来自红藻紫菜的铁氧化还原蛋白。

Ferredoxin from a red alga, Porphyra umbilicalis.

作者信息

Andrew P W, Rogers L J, Boulter D, Haslett B G

出版信息

Eur J Biochem. 1976 Oct 1;69(1):243-8. doi: 10.1111/j.1432-1033.1976.tb10879.x.

DOI:10.1111/j.1432-1033.1976.tb10879.x

Abstract

A plant-algal type ferredoxin was isolated from the red alga, Porphyra umbilicalis. In its oxidised form the ferredoxin had absorption maxima at 277, (281), 323, 420 and 462 nm. Two atoms each of non-haem iron and labile sulphur were present per molecule protein. The midpoint potential of the protein was -400 mV and it effectively mediated electron transport in the NADP-photoreduction system of barley. The amino acid composition of Porphyra umbilicalis ferredoxin was determined as (Lys4, His2, Arg1, Asx10, Thr8, Ser7, Glx16-17, Pro3, Gly7, Ala8, Cys5, Val6, Met1, Ile5, Leu8, Tyr5, Phe2). The minimum molecular weight of approximately 11000 was confirmed by sedimentation-equilibrium studies in the analytical ultracentrifuge. Approaching half of the total amino acid sequence was determined by means of an automatic sequencer.

摘要

从红藻紫菜中分离出一种植物-藻类型铁氧化还原蛋白。氧化态的铁氧化还原蛋白在277、（281）、323、420和462纳米处有吸收最大值。每个蛋白质分子含有两个非血红素铁原子和两个不稳定硫原子。该蛋白质的中点电位为-400毫伏，它在大麦的NADP光还原系统中有效地介导电子传递。紫菜铁氧化还原蛋白的氨基酸组成确定为（赖氨酸4、组氨酸2、精氨酸1、天冬氨酸10、苏氨酸8、丝氨酸7、谷氨酰胺16 - 17、脯氨酸3、甘氨酸7、丙氨酸8、半胱氨酸5、缬氨酸6、甲硫氨酸1、异亮氨酸5、亮氨酸8、酪氨酸5、苯丙氨酸2）。通过分析超速离心机中的沉降平衡研究证实其最小分子量约为11000。通过自动测序仪测定了大约一半的总氨基酸序列。