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2
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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。
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本文引用的文献

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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.
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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.
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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.
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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。
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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.
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Proton NMR study of yellowfin tuna myoglobin in whole muscle and solution. Evidence for functional metastable protein forms involving heme orientational disorder.
J Biol Chem. 1985 Nov 5;260(25):13694-8.
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.
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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。
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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.

DOI:10.1042/bj2460787
PMID:3689333
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1148347/
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。