Id |
Subject |
Object |
Predicate |
Lexical cue |
T1 |
0-108 |
Sentence |
denotes |
Specific modification of structure and property of myoglobin by the formation of tetrazolylhistidine 64(E7). |
T2 |
109-166 |
Sentence |
denotes |
Reaction of the modified myoglobin with molecular oxygen. |
T3 |
167-426 |
Sentence |
denotes |
Tetrazole-myoglobin (Tet-Mb), a site selectively modified myoglobin with tetrazole anion (-CN4-) covalently attached to the imidazole N epsilon of the distal histidine 64(E7) (see Fig. 1; Kamiya, N., Shiro, Y., Iwata, T., Iizuka, T., and Iwasaki, H. (1991) J. |
T4 |
427-430 |
Sentence |
denotes |
Am. |
T5 |
431-436 |
Sentence |
denotes |
Chem. |
T6 |
437-441 |
Sentence |
denotes |
Soc. |
T7 |
442-580 |
Sentence |
denotes |
113, 1826-1829), exhibited unique properties in the reduction from ferric to ferrous states and in the reaction of its deoxy form with O2. |
T8 |
581-802 |
Sentence |
denotes |
The redox potential of Tet-Mb is obtained to be -193 mV, which is much lower than that of unmodified (native) myoglobin (50 mV), possibly due to the electrostatic interaction between the heme iron and the tetrazole group. |
T9 |
803-1001 |
Sentence |
denotes |
The ferrous deoxy form of Tet-Mb was rapidly oxidized to its ferric form in the reaction with O2 at room temperature through an intermediary formation of its oxy form and with the generation of O2-. |
T10 |
1002-1247 |
Sentence |
denotes |
The oxy form of Tet-Mb can be detected by the optical spectral measurement at -12 degrees C, the rapid scan measurement at room temperature, and the electron spin resonance measurement of its cobalt-substituted derivative (Tet-Mb(Co2+)) at 77 K. |
T11 |
1248-1553 |
Sentence |
denotes |
In the kinetic measurement of the O2 binding reaction to Tet-Mb, its association and dissociation rate constants in the bimolecular reaction were 6.1 x 10(7) M-1 s-1 and 2200 s-1, respectively, showing that the tetrazole modification of His-64 extremely accelerates its association and dissociation rates. |
T12 |
1554-1776 |
Sentence |
denotes |
Taken together with the extremely fast autoxidation rate (53 h-1) obtained, these kinetic results suggested that the channel of O2 from the solvent region to the protein interior is open enough to pass the external ligand. |
T13 |
1777-1849 |
Sentence |
denotes |
The structure is discussed in relation to those of some genetic mutants. |
T14 |
1850-2057 |
Sentence |
denotes |
Taking these properties, we demonstrated that Tet-Mb can catalyze O2 consumption to generate O2-, coupled with the NADH-supported enzymatic reduction system of cytochrome P-450cam under an aerobic condition. |
T1 |
0-108 |
Sentence |
denotes |
Specific modification of structure and property of myoglobin by the formation of tetrazolylhistidine 64(E7). |
T2 |
109-166 |
Sentence |
denotes |
Reaction of the modified myoglobin with molecular oxygen. |
T3 |
167-426 |
Sentence |
denotes |
Tetrazole-myoglobin (Tet-Mb), a site selectively modified myoglobin with tetrazole anion (-CN4-) covalently attached to the imidazole N epsilon of the distal histidine 64(E7) (see Fig. 1; Kamiya, N., Shiro, Y., Iwata, T., Iizuka, T., and Iwasaki, H. (1991) J. |
T4 |
427-430 |
Sentence |
denotes |
Am. |
T5 |
431-436 |
Sentence |
denotes |
Chem. |
T6 |
437-441 |
Sentence |
denotes |
Soc. |
T7 |
442-580 |
Sentence |
denotes |
113, 1826-1829), exhibited unique properties in the reduction from ferric to ferrous states and in the reaction of its deoxy form with O2. |
T8 |
581-802 |
Sentence |
denotes |
The redox potential of Tet-Mb is obtained to be -193 mV, which is much lower than that of unmodified (native) myoglobin (50 mV), possibly due to the electrostatic interaction between the heme iron and the tetrazole group. |
T9 |
803-1001 |
Sentence |
denotes |
The ferrous deoxy form of Tet-Mb was rapidly oxidized to its ferric form in the reaction with O2 at room temperature through an intermediary formation of its oxy form and with the generation of O2-. |
T10 |
1002-1247 |
Sentence |
denotes |
The oxy form of Tet-Mb can be detected by the optical spectral measurement at -12 degrees C, the rapid scan measurement at room temperature, and the electron spin resonance measurement of its cobalt-substituted derivative (Tet-Mb(Co2+)) at 77 K. |
T11 |
1248-1553 |
Sentence |
denotes |
In the kinetic measurement of the O2 binding reaction to Tet-Mb, its association and dissociation rate constants in the bimolecular reaction were 6.1 x 10(7) M-1 s-1 and 2200 s-1, respectively, showing that the tetrazole modification of His-64 extremely accelerates its association and dissociation rates. |
T12 |
1554-1776 |
Sentence |
denotes |
Taken together with the extremely fast autoxidation rate (53 h-1) obtained, these kinetic results suggested that the channel of O2 from the solvent region to the protein interior is open enough to pass the external ligand. |
T13 |
1777-1849 |
Sentence |
denotes |
The structure is discussed in relation to those of some genetic mutants. |
T14 |
1850-2057 |
Sentence |
denotes |
Taking these properties, we demonstrated that Tet-Mb can catalyze O2 consumption to generate O2-, coupled with the NADH-supported enzymatic reduction system of cytochrome P-450cam under an aerobic condition. |