两种肌红蛋白中的血液疾病：重定向速率的比较
Haem disorder in two myoglobins: comparison of reorientation rate.
作者信息
Bellelli A, Foon R, Ascoli F, Brunori M
机构信息
Dipartimento di Scienze Biochimiche, Università La Sapienza, Roma, Italy.
出版信息
Biochem J. 1987 Sep 15;246(3):787-9. doi: 10.1042/bj2460787.
Abstract
The globins from sperm whale and from Aplysia limacina myoglobins were reconstituted by addition of stoichiometric ferric protohaem and the Soret c.d. was followed as a function of time. For both reconstituted proteins, the Soret c.d. changes with time, reflecting haem reorientation inside its pocket, as previously described [Aojula, Wilson & Drake (1986) Biochem. J. 237, 613-616] for sperm whale myoglobin. The time course of the c.d. transition is found to be approx. 10 times faster in Aplysia than in sperm whale myoglobin, a result which is in agreement with the known structural and physicochemical properties of the two myoglobins; furthermore, these results confirm that c.d. and n.m.r. data on haem orientation in haemoproteins reflect the same molecular phenomenon.
摘要
通过添加化学计量的高铁原卟啉来重构抹香鲸和海兔肌红蛋白的珠蛋白，并跟踪索雷特圆二色性随时间的变化。对于这两种重构蛋白，索雷特圆二色性随时间变化，反映了血红素在其口袋内的重新取向，如先前针对抹香鲸肌红蛋白所描述的那样[Aojula、Wilson和Drake（1986年），《生物化学杂志》237卷，613 - 616页]。发现圆二色性转变的时间进程在海兔中比在抹香鲸肌红蛋白中快约10倍，这一结果与两种肌红蛋白已知的结构和物理化学性质一致；此外，这些结果证实了关于血红素蛋白中血红素取向的圆二色性和核磁共振数据反映了相同的分子现象。
相似文献
1
Haem disorder in two myoglobins: comparison of reorientation rate.两种肌红蛋白中的血液疾病：重定向速率的比较
Biochem J. 1987 Sep 15;246(3):787-9. doi: 10.1042/bj2460787.
2
1H-n.m.r. and c.d. studies of haem orientational disorder in sperm-whale myoglobin and human haemoglobin.对抹香鲸肌红蛋白和人血红蛋白中血红素取向无序的1H-核磁共振和圆二色性研究。
Biochem J. 1988 Mar 15;250(3):853-8. doi: 10.1042/bj2500853.
3
Transient spectroscopy of the reaction of cyanide with ferrous myoglobin. Effect of distal side residues.氰化物与亚铁肌红蛋白反应的瞬态光谱。远端侧残基的影响。
J Biol Chem. 1990 Nov 5;265(31):18898-901.
4
Crystal structures of modified myoglobins. I. Heme orientation and structural changes around heme in myoglobins reconstituted with isopemptoheme, pemptoheme, 2-ethyldeuteroheme, and 4-ethyldeuteroheme.
J Biochem. 1986 Aug;100(2):269-76. doi: 10.1093/oxfordjournals.jbchem.a121712.
5
Aplysia myoglobins with an unusual amino acid sequence.
J Mol Biol. 1984 Dec 25;180(4):1179-84. doi: 10.1016/0022-2836(84)90277-8.
6
Proton nuclear magnetic resonance study of the molecular and electronic structure of the heme cavity in Aplysia cyanometmyoglobin.海兔氰化高铁肌红蛋白血红素腔分子与电子结构的质子核磁共振研究
Biochemistry. 1989 May 30;28(11):4880-7. doi: 10.1021/bi00437a053.
7
Trimethylphosphine binding to horse-heart and sperm-whale myoglobins. Kinetics, proton magnetic resonance assignment and nuclear Overhauser effect investigation of the heme pocket.三甲基膦与马心脏肌红蛋白和抹香鲸肌红蛋白的结合。血红素口袋的动力学、质子磁共振归属及核Overhauser效应研究。
Eur J Biochem. 1993 Jun 1;214(2):405-14. doi: 10.1111/j.1432-1033.1993.tb17936.x.
8
Functional consequences of haem orientational disorder in sperm-whale and yellow-fin-tuna myoglobins.抹香鲸和黄鳍金枪鱼肌红蛋白中血红素取向紊乱的功能后果。
Biochem J. 1987 Apr 1;243(1):205-10. doi: 10.1042/bj2430205.
9
NMR study of the molecular and electronic structure of the heme cavity of Aplysia metmyoglobin. Resonance assignments based on isotope labeling and proton nuclear Overhauser effect measurements.海兔高铁肌红蛋白血红素腔的分子和电子结构的核磁共振研究。基于同位素标记和质子核Overhauser效应测量的共振归属。
Biochemistry. 1986 Sep 23;25(19):5638-46. doi: 10.1021/bi00367a044.
10
Oxygenation and EPR spectral properties of Aplysia myoglobins containing cobaltous porphyrins.含钴卟啉的海兔肌红蛋白的氧合作用及电子顺磁共振光谱特性
Biochim Biophys Acta. 1978 Mar 28;533(1):173-80. doi: 10.1016/0005-2795(78)90561-5.
引用本文的文献
1
Resonance Raman interrogation of the consequences of heme rotational disorder in myoglobin and its ligated derivatives.共振拉曼光谱法研究肌红蛋白及其配位衍生物中血红素旋转无序的后果。
Biochemistry. 2008 Dec 2;47(48):12869-77. doi: 10.1021/bi801779d.
2
1H-NMR study of the effect of temperature through reversible unfolding on the heme pocket molecular structure and magnetic properties of aplysia limacina cyano-metmyoglobin.通过可逆去折叠研究温度对海兔氰化高铁肌红蛋白血红素口袋分子结构和磁性的影响的1H核磁共振研究
Biophys J. 2005 Dec;89(6):4149-58. doi: 10.1529/biophysj.105.062398. Epub 2005 Sep 8.
3
Properties of a recombinant human hemoglobin with aspartic acid 99(beta), an important intersubunit contact site, substituted by lysine.一种重组人血红蛋白的特性，其99位（β链）天冬氨酸（一个重要的亚基间接触位点）被赖氨酸取代。
Protein Sci. 1994 Aug;3(8):1213-23. doi: 10.1002/pro.5560030807.
4
Haem-binding-site heterogeneity and haem Cotton effects of Glycera dibranchiata monomeric haemoglobins.双吻前口虫单体血红蛋白的血红素结合位点异质性和血红素科顿效应
Biochem J. 1989 Jun 15;260(3):863-71. doi: 10.1042/bj2600863.
5
Complete sequence-specific 1H NMR resonance assignment of hyperfine-shifted residues in the active site of a paramagnetic protein: application to Aplysia cyano-metmyoglobin.顺磁蛋白活性位点中超精细位移残基的完整序列特异性 1H NMR 共振归属：应用于海兔氰化高铁肌红蛋白
J Biomol NMR. 1992 Nov;2(6):597-618. doi: 10.1007/BF02192849.
本文引用的文献
1
Kinetic studies on the reaction between native globin and haem derivatives.天然球蛋白与血红素衍生物之间反应的动力学研究。
Biochem J. 1960 Nov;77(2):328-41. doi: 10.1042/bj0770328.
2
Studies on the structure of hemoglobin. I. Physicochemical properties of human globin.血红蛋白结构研究。I. 人珠蛋白的物理化学性质。
Biochim Biophys Acta. 1958 Dec;30(3):608-15. doi: 10.1016/0006-3002(58)90108-2.
3
A new type of myoglobin isolated and crystallized from the muscles of Aplysiae.从海兔肌肉中分离并结晶出的一种新型肌红蛋白。
Biokhimiia. 1957 Jan-Feb;22(1-2):336-44.
4
Preparation and properties of apohemoglobin and reconstituted hemoglobins.脱辅基血红蛋白及重组血红蛋白的制备与性质
Methods Enzymol. 1981;76:72-87. doi: 10.1016/0076-6879(81)76115-9.
5
Haem disorder in reconstituted human haemoglobin.重组人血红蛋白中的血液疾病。
Biochem J. 1982 Dec 1;207(3):583-7. doi: 10.1042/bj2070583.
6
Heme orientational disorder in reconstituted and native sperm whale myoglobin. Proton nuclear magnetic resonance characterizations by heme methyl deuterium labeling in the Met-cyano protein.重组和天然抹香鲸肌红蛋白中的血红素取向紊乱。通过甲硫氨酸氰基蛋白中的血红素甲基氘标记进行质子核磁共振表征。
J Mol Biol. 1983 Aug 25;168(4):887-96. doi: 10.1016/s0022-2836(83)80080-1.
7
Fluorescence studies of Aplysia and sperm whale apomyoglobins.海兔和抹香鲸脱辅基肌红蛋白的荧光研究。
Biochemistry. 1970 Nov 24;9(24):4723-9. doi: 10.1021/bi00826a015.
8
9
Crystal structure of ferric Aplysia limacina myoglobin at 2 X 0 A resolution.海兔肌红蛋白铁（Ⅲ）在2.0 Å分辨率下的晶体结构。
J Mol Biol. 1985 May 5;183(1):113-5. doi: 10.1016/0022-2836(85)90285-2.
10
Estimation of the polarity of the protein interior by optical spectroscopy.通过光谱学估算蛋白质内部的极性。
Nature. 1986;319(6048):70-3. doi: 10.1038/319070a0.
Zotero 插件