Proton magnetic resonance study of the histidine residues of sperm whale and horse myoglobins

Jack S. Cohen; Hanspaul Hagenmaier; Harvey Pollard; Alan N. Schechter

doi:10.1016/0022-2836(72)90367-1

Proton magnetic resonance study of the histidine residues of sperm whale and horse myoglobins

Jack S. Cohen
, Hanspaul Hagenmaier
, Harvey Pollard
, Alan N. Schechter

Research output: Contribution to journal › Article › peer-review

19 Scopus citations

Abstract

A 220 MHz proton magnetic resonance study of the downfield (7 to 9 p.p.m.) region of two metmyoglobins as a function of pH reveals seven titrating histidine C(2) protons in sperm whale and six in horse heart myoglobin. Comparison between the results for these two proteins and the use of computer curve-fitting facilitates the determination of the continuities of the titration curves and the apparent ionization constants. One titration curve in each case is shifted upfield relative to the other curves and has a much higher pK_a value (8·05 in sperm whale metmyoglobin). Possible assignments of the resonances are discussed from the consideration of the environments of the histidine residues in the X-ray structure of sperm whale myoglobin.

Original language	English
Pages (from-to)	513-519
Number of pages	7
Journal	Journal of Molecular Biology
Volume	71
Issue number	2
DOIs	https://doi.org/10.1016/0022-2836(72)90367-1
State	Published - 14 Nov 1972

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title = "Proton magnetic resonance study of the histidine residues of sperm whale and horse myoglobins",

abstract = "A 220 MHz proton magnetic resonance study of the downfield (7 to 9 p.p.m.) region of two metmyoglobins as a function of pH reveals seven titrating histidine C(2) protons in sperm whale and six in horse heart myoglobin. Comparison between the results for these two proteins and the use of computer curve-fitting facilitates the determination of the continuities of the titration curves and the apparent ionization constants. One titration curve in each case is shifted upfield relative to the other curves and has a much higher pKa value (8·05 in sperm whale metmyoglobin). Possible assignments of the resonances are discussed from the consideration of the environments of the histidine residues in the X-ray structure of sperm whale myoglobin.",

author = "Cohen, \{Jack S.\} and Hanspaul Hagenmaier and Harvey Pollard and Schechter, \{Alan N.\}",

note = "Funding Information: t Visiting Scientist from Lehrstuhl fiic Organische Chemie, UniversitBt Tiibingen, Tiibingen, Germany; supported by Deutsche Forschungs-gemeinsch.",

year = "1972",

month = nov,

day = "14",

doi = "10.1016/0022-2836(72)90367-1",

language = "English",

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T1 - Proton magnetic resonance study of the histidine residues of sperm whale and horse myoglobins

AU - Cohen, Jack S.

AU - Hagenmaier, Hanspaul

AU - Pollard, Harvey

AU - Schechter, Alan N.

N1 - Funding Information: t Visiting Scientist from Lehrstuhl fiic Organische Chemie, UniversitBt Tiibingen, Tiibingen, Germany; supported by Deutsche Forschungs-gemeinsch.

PY - 1972/11/14

Y1 - 1972/11/14

N2 - A 220 MHz proton magnetic resonance study of the downfield (7 to 9 p.p.m.) region of two metmyoglobins as a function of pH reveals seven titrating histidine C(2) protons in sperm whale and six in horse heart myoglobin. Comparison between the results for these two proteins and the use of computer curve-fitting facilitates the determination of the continuities of the titration curves and the apparent ionization constants. One titration curve in each case is shifted upfield relative to the other curves and has a much higher pKa value (8·05 in sperm whale metmyoglobin). Possible assignments of the resonances are discussed from the consideration of the environments of the histidine residues in the X-ray structure of sperm whale myoglobin.

AB - A 220 MHz proton magnetic resonance study of the downfield (7 to 9 p.p.m.) region of two metmyoglobins as a function of pH reveals seven titrating histidine C(2) protons in sperm whale and six in horse heart myoglobin. Comparison between the results for these two proteins and the use of computer curve-fitting facilitates the determination of the continuities of the titration curves and the apparent ionization constants. One titration curve in each case is shifted upfield relative to the other curves and has a much higher pKa value (8·05 in sperm whale metmyoglobin). Possible assignments of the resonances are discussed from the consideration of the environments of the histidine residues in the X-ray structure of sperm whale myoglobin.

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U2 - 10.1016/0022-2836(72)90367-1

DO - 10.1016/0022-2836(72)90367-1

M3 - Article

C2 - 4635996

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JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

IS - 2

ER -

Proton magnetic resonance study of the histidine residues of sperm whale and horse myoglobins

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