血红蛋白A血红素口袋中变构响应性不稳定质子交换率的核磁共振研究。
NMR study of the exchange rates of allosterically responsive labile protons in the heme pockets of hemoglobin A.
作者信息
Jue T, La Mar G N, Han K, Yamamoto Y
出版信息
Biophys J. 1984 Jul;46(1):117-20. doi: 10.1016/S0006-3495(84)84004-7.
Abstract
1H NMR spectroscopy has been used to measure the proximal histidyl labile ring proton (NH) rates of exchange with bulk solvent in the individual subunits of hemoglobin (Hb) A. These protons displayed a substantial decrease in their exchange rates in comparison with related monomeric proteins and exhibited sensitivity to the quarternary state. With the beta subunit NH, the exchange behaviour was similar to an allosterically responsive subset of protons, which have been identified using 1H-3H methods (Englander, J.J., R. Rogero, and S. W. Englander, 1983, J. Mol. Biol. 169:325-344). Assuming similar exchange mechanisms for the two subunits, the NMR data suggested a more flexible alpha than beta subunit in Hb A.
摘要
1H核磁共振光谱已被用于测量血红蛋白（Hb）A各个亚基中近端组氨酸不稳定环质子（NH）与大量溶剂的交换速率。与相关单体蛋白相比，这些质子的交换速率大幅降低，并对四级结构状态敏感。对于β亚基的NH，其交换行为类似于使用1H-3H方法鉴定的质子的变构响应子集（英格兰德，J.J.，R.罗赫罗，和S.W.英格兰德，1983，《分子生物学杂志》169:325 - 344）。假设两个亚基的交换机制相似，核磁共振数据表明Hb A中的α亚基比β亚基更灵活。
相似文献
1
NMR study of the exchange rates of allosterically responsive labile protons in the heme pockets of hemoglobin A.血红蛋白A血红素口袋中变构响应性不稳定质子交换率的核磁共振研究。
Biophys J. 1984 Jul;46(1):117-20. doi: 10.1016/S0006-3495(84)84004-7.
2
Proton magnetic resonance study of the influence of chemical modification, mutation, quaternary state, and ligation state on dynamic stability of the heme pocket in hemoglobin as reflected in the exchange of the proximal histidyl ring labile proton.
Biochemistry. 1989 Mar 7;28(5):2169-70. doi: 10.1021/bi00431a031.
3
Nuclear magnetic resonance study of the isotope exchange of the proximal histidyl ring labile protons in hemoglobin A. The exchange rates and mechanisms of individual subunits in deoxy and oxy-hemoglobin.血红蛋白A中近端组氨酸环不稳定质子的同位素交换的核磁共振研究。脱氧血红蛋白和氧合血红蛋白中各个亚基的交换速率及机制。
J Mol Biol. 1986 Jun 5;189(3):541-52. doi: 10.1016/0022-2836(86)90323-2.
4
A proton nuclear magnetic resonance investigation of proximal histidyl residues in human normal and abnormal hemoglobins. A probe for the heme pocket.对人正常和异常血红蛋白中近端组氨酸残基的质子核磁共振研究。血红素口袋的一种探针。
Biophys J. 1982 Jul;39(1):33-40. doi: 10.1016/S0006-3495(82)84487-1.
5
Proton magnetic resonance study of the influence of heme 2,4 substituents on the exchange rates of labile protons in the heme pocket of myoglobin.关于血红素2,4位取代基对肌红蛋白血红素口袋中不稳定质子交换速率影响的质子磁共振研究。
Biophys J. 1983 Nov;44(2):177-83. doi: 10.1016/S0006-3495(83)84289-1.
6
Assessment of role of beta 146-histidyl and other histidyl residues in the Bohr effect of human normal adult hemoglobin.评估β146-组氨酰及其他组氨酰残基在成人正常血红蛋白玻尔效应中的作用。
Biochemistry. 1986 Apr 8;25(7):1706-16. doi: 10.1021/bi00355a040.
7
Proton magnetic resonance characterization of the dynamic stability of the heme pocket in myoglobin by the exchange behavior of the labile proton of the proximal histidyl imidazole.通过近端组氨酸咪唑的不稳定质子的交换行为对肌红蛋白中血红素口袋动态稳定性进行质子磁共振表征。
Biophys J. 1981 May;34(2):217-26. doi: 10.1016/S0006-3495(81)84846-1.
8
9
Proton NMR investigation of the influence of subunit assembly on the low-spin in equilibrium high-spin equilibrium of met-azido hemoglobin A.
Biochim Biophys Acta. 1989 Jul 6;996(3):187-94. doi: 10.1016/0167-4838(89)90246-x.
10
Proton nuclear Overhauser effect investigation of the heme pockets in ligated hemoglobin: conformational differences between oxy and carbonmonoxy forms.
Biochemistry. 1985 Jul 2;24(14):3398-407. doi: 10.1021/bi00335a003.
引用本文的文献
1
Myoglobin and hemoglobin rotational diffusion in the cell.细胞中的肌红蛋白和血红蛋白旋转扩散
Biophys J. 1997 Nov;73(5):2764-70. doi: 10.1016/S0006-3495(97)78305-X.
本文引用的文献
1
STUDIES ON THE STRUCTURE OF HEMOGLOBIN. III. PHYSICOCHEMICAL PROPERTIES OF RECONSTITUTED HEMOGLOBINS.
Biochim Biophys Acta. 1964 Mar 30;79:284-92. doi: 10.1016/0926-6577(64)90009-9.
2
Structure and refinement of oxymyoglobin at 1.6 A resolution.分辨率为1.6埃的氧合肌红蛋白的结构与精修
J Mol Biol. 1980 Oct 5;142(4):531-54. doi: 10.1016/0022-2836(80)90262-4.
3
Assignment of proximal histidyl imidazole exchangeable proton NMR resonances to individual subunits in hemoglobins A, Boston, Iwate and Milwaukee.
Biochem Biophys Res Commun. 1980 Oct 16;96(3):1172-7. doi: 10.1016/0006-291x(80)90075-3.
4
The slowest allosterically responsive hydrogens in hemoglobin. Completion of the hydrogen exchange survey.
J Biol Chem. 1980 Nov 25;255(22):10695-701.
5
Individual breathing reactions measured in hemoglobin by hydrogen exchange methods.通过氢交换法在血红蛋白中测量的个体呼吸反应。
Biophys J. 1980 Oct;32(1):577-89. doi: 10.1016/S0006-3495(80)84991-5.
6
Proton magnetic resonance characterization of the dynamic stability of the heme pocket in myoglobin by the exchange behavior of the labile proton of the proximal histidyl imidazole.通过近端组氨酸咪唑的不稳定质子的交换行为对肌红蛋白中血红素口袋动态稳定性进行质子磁共振表征。
Biophys J. 1981 May;34(2):217-26. doi: 10.1016/S0006-3495(81)84846-1.
7
The internal dynamics of globular proteins.球状蛋白质的内部动力学。
CRC Crit Rev Biochem. 1981;9(4):293-349. doi: 10.3109/10409238109105437.
8
9
Proton magnetic resonance study of the influence of heme 2,4 substituents on the exchange rates of labile protons in the heme pocket of myoglobin.关于血红素2,4位取代基对肌红蛋白血红素口袋中不稳定质子交换速率影响的质子磁共振研究。
Biophys J. 1983 Nov;44(2):177-83. doi: 10.1016/S0006-3495(83)84289-1.
10
Identification of an allosterically sensitive unfolding unit in hemoglobin.血红蛋白中变构敏感解折叠单元的鉴定。
J Mol Biol. 1983 Sep 5;169(1):325-44. doi: 10.1016/s0022-2836(83)80186-7.
Zotero 插件