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ALTERATION OF AXIAL COORDINATION BY PROTEIN ENGINEERING IN MYOGLOBIN - BISIMIDAZOLE LIGATION IN THE HIS(64)-]VAL/VAL(68)-]HIS DOUBLE MUTANT

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ALTERATION OF AXIAL COORDINATION BY PROTEIN ENGINEERING IN MYOGLOBIN - BISIMIDAZOLE LIGATION IN THE HIS(64)-]VAL/VAL(68)-]HIS DOUBLE MUTANT. / DOU, Y ; ADMIRAAL, S J ; IKEDASAITO, M ; KRZYWDA, S ; WILKINSON, A J ; LI, T S ; OLSON, J S ; PRINCE, R C ; PICKERING, I J ; GEORGE, G N .

In: Journal of Biological Chemistry, Vol. 270, No. 27, 07.07.1995, p. 15993-16001.

Research output: Contribution to journalArticle

Harvard

DOU, Y, ADMIRAAL, SJ, IKEDASAITO, M, KRZYWDA, S, WILKINSON, AJ, LI, TS, OLSON, JS, PRINCE, RC, PICKERING, IJ & GEORGE, GN 1995, 'ALTERATION OF AXIAL COORDINATION BY PROTEIN ENGINEERING IN MYOGLOBIN - BISIMIDAZOLE LIGATION IN THE HIS(64)-]VAL/VAL(68)-]HIS DOUBLE MUTANT', Journal of Biological Chemistry, vol. 270, no. 27, pp. 15993-16001.

APA

DOU, Y., ADMIRAAL, S. J., IKEDASAITO, M., KRZYWDA, S., WILKINSON, A. J., LI, T. S., ... GEORGE, G. N. (1995). ALTERATION OF AXIAL COORDINATION BY PROTEIN ENGINEERING IN MYOGLOBIN - BISIMIDAZOLE LIGATION IN THE HIS(64)-]VAL/VAL(68)-]HIS DOUBLE MUTANT. Journal of Biological Chemistry, 270(27), 15993-16001.

Vancouver

DOU Y, ADMIRAAL SJ, IKEDASAITO M, KRZYWDA S, WILKINSON AJ, LI TS et al. ALTERATION OF AXIAL COORDINATION BY PROTEIN ENGINEERING IN MYOGLOBIN - BISIMIDAZOLE LIGATION IN THE HIS(64)-]VAL/VAL(68)-]HIS DOUBLE MUTANT. Journal of Biological Chemistry. 1995 Jul 7;270(27):15993-16001.

Author

DOU, Y ; ADMIRAAL, S J ; IKEDASAITO, M ; KRZYWDA, S ; WILKINSON, A J ; LI, T S ; OLSON, J S ; PRINCE, R C ; PICKERING, I J ; GEORGE, G N . / ALTERATION OF AXIAL COORDINATION BY PROTEIN ENGINEERING IN MYOGLOBIN - BISIMIDAZOLE LIGATION IN THE HIS(64)-]VAL/VAL(68)-]HIS DOUBLE MUTANT. In: Journal of Biological Chemistry. 1995 ; Vol. 270, No. 27. pp. 15993-16001.

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@article{8ef6492e12814e57996de97bcaee6465,
title = "ALTERATION OF AXIAL COORDINATION BY PROTEIN ENGINEERING IN MYOGLOBIN - BISIMIDAZOLE LIGATION IN THE HIS(64)-]VAL/VAL(68)-]HIS DOUBLE MUTANT",
abstract = "Pig and human myoglobin have been engineered to reverse the positions of the distal histidine and valine (i.e. His(64)(E7) --> Val and Val(68)(E11) --> His). Spectroscopic and ligand binding properties have been measured for human and pig H64V/V68H myoglobin, and the structure of the pig H64V/V68H double mutant has been determined to 2.07-Angstrom resolution by x-ray crystallography. The crystal structure shows that the N-epsilon of His(68) is located 2.3 Angstrom away from the heme iron, resulting in the formation of a hexacoordinate species, The imidazole plane of His(68) is tilted relative to the heme normal; moreover it is not parallel to that of His(93), in agreement with our previous proposal (Qin, J,, La Mar, G. N., Dou, Y,, Admiraal, S. J., and Ikeda-Saito, M. (1994) J. Biol. Chem. 269, 1083-1090). At cryogenic temperatures, the heme iron is in a low spin state, which exhibits a highly anisotropic EPR spectrum (g(1) = 3.34, g(2) = 2.0, and g(3) < 1), quite different from that of the imidazole complex of metmyoglobin. The mean iron-nitrogen distance is 2.01 Angstrom for the low spin ferric state as determined by x-ray spectroscopy, The ferrous form of H64V/V68H myoglobin shows an optical spectrum that is similar to that of b-type cytochromes and consistent with the hexacoordinate bisimidazole hemin structure determined by the x-ray crystallography, The double mutation lowers the ferric/ferrous couple midpoint potential from +54 mV of the wild-type protein to -128 mV. Ferrous H64V/V68H myoglobin binds CO and NO to form stable complexes, but its reaction with O-2 results in a rapid autooxidation to the ferric species. All of these results demonstrate that the three-dimensional positions of His(64) and Val(68) in the wild-type myoglobin are as important as the chemical nature of the side chains in facilitating reversible O-2 binding and inhibiting autooxidation.",
keywords = "SPERM WHALE MYOGLOBIN, SITE-DIRECTED MUTAGENESIS, ELECTRON-PARAMAGNETIC-RES, ABSORPTION FINE-STRUCTURE, DISTAL HISTIDINE MUTANTS, LIGAND-BINDING, INFRARED-SPECTROSCOPY, ESCHERICHIA-COLI, POCKET POLARITY, CARBON-MONOXIDE",
author = "Y DOU and ADMIRAAL, {S J} and M IKEDASAITO and S KRZYWDA and WILKINSON, {A J} and LI, {T S} and OLSON, {J S} and PRINCE, {R C} and PICKERING, {I J} and GEORGE, {G N}",
year = "1995",
month = "7",
day = "7",
language = "English",
volume = "270",
pages = "15993--16001",
journal = "The Journal of biological chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "27",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - ALTERATION OF AXIAL COORDINATION BY PROTEIN ENGINEERING IN MYOGLOBIN - BISIMIDAZOLE LIGATION IN THE HIS(64)-]VAL/VAL(68)-]HIS DOUBLE MUTANT

AU - DOU, Y

AU - ADMIRAAL, S J

AU - IKEDASAITO, M

AU - KRZYWDA, S

AU - WILKINSON, A J

AU - LI, T S

AU - OLSON, J S

AU - PRINCE, R C

AU - PICKERING, I J

AU - GEORGE, G N

PY - 1995/7/7

Y1 - 1995/7/7

N2 - Pig and human myoglobin have been engineered to reverse the positions of the distal histidine and valine (i.e. His(64)(E7) --> Val and Val(68)(E11) --> His). Spectroscopic and ligand binding properties have been measured for human and pig H64V/V68H myoglobin, and the structure of the pig H64V/V68H double mutant has been determined to 2.07-Angstrom resolution by x-ray crystallography. The crystal structure shows that the N-epsilon of His(68) is located 2.3 Angstrom away from the heme iron, resulting in the formation of a hexacoordinate species, The imidazole plane of His(68) is tilted relative to the heme normal; moreover it is not parallel to that of His(93), in agreement with our previous proposal (Qin, J,, La Mar, G. N., Dou, Y,, Admiraal, S. J., and Ikeda-Saito, M. (1994) J. Biol. Chem. 269, 1083-1090). At cryogenic temperatures, the heme iron is in a low spin state, which exhibits a highly anisotropic EPR spectrum (g(1) = 3.34, g(2) = 2.0, and g(3) < 1), quite different from that of the imidazole complex of metmyoglobin. The mean iron-nitrogen distance is 2.01 Angstrom for the low spin ferric state as determined by x-ray spectroscopy, The ferrous form of H64V/V68H myoglobin shows an optical spectrum that is similar to that of b-type cytochromes and consistent with the hexacoordinate bisimidazole hemin structure determined by the x-ray crystallography, The double mutation lowers the ferric/ferrous couple midpoint potential from +54 mV of the wild-type protein to -128 mV. Ferrous H64V/V68H myoglobin binds CO and NO to form stable complexes, but its reaction with O-2 results in a rapid autooxidation to the ferric species. All of these results demonstrate that the three-dimensional positions of His(64) and Val(68) in the wild-type myoglobin are as important as the chemical nature of the side chains in facilitating reversible O-2 binding and inhibiting autooxidation.

AB - Pig and human myoglobin have been engineered to reverse the positions of the distal histidine and valine (i.e. His(64)(E7) --> Val and Val(68)(E11) --> His). Spectroscopic and ligand binding properties have been measured for human and pig H64V/V68H myoglobin, and the structure of the pig H64V/V68H double mutant has been determined to 2.07-Angstrom resolution by x-ray crystallography. The crystal structure shows that the N-epsilon of His(68) is located 2.3 Angstrom away from the heme iron, resulting in the formation of a hexacoordinate species, The imidazole plane of His(68) is tilted relative to the heme normal; moreover it is not parallel to that of His(93), in agreement with our previous proposal (Qin, J,, La Mar, G. N., Dou, Y,, Admiraal, S. J., and Ikeda-Saito, M. (1994) J. Biol. Chem. 269, 1083-1090). At cryogenic temperatures, the heme iron is in a low spin state, which exhibits a highly anisotropic EPR spectrum (g(1) = 3.34, g(2) = 2.0, and g(3) < 1), quite different from that of the imidazole complex of metmyoglobin. The mean iron-nitrogen distance is 2.01 Angstrom for the low spin ferric state as determined by x-ray spectroscopy, The ferrous form of H64V/V68H myoglobin shows an optical spectrum that is similar to that of b-type cytochromes and consistent with the hexacoordinate bisimidazole hemin structure determined by the x-ray crystallography, The double mutation lowers the ferric/ferrous couple midpoint potential from +54 mV of the wild-type protein to -128 mV. Ferrous H64V/V68H myoglobin binds CO and NO to form stable complexes, but its reaction with O-2 results in a rapid autooxidation to the ferric species. All of these results demonstrate that the three-dimensional positions of His(64) and Val(68) in the wild-type myoglobin are as important as the chemical nature of the side chains in facilitating reversible O-2 binding and inhibiting autooxidation.

KW - SPERM WHALE MYOGLOBIN

KW - SITE-DIRECTED MUTAGENESIS

KW - ELECTRON-PARAMAGNETIC-RES

KW - ABSORPTION FINE-STRUCTURE

KW - DISTAL HISTIDINE MUTANTS

KW - LIGAND-BINDING

KW - INFRARED-SPECTROSCOPY

KW - ESCHERICHIA-COLI

KW - POCKET POLARITY

KW - CARBON-MONOXIDE

M3 - Article

VL - 270

SP - 15993

EP - 16001

JO - The Journal of biological chemistry

JF - The Journal of biological chemistry

SN - 0021-9258

IS - 27

ER -