-
1
-
-
84940915988
-
Heme oxygenase structure and mechanism
-
Kadish, K, Smith, K. and Guilard, R, eds, pp, Academic Press, New York
-
Ortiz de Montellano, P. R. and Auclair, K. (2003) Heme oxygenase structure and mechanism. In Porphyrin Handbook, vol. 12 (Kadish, K., Smith, K. and Guilard, R., eds), pp. 183-210, Academic Press, New York
-
(2003)
Porphyrin Handbook
, vol.12
, pp. 183-210
-
-
Ortiz de Montellano, P.R.1
Auclair, K.2
-
3
-
-
0014670945
-
Microsomal heme oxygenase: Characterization of the enzyme
-
Tenhunen, R., Marver, H. S. and Schmid, R. (1969) Microsomal heme oxygenase: characterization of the enzyme. J. Biol. Chem. 244, 6388-6394
-
(1969)
J. Biol. Chem
, vol.244
, pp. 6388-6394
-
-
Tenhunen, R.1
Marver, H.S.2
Schmid, R.3
-
4
-
-
0015501157
-
Immunochemical evidence for an association of heme oxygenase with the microsomal electron transport system
-
Schacter, B. A., Nelson, E. B., Marver, H. S. and Masters, B. S. S. (1972) Immunochemical evidence for an association of heme oxygenase with the microsomal electron transport system. J. Biol. Chem. 247, 3601-3607
-
(1972)
J. Biol. Chem
, vol.247
, pp. 3601-3607
-
-
Schacter, B.A.1
Nelson, E.B.2
Marver, H.S.3
Masters, B.S.S.4
-
5
-
-
0019332526
-
Oxygenated form of heme-heme oxygenase complex and requirement for second electron to initiate heme degradation from the oxygenated complex
-
Yoshida, T., Noguchi, M. and Kikuchi, G. (1980) Oxygenated form of heme-heme oxygenase complex and requirement for second electron to initiate heme degradation from the oxygenated complex. J. Biol. Chem. 255, 4418-4420
-
(1980)
J. Biol. Chem
, vol.255
, pp. 4418-4420
-
-
Yoshida, T.1
Noguchi, M.2
Kikuchi, G.3
-
6
-
-
33645945014
-
Heme oxygenase-1/carbon monoxide: From basic science to therapeutic applications
-
Ryter, S. W., Alam, J. and Choi, A. M. K. (2006) Heme oxygenase-1/carbon monoxide: from basic science to therapeutic applications. Physiol. Rev. 86, 583-650
-
(2006)
Physiol. Rev
, vol.86
, pp. 583-650
-
-
Ryter, S.W.1
Alam, J.2
Choi, A.M.K.3
-
7
-
-
0023731036
-
Heme oxygenase: Function, multiplicity, regulatory mechanisms, and clinical applications
-
Maines, M. D. (1988) Heme oxygenase: function, multiplicity, regulatory mechanisms, and clinical applications. FASEB J. 2, 2557-2568
-
(1988)
FASEB J
, vol.2
, pp. 2557-2568
-
-
Maines, M.D.1
-
8
-
-
0035949667
-
Neural roles for heme oxygenase: Contrasts to nitric oxide synthase
-
Barañano, D. E. and Snyder, S. H. (2001) Neural roles for heme oxygenase: contrasts to nitric oxide synthase. Proc. Natl. Acad. Sci. U.S.A. 98, 10996-11002
-
(2001)
Proc. Natl. Acad. Sci. U.S.A
, vol.98
, pp. 10996-11002
-
-
Barañano, D.E.1
Snyder, S.H.2
-
9
-
-
0019590350
-
Degradation of mesoheme and hydroxymesoheme catalyzed by the heme oxygenase system: Involvement of hydroxyheme in the sequence of heme catabolism
-
Yoshida, T., Noguchi, M., Kikuchi, G. and Sano, S. (1981) Degradation of mesoheme and hydroxymesoheme catalyzed by the heme oxygenase system: involvement of hydroxyheme in the sequence of heme catabolism. J. Biochem. (Tokyo) 90, 125-131
-
(1981)
J. Biochem. (Tokyo)
, vol.90
, pp. 125-131
-
-
Yoshida, T.1
Noguchi, M.2
Kikuchi, G.3
Sano, S.4
-
10
-
-
0036428431
-
The reactivity of α-hydroxyhaem and verdohaem bound to haem oxygenase-1 to dioxygen and sodium dithionite
-
Sakamoto, H., Omata, Y., Hayashi, S., Harada, S., Palmer, G. and Noguchi, M. (2002) The reactivity of α-hydroxyhaem and verdohaem bound to haem oxygenase-1 to dioxygen and sodium dithionite. Eur. J. Biochem. 269, 5231-5239
-
(2002)
Eur. J. Biochem
, vol.269
, pp. 5231-5239
-
-
Sakamoto, H.1
Omata, Y.2
Hayashi, S.3
Harada, S.4
Palmer, G.5
Noguchi, M.6
-
11
-
-
0033603348
-
Ferric a-hydroxyheme bound to heme oxygenase can be converted to verdoheme by dioxygen in the absence of added reducing equivalents
-
Sakamoto, H., Omata, Y., Palmer, G. and Noguchi, M. (1999) Ferric a-hydroxyheme bound to heme oxygenase can be converted to verdoheme by dioxygen in the absence of added reducing equivalents. J. Biol. Chem. 274, 18196-18200
-
(1999)
J. Biol. Chem
, vol.274
, pp. 18196-18200
-
-
Sakamoto, H.1
Omata, Y.2
Palmer, G.3
Noguchi, M.4
-
12
-
-
0020353758
-
The step of carbon monoxide liberation in the sequence of heme degradation catalyzed by the reconstituted microsomal heme oxygenase system
-
Yoshida, T., Noguchi, M. and Kikuchi, G. (1982) The step of carbon monoxide liberation in the sequence of heme degradation catalyzed by the reconstituted microsomal heme oxygenase system. J. Biol. Chem. 257, 9345-9348
-
(1982)
J. Biol. Chem
, vol.257
, pp. 9345-9348
-
-
Yoshida, T.1
Noguchi, M.2
Kikuchi, G.3
-
13
-
-
0029917163
-
Oxygen and one reducing equivalent are both required for the conversion of α-hydroxyhemin to verdoheme in heme oxygenase
-
Matera, K. M., Takahashi, S., Fujii, H., Zohu, H., Ishikawa, K., Yoshimura, T., Rousseau, D. L., Yoshida, T. and Ikeda-Saito, M. (1996) Oxygen and one reducing equivalent are both required for the conversion of α-hydroxyhemin to verdoheme in heme oxygenase. J. Biol. Chem. 271, 6618-6624
-
(1996)
J. Biol. Chem
, vol.271
, pp. 6618-6624
-
-
Matera, K.M.1
Takahashi, S.2
Fujii, H.3
Zohu, H.4
Ishikawa, K.5
Yoshimura, T.6
Rousseau, D.L.7
Yoshida, T.8
Ikeda-Saito, M.9
-
14
-
-
0033733182
-
Separation and identification of the regioisomers of verdoheme by reversed-phase ion-pair high-performance liquid chromatography, and characterization of their complexes with heme oxygenase
-
Sakamoto, H., Omata, Y., Adachi, Y., Palmer, G. and Noguchi, M. (2000) Separation and identification of the regioisomers of verdoheme by reversed-phase ion-pair high-performance liquid chromatography, and characterization of their complexes with heme oxygenase. J. Inorg. Biochem. 82, 113-121
-
(2000)
J. Inorg. Biochem
, vol.82
, pp. 113-121
-
-
Sakamoto, H.1
Omata, Y.2
Adachi, Y.3
Palmer, G.4
Noguchi, M.5
-
15
-
-
27544432712
-
A kinetic study of the mechanism of conversion of α-hydroxyheme to verdoheme while bound to heme oxygenase
-
Sakamoto, H., Takahashi, K., Higashimoto, Y., Harada, S., Palmer, G. and Noguchi, M. (2005) A kinetic study of the mechanism of conversion of α-hydroxyheme to verdoheme while bound to heme oxygenase. Biochem. Biophys. Res. Commun. 338, 578-583
-
(2005)
Biochem. Biophys. Res. Commun
, vol.338
, pp. 578-583
-
-
Sakamoto, H.1
Takahashi, K.2
Higashimoto, Y.3
Harada, S.4
Palmer, G.5
Noguchi, M.6
-
16
-
-
4143105792
-
CO-trapping site in heme oxygenase revealed by photolysis of its CO-bound heme complex: Mechanism of escaping from product inhibition
-
Sugishima, M., Sakamoto, H., Noguchi, M. and Fukuyama, K. (2004) CO-trapping site in heme oxygenase revealed by photolysis of its CO-bound heme complex: mechanism of escaping from product inhibition. J. Mol. Biol. 341, 7-13
-
(2004)
J. Mol. Biol
, vol.341
, pp. 7-13
-
-
Sugishima, M.1
Sakamoto, H.2
Noguchi, M.3
Fukuyama, K.4
-
17
-
-
27744467540
-
2-dependent verdoheme degradation by heme oxygenase: Reaction mechanisms and potential physiological roles of the dual pathway degradation
-
2-dependent verdoheme degradation by heme oxygenase: reaction mechanisms and potential physiological roles of the dual pathway degradation. J. Biol. Chem. 280, 36833-36840
-
(2005)
J. Biol. Chem
, vol.280
, pp. 36833-36840
-
-
Matsui, T.1
Nakajima, A.2
Fujii, H.3
Matera, K.M.4
Migita, C.T.5
Yoshida, T.6
Ikeda-Saito, M.7
-
18
-
-
0027440198
-
Rat liver heme oxygenase: High level expression of a truncated soluble form and nature of the meso-hydroxylating species
-
Wilks, A. and Ortiz de Montellano, P. R. (1993) Rat liver heme oxygenase: high level expression of a truncated soluble form and nature of the meso-hydroxylating species. J. Biol. Chem. 268, 22357-22362
-
(1993)
J. Biol. Chem
, vol.268
, pp. 22357-22362
-
-
Wilks, A.1
Ortiz de Montellano, P.R.2
-
19
-
-
0000556983
-
Verdohemochrome IXα: Preparation and oxidoreductive cleavage to biliverdin IXα
-
Saito, S. and Itano, H. A. (1982) Verdohemochrome IXα: preparation and oxidoreductive cleavage to biliverdin IXα. Proc. Natl. Acad. Sci. U.S.A. 79, 1393-1397
-
(1982)
Proc. Natl. Acad. Sci. U.S.A
, vol.79
, pp. 1393-1397
-
-
Saito, S.1
Itano, H.A.2
-
20
-
-
0021132163
-
Features of intermediary steps around the 688-nm substance in the heme oxygenase reaction
-
Yoshida, T. and Noguchi, M. (1984) Features of intermediary steps around the 688-nm substance in the heme oxygenase reaction. J. Biochem. (Tokyo) 96, 563-570
-
(1984)
J. Biochem. (Tokyo)
, vol.96
, pp. 563-570
-
-
Yoshida, T.1
Noguchi, M.2
-
21
-
-
0040141555
-
Reaction intermediates and single turnover rate constants for the oxidation of heme by human heme oxygenase-1
-
Liu, Y. and Ortiz de Montellano, P. R. (2000) Reaction intermediates and single turnover rate constants for the oxidation of heme by human heme oxygenase-1. J. Biol. Chem. 275, 5297-5307
-
(2000)
J. Biol. Chem
, vol.275
, pp. 5297-5307
-
-
Liu, Y.1
Ortiz de Montellano, P.R.2
-
22
-
-
7544235538
-
Crystal structures of ferrous and ferrous-NO forms of verdoheme in a complex with human heme oxygenase-1: Catalytic implications for heme cleavage
-
Lad, L., Ortiz de Montellano, P. R. and Poulos, T. L. (2004) Crystal structures of ferrous and ferrous-NO forms of verdoheme in a complex with human heme oxygenase-1: catalytic implications for heme cleavage. J. Inorg. Biochem. 98, 1686-1695
-
(2004)
J. Inorg. Biochem
, vol.98
, pp. 1686-1695
-
-
Lad, L.1
Ortiz de Montellano, P.R.2
Poulos, T.L.3
-
23
-
-
0542422859
-
Heme oxygenase mechanism: Evidence for an electrophilic, ferric peroxide species
-
Ortiz de Montellano, P. R. (1998) Heme oxygenase mechanism: evidence for an electrophilic, ferric peroxide species. Acc. Chem. Res. 31, 543-549
-
(1998)
Acc. Chem. Res
, vol.31
, pp. 543-549
-
-
Ortiz de Montellano, P.R.1
-
24
-
-
34548440800
-
Electrochemical reduction of ferrous α-verdoheme in complex with heme oxygenase-1
-
Sato, H., Higashimoto, Y., Sakamoto, H., Sugishima, M., Takahashi, K., Palmer, G. and Noguchi, M. (2007) Electrochemical reduction of ferrous α-verdoheme in complex with heme oxygenase-1. J. Inorg. Biochem. 101, 1394-1399
-
(2007)
J. Inorg. Biochem
, vol.101
, pp. 1394-1399
-
-
Sato, H.1
Higashimoto, Y.2
Sakamoto, H.3
Sugishima, M.4
Takahashi, K.5
Palmer, G.6
Noguchi, M.7
-
25
-
-
0037732736
-
Stereoselectivity of each of the three steps of the heme oxygenase reaction: Hemin to meso-hydroxyhemin, meso-hydroxyhemin to verdoheme, and verdoheme to biliverdin
-
Zhang, X., Fujii, H., Matera, K. M., Migita, C. T., Sun, D., Sato, M., Ikeda-Saito, M. and Yoshida, T. (2003) 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, 7418-7426
-
(2003)
Biochemistry
, vol.42
, pp. 7418-7426
-
-
Zhang, X.1
Fujii, H.2
Matera, K.M.3
Migita, C.T.4
Sun, D.5
Sato, M.6
Ikeda-Saito, M.7
Yoshida, T.8
-
26
-
-
0019166680
-
A new intermediate of heme degradation catalyzed by the heme oxygenase system
-
Yoshida, T., Noguchi, M. and Kikuchi, G. (1980) A new intermediate of heme degradation catalyzed by the heme oxygenase system. J. Biochem. (Tokyo) 88, 557-563
-
(1980)
J. Biochem. (Tokyo)
, vol.88
, pp. 557-563
-
-
Yoshida, T.1
Noguchi, M.2
Kikuchi, G.3
-
27
-
-
41549098745
-
Alkyl peroxides reveal the ring opening mechanism of verdoheme catalyzed by heme oxygenase
-
Matsui, T., Omori, K., Jin, H. and Ikeda-Saito, M. (2008) Alkyl peroxides reveal the ring opening mechanism of verdoheme catalyzed by heme oxygenase. J. Am. Chem. Soc. 130, 4220-4221
-
(2008)
J. Am. Chem. Soc
, vol.130
, pp. 4220-4221
-
-
Matsui, T.1
Omori, K.2
Jin, H.3
Ikeda-Saito, M.4
-
28
-
-
0032830567
-
Crystal structure of human heme oxygenase-1
-
Schuller, D. J., Wilks, A., Ortiz de Montellano, P. R. and Poulos, T. L. (1999) Crystal structure of human heme oxygenase-1. Nat. Struct. Biol. 6, 860-867
-
(1999)
Nat. Struct. Biol
, vol.6
, pp. 860-867
-
-
Schuller, D.J.1
Wilks, A.2
Ortiz de Montellano, P.R.3
Poulos, T.L.4
-
29
-
-
0034616274
-
Crystal structure of rat heme oxygenase-1 in complex with heme
-
Sugishima, M., Omata, Y., Kakuta, Y., Sakamoto, H., Noguchi, M. and Fukuyama, K. (2000) Crystal structure of rat heme oxygenase-1 in complex with heme. FEBS Lett. 471, 61-66
-
(2000)
FEBS Lett
, vol.471
, pp. 61-66
-
-
Sugishima, M.1
Omata, Y.2
Kakuta, Y.3
Sakamoto, H.4
Noguchi, M.5
Fukuyama, K.6
-
30
-
-
0346003806
-
Crystal structure of rat heme oxygenase-1 in complex with heme bound to azide: Implication for regiospecific hydroxylation of heme at the -meso carbon
-
Sugishima, M., Sakamoto, H., Higashimoto, Y., Omata, Y., Hayashi, S., Noguchi, M. and Fukuyama, K. (2002) Crystal structure of rat heme oxygenase-1 in complex with heme bound to azide: implication for regiospecific hydroxylation of heme at the "-meso carbon. J. Biol. Chem. 277, 45086-45090
-
(2002)
J. Biol. Chem
, vol.277
, pp. 45086-45090
-
-
Sugishima, M.1
Sakamoto, H.2
Higashimoto, Y.3
Omata, Y.4
Hayashi, S.5
Noguchi, M.6
Fukuyama, K.7
-
32
-
-
0037709372
-
Crystal structures of the ferric, ferrous, and ferrous-NO forms of the Asp140Ala mutant of human heme oxygenase-1: Catalytic implications
-
Lad, L., Wang, J., Li, H., Friedman, J., Bhaskar, B., Ortiz de Montellano, P. R. and Poulos, T. L. (2003) Crystal structures of the ferric, ferrous, and ferrous-NO forms of the Asp140Ala mutant of human heme oxygenase-1: catalytic implications. J. Mol. Biol. 330, 527-538
-
(2003)
J. Mol. Biol
, vol.330
, pp. 527-538
-
-
Lad, L.1
Wang, J.2
Li, H.3
Friedman, J.4
Bhaskar, B.5
Ortiz de Montellano, P.R.6
Poulos, T.L.7
-
33
-
-
0041355223
-
Crystal structure of rat heme oxygenase-1 in complex with biliverdin-iron chelate: Conformational change of the distal helix during the heme cleavage reaction
-
Sugishima, M., Sakamoto, H., Higashimoto, Y., Noguchi, M. and Fukuyama, K. (2003) Crystal structure of rat heme oxygenase-1 in complex with biliverdin-iron chelate: conformational change of the distal helix during the heme cleavage reaction. J. Biol. Chem. 278, 32352-32358
-
(2003)
J. Biol. Chem
, vol.278
, pp. 32352-32358
-
-
Sugishima, M.1
Sakamoto, H.2
Higashimoto, Y.3
Noguchi, M.4
Fukuyama, K.5
-
34
-
-
0035844131
-
Solution 1H NMR of the active site of substrate-bound, cyanide-inhibited human heme oxygenase: Comparison to the crystal structure of the water-ligated form
-
La Mar, G. N., Asokan, A., Espiritu, B., Yeh, D. C., Auclair, K. and Ortiz de Montellano, P. R. (2001) Solution 1H NMR of the active site of substrate-bound, cyanide-inhibited human heme oxygenase: comparison to the crystal structure of the water-ligated form. J. Biol. Chem. 276, 15676-15687
-
(2001)
J. Biol. Chem
, vol.276
, pp. 15676-15687
-
-
La Mar, G.N.1
Asokan, A.2
Espiritu, B.3
Yeh, D.C.4
Auclair, K.5
Ortiz de Montellano, P.R.6
-
35
-
-
0031033674
-
Resonance Raman spectroscopic characterization of α-hydroxyheme and verdoheme complexes of heme oxygenase
-
Takahashi, S., Matera, K. M., Fujii, H., Zhou, H., Ishikawa, K., Yoshida, T., Ikeda-Saito, M. and Rousseau, D. L. (1997) Resonance Raman spectroscopic characterization of α-hydroxyheme and verdoheme complexes of heme oxygenase. Biochemistry 36, 1402-1410
-
(1997)
Biochemistry
, vol.36
, pp. 1402-1410
-
-
Takahashi, S.1
Matera, K.M.2
Fujii, H.3
Zhou, H.4
Ishikawa, K.5
Yoshida, T.6
Ikeda-Saito, M.7
Rousseau, D.L.8
-
36
-
-
29344472101
-
The ferrous verdoheme-heme oxygenase complex is six-coordinate and low-spin
-
Damaso, C. O., Bunce, R. A., Barybin, M. V., Wilks, A. and Rivera, M. (2005) The ferrous verdoheme-heme oxygenase complex is six-coordinate and low-spin. J. Am. Chem. Soc. 127, 17582-17583
-
(2005)
J. Am. Chem. Soc
, vol.127
, pp. 17582-17583
-
-
Damaso, C.O.1
Bunce, R.A.2
Barybin, M.V.3
Wilks, A.4
Rivera, M.5
-
37
-
-
0032169653
-
Crystallization and preliminary X-ray diffraction studies on the water soluble form of rat heme oxygenase-1 in complex with heme
-
Omata, Y., Asada, S., Sakamoto, H., Fukuyama, K. and Noguchi, M. (1998) Crystallization and preliminary X-ray diffraction studies on the water soluble form of rat heme oxygenase-1 in complex with heme. Acta Crystallogr. Sect. D Biol. Crystallogr. 54, 1017-1019
-
(1998)
Acta Crystallogr. Sect. D Biol. Crystallogr
, vol.54
, pp. 1017-1019
-
-
Omata, Y.1
Asada, S.2
Sakamoto, H.3
Fukuyama, K.4
Noguchi, M.5
-
38
-
-
33845992927
-
The reactions of heme- and verdoheme-heme oxygenase-1 complexes with FMN-depleted NADPH-cytochrome P450 reductase: Electrons required for verdoheme oxidation can be transferred through a pathway not involving FMN
-
Higashimoto, Y., Sato, H., Sakamoto, H., Takahashi, K., Palmer, G. and Noguchi, M. (2006) The reactions of heme- and verdoheme-heme oxygenase-1 complexes with FMN-depleted NADPH-cytochrome P450 reductase: electrons required for verdoheme oxidation can be transferred through a pathway not involving FMN. J. Biol. Chem. 281, 31659-31667
-
(2006)
J. Biol. Chem
, vol.281
, pp. 31659-31667
-
-
Higashimoto, Y.1
Sato, H.2
Sakamoto, H.3
Takahashi, K.4
Palmer, G.5
Noguchi, M.6
-
39
-
-
9144237033
-
The low-spin heme of cytochrome c oxidase as the driving element of the proton-pumping process
-
Tsukihara, T., Shimokata, K., Katayama, Y., Shimada, H., Muramoto, K., Aoyama, H., Mochizuki, M., Shinzawa-Itoh, K., Yamashita, E., Yao, M. et al. (2003) The low-spin heme of cytochrome c oxidase as the driving element of the proton-pumping process. Proc. Natl. Acad. Sci. U.S.A. 100, 15304-15309
-
(2003)
Proc. Natl. Acad. Sci. U.S.A
, vol.100
, pp. 15304-15309
-
-
Tsukihara, T.1
Shimokata, K.2
Katayama, Y.3
Shimada, H.4
Muramoto, K.5
Aoyama, H.6
Mochizuki, M.7
Shinzawa-Itoh, K.8
Yamashita, E.9
Yao, M.10
-
40
-
-
0031059866
-
Processing of X-ray diffraction data collected in oscillation mode
-
Otwinowski, Z. and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326
-
(1997)
Methods Enzymol
, vol.276
, pp. 307-326
-
-
Otwinowski, Z.1
Minor, W.2
-
41
-
-
0000560808
-
MOLREP: An automated program for molecular replacement
-
Vagin, A. and Teplyakov, A. (1997) MOLREP: an automated program for molecular replacement. J. Appl. Crystallogr. 30, 1022-1025
-
(1997)
J. Appl. Crystallogr
, vol.30
, pp. 1022-1025
-
-
Vagin, A.1
Teplyakov, A.2
-
42
-
-
0028103275
-
-
Collaborative Computational Project, Number 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr. Sect. D Biol. Crystallogr. 50, 760-763
-
Collaborative Computational Project, Number 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr. Sect. D Biol. Crystallogr. 50, 760-763
-
-
-
-
43
-
-
0030924992
-
Refinement of macromolecular structures by the maximum-likelihood method
-
Murshudov, G. N., Vagin, A. A. and Dodson, E. J. (1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr. Sect. D Biol. Crystallogr. 53, 240-255
-
(1997)
Acta Crystallogr. Sect. D Biol. Crystallogr
, vol.53
, pp. 240-255
-
-
Murshudov, G.N.1
Vagin, A.A.2
Dodson, E.J.3
-
44
-
-
0037181030
-
Catalytic mechanism of heme oxygenase through EPR and ENDOR of cryoreduced oxy-heme oxygenase and its Asp 140 mutants
-
Davydov, R., Kofman, V., Fujii, H., Yoshida, T., Ikeda-Saito, M. and Hoffman, B. M. (2002) Catalytic mechanism of heme oxygenase through EPR and ENDOR of cryoreduced oxy-heme oxygenase and its Asp 140 mutants. J. Am. Chem. Soc. 124, 1798-1808
-
(2002)
J. Am. Chem. Soc
, vol.124
, pp. 1798-1808
-
-
Davydov, R.1
Kofman, V.2
Fujii, H.3
Yoshida, T.4
Ikeda-Saito, M.5
Hoffman, B.M.6
|