OXYGEN DIFFUSION THROUGH HORSERADISH-PEROXIDASE

被引：9
|
作者：
BRUNET, JE [1 ]
JULLIAN, C [1 ]
JAMESON, DM [1 ]
机构：
[1] UNIV HAWAII, JOHN A BURNS SCH MED, DEPT BIOCHEM & BIOPHYS, 1960 E W RD, HONOLULU, HI 96822 USA
来源：
PHOTOCHEMISTRY AND PHOTOBIOLOGY | 1990年 / 51卷 / 04期
关键词：
D O I：
10.1111/j.1751-1097.1990.tb01742.x
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Abstract— The quenching by molecular oxygen of the fluorescence from a protoporphyrin IX adduct of horseradish peroxidase has been investigated using both intensity and time‐resolved techniques. The bimolecular quenching rate constant determined for this process, as evaluated by the conventional Stern‐Volmer analysis, was 2 × 108 M−1 s−1, among the lowest observed for protein systems. This result suggests that the heme binding site in horseradish peroxidase is relatively inaccessible to oxygen, which may account for the observation of room temperature phosphorescence in aerated solutions from enzymatically created triplet states. Copyright © 1990, Wiley Blackwell. All rights reserved
引用
收藏
页码：487 / 489
页数：3
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