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Liganded and unliganded forms of Antarctic fish haemoglobins in polyethylene glycol: crystallization of an R-state haemichrome intermediate.

作者信息

Riccio A, Vitagliano L, di Prisco G, Zagari A, Mazzarella L

机构信息

Istituto di Biochimica delle Proteine ed Enzimologia, CNR, Via Marconi 12, I-80125 Naples, Italy.

出版信息

Acta Crystallogr D Biol Crystallogr. 2001 Aug;57(Pt 8):1144-6. doi: 10.1107/s0907444901007739. Epub 2001 Jul 23.

DOI:10.1107/s0907444901007739
PMID:11468400
Abstract

Liganded and unliganded forms of two Antarctic fish haemoglobins, from Trematomus newnesi and T. bernacchii, have been crystallized in low-salt media using polyethylene glycol as precipitant. In particular, crystals of air-exposed T. newnesi carbomonoxy haemoglobin were found to be isomorphous to the crystals grown in high-salt media. Preliminary X-ray analysis of the diffraction data revealed that the beta-haem iron of this haemoglobin is in the haemichrome state, with both the proximal and distal histidyl residues linked to the iron. This is the first crystallization of a haemichrome intermediate of a vertebrate haemoglobin.

摘要

相似文献

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引用本文的文献

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2
The crystal structure of a tetrameric hemoglobin in a partial hemichrome state.处于部分半色素状态的四聚体血红蛋白的晶体结构。
Proc Natl Acad Sci U S A. 2002 Jul 23;99(15):9801-6. doi: 10.1073/pnas.132182099. Epub 2002 Jul 1.