America. 88: 11148-52. PMID 1662385 DOI: 10.1073/Pnas.88.24.11148 |
0.429 |
|
| 1991 |
Ikeda-Saito M, Lutz RS, Shelley DA, McKelvey EJ, Mattera R, Hori H. EPR characterization of the stereochemistry of the distal heme pocket of the engineered human myoglobin mutants Journal of Biological Chemistry. 266: 23641-23647. PMID 1660880 |
0.308 |
|
| 1990 |
Ikeda-Saito M, Kimura S. Axial ligand coordination in intestinal peroxidase Archives of Biochemistry and Biophysics. 283: 351-355. PMID 2177328 DOI: 10.1016/0003-9861(90)90653-G |
0.333 |
|
| 1990 |
Hori H, Ikeda-Saito M. Photochemically modified myeloperoxidase, with optical spectral properties analogous to those of lactoperoxidase, retains its original catalytic activity Biochemistry®. 29: 7106-7112. PMID 2171641 DOI: 10.1021/Bi00482A023 |
0.41 |
|
| 1988 |
Murray LP, Hofrichter J, Henry ER, Ikeda-Saito M, Kitagishi K, Yonetani T, Eaton WA. The effect of quaternary structure on the kinetics of conformational changes and nanosecond geminate rebinding of carbon monoxide to hemoglobin. Proceedings of the National Academy of Sciences of the United States of America. 85: 2151-5. PMID 3353372 DOI: 10.1073/Pnas.85.7.2151 |
0.37 |
|
| 1987 |
Miura S, Ikeda-Saito M, Yonetani T, Ho C. Oxygen equilibrium studies of cross-linked asymmetrical cyanomet valency hybrid hemoglobins: Models for partially oxygenated species Biochemistry. 26: 2149-2155. PMID 3620444 DOI: 10.1021/Bi00382A013 |
0.36 |
|
| 1987 |
Ikeda-Saito M, Inubushi T. Proton magnetic resonance of the bovine spleen green heme-protein Febs Letters. 214: 111-116. PMID 3032675 DOI: 10.1016/0014-5793(87)80023-6 |
0.344 |
|
| 1986 |
Inubushi T, D'Ambrosio C, Ikeda-Saito M, Yonetani T. NMR studies of mono-liganded iron-cobalt hybrid hemoglobins: their quaternary structure and proximal histidine coordination Journal of the American Chemical Society. 108: 3799-3803. DOI: 10.1021/Ja00273A040 |
0.407 |
|
| 1986 |
Inubushi T, D'ambrosio C, Ikeda-Saito M, Yonetani T. NMR Studies of Monoliganded Fe-Co Hybrid Hemoglobins: Their Quaternary Structure and Proximal Histidine Coordination (use of CO derivatives of tricobaltsubstituted Fe-Co hybrid hemoglobins as models for the intermediate species produc Cheminform. 17. DOI: 10.1002/Chin.198642053 |
0.339 |
|
| 1985 |
Hofrichter J, Henry ER, Sommer JH, Deutsch R, Ikeda-Saito M, Yonetani T, Eaton WA. Nanosecond optical spectra of iron-cobalt hybrid hemoglobins: geminate recombination, conformational changes, and intersubunit communication. Biochemistry. 24: 2667-79. PMID 4027219 DOI: 10.1021/Bi00332A012 |
0.358 |
|
| 1985 |
Ikeda-Saito M, Prince RC. The effect of chloride on the redox and EPR properties of myeloperoxidase Journal of Biological Chemistry. 260: 8301-8305. PMID 2989285 |
0.301 |
|
| 1984 |
Argade PV, Sassardi M, Rousseau DL, Inubushi T, Ikeda-Saito M, Lapidot A. Confirmation of the assignment of the iron-histidine stretching mode in myoglobin Journal of the American Chemical Society. 106: 6593-6596. DOI: 10.1021/Ja00334A024 |
0.333 |
|
| 1983 |
Friedman JM, Scott TW, Stepnoski RA, Ikeda-Saito M, Yonetani T. The iron-proximal histidine linkage and protein control of oxygen binding in hemoglobin. A transient Raman study. The Journal of Biological Chemistry. 258: 10564-72. PMID 6885793 |
0.302 |
|
| 1983 |
Inubushi T, Ikeda-Saito M, Yonetani T. Isotropically shifted NMR resonances for the proximal histidyl imidazole NH protons in cobalt hemoglobin and iron-cobalt hybrid hemoglobins. Binding of the proximal histidine toward porphyrin metal ion in the intermediate state of cooperative ligand binding Biochemistry. 22: 2904-2907. PMID 6871170 DOI: 10.1021/Bi00281A019 |
0.361 |
|
| 1982 |
Kitagawa T, Ondrias MR, Rousseau DL, Ikeda-saito M, Yonetani T. Evidence for hydrogen bonding of bound dioxygen to the distal histidine of oxycobalt myoglobin and haemoglobin Nature. 298: 869-871. PMID 7110321 DOI: 10.1038/298869A0 |
0.381 |
|
| 1982 |
Verzili D, Santucci R, Ikeda-saito M, Chiancone E, Ascoli F, Yonetani T, Antonini E. Studies on scapharca hemoglobins. Properties of the dimeric protein reconstituted with Fe- or Co-porphyrin Biochimica Et Biophysica Acta (Bba)/Protein Structure and Molecular. 704: 215-220. PMID 6285982 DOI: 10.1016/0167-4838(82)90148-0 |
0.351 |
|
| 1982 |
Hori H, Ikeda-Saito M, Yonetani T. Ligand orientation of oxyproto- and oxymesocobalt porphyrin-substituted myoglobin by single crystal EPR spectroscopy Journal of Biological Chemistry. 257: 3636-3642. PMID 6277941 |
0.319 |
|
| 1981 |
Ikeda-Saito M, Inubushi T, Yonetani T. [9] Preparation of hybrid hemoglobins with different prosthetic groups Methods in Enzymology. 76: 113-121. PMID 7329254 DOI: 10.1016/0076-6879(81)76119-6 |
0.35 |
|
| 1979 |
Ikeda-Saito M, Brunori M, Winterhalter KH, Tonetani T. Cobalt-substituted hemoglobin Zürich (α2β2 63His→Arg). Oxygen equilibria and EPR spectra Bba - Protein Structure. 580: 91-99. PMID 232666 DOI: 10.1016/0005-2795(79)90200-9 |
0.3 |
|
| 1975 |
Kitagawa T, Kyogoku Y, Iizuka T, Ikeda-saito M, Yamanaka T. Resonance Raman scattering from hemoproteins: Effects of ligands upon the raman spectra of various c-type cytochromes Journal of Biochemistry. 78: 719-728. PMID 2584 DOI: 10.1093/Oxfordjournals.Jbchem.A130960 |
0.36 |
|
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