Chloride acts as a novel negative heterotropic effector of hemoglobin Rothschild (beta 37 Trp-->Arg) in solution.
Chloride acts as a novel negative heterotropic effector of hemoglobin Rothschild (beta 37 Trp-->Arg) in solution.
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氯化物在溶液中充当罗斯柴尔德血红蛋白（β 37 Trp-->Arg）的新型负异向效应子。
DOI：
10.1021/bi00180a033
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发表时间：
1994
期刊：
影响因子：
2.9
通讯作者：
Noble,RW
中科院分区：
文献类型：
--
作者：
Kelly,RM;Hui,HL;Noble,RW
用停流技术研究了氯离子浓度对一氧化碳与人血红蛋白A和突变型血红蛋白Rothschild(/337Trp-Arg)结合速率常数的影响。以前对在T状态结晶的血红蛋白Rothschild的结构[Kavanaugh等人(1992)生物化学37,4111]和功能性质[Rivetti等人(1993)生物化学32,2888]的研究表明，突变的精氨酸残基创建了新的氯离子结合部位，氯离子作用于降低这些晶体中Hb Rothschild的氧亲和力。这里报道的研究表明，氯离子对溶液中CO与脱氧血红蛋白Rothschild的结合速率有平行的影响。尽管CO与该血红蛋白在溶液中的结合动力学表现为玻尔效应，但氯化物效应与pH无关。最近Rivetti等人(1993A)和Mozzarelli等人(1991)在血红蛋白晶体上的工作首次获得了关于血红蛋白在晶态下的功能性质的信息。这些研究人员发现，在聚乙二醇1中生长的脱氧人血红蛋白A(HBA)1晶体可以通过增加聚乙二醇1的浓度来充分稳定，从而在不破坏晶体结构的情况下实现可逆氧结合。因此，可以测量四元T态血红蛋白晶体上氧结合的平衡。这是第一次有可能测量结晶学确定的血红蛋白结构的功能性质，并确定结晶状态下的性质是否与溶液中同等结构状态下的性质显著不同。
The effects of chloride ion concentration on the rate constants for association of carbon monoxide with human hemoglobin A and a synthetic form of the mutant hemoglobin Rothschild (/337 Trp—Arg) have been investigated by stopped-flow techniques. Previous studies of the structure [Kavanaugh et al.(1992) Biochemistry 37, 4111] and functional properties [Rivetti et al.(1993) Biochemistry 32, 2888] of hemoglobin Rothschild crystallized in the T state have demonstrated that the mutant arginine residues create new chloride ion binding sites and that chloride ions act to lower the oxygen affinity of hemoglobin Rothschild in these crystals. The studies reported here demonstrate a parallel effect of chloride ions on the rate of CO association with deoxygenated hemoglobin Rothschild in solution. Although the kinetics of CO binding to this hemoglobin in solutionexhibit a Bohr effect, the chloride effect is independent of pH. In addition, we find that other halide ions have similar effects on the rate constants for the association of CO with this hemoglobin variant.Recent work on hemoglobin crystals by Rivetti et al.(1993a) and Mozzarelli et al.(1991) has yielded the first information about the functional properties of hemoglobin in the crystalline state. These investigators discovered that crystals of deoxygenated human hemoglobin A (HbA) 1grown in poly (ethylene glycol)(PEG) 1 could be sufficiently stabilized by increasing the PEG concentration topermit reversible oxygen binding without disruption of the crystal structure. As a result, the equilibrium of oxygen binding to crystals of hemoglobin in the quaternary T state could be measured. For the first time it was possible to measure the functional properties of a crystallographically determined structure of hemoglobin and to ascertain if the propertiesexhibited in the crystalline state differ significantly from those attributed to the equivalent structural state in solution.
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影响因子：
64.8
作者：
MOZZARELLI, A;RIVETTI, C;EATON, WA
通讯作者：
EATON, WA
由重组突变β-珠蛋白合成的人血红蛋白的功能特性。
影响因子：
2.9
作者：
Doyle,ML;Lew,G;DeYoung,A;Kwiatkowski,L;Wierzba,A;Noble,RW;Ackers,GK
通讯作者：
Ackers,GK
快速灵敏的分光光度测定仪器。
影响因子：
4.1
作者：
Q. Gibson;L. Milnes
通讯作者：
L. Milnes
α 链和 β 链对氧与血红蛋白结合和解离动力学的贡献
DOI：
--
发表时间：
1973
期刊：
影响因子：
--
作者：
Q. Gibson
通讯作者：
Q. Gibson
人血红蛋白α链和β链的制备及其性质
DOI：
--
发表时间：
1969
期刊：
影响因子：
--
作者：
G. Geraci;L. Parkhurst;Q. Gibson
通讯作者：
Q. Gibson