CONFORMATIONAL RELAXATION OF A LOW-TEMPERATURE PROTEIN AS PROBED BY PHOTOCHEMICAL HOLE BURNING - HORSERADISH-PEROXIDASE

被引:47
作者
ZOLLFRANK, J
FRIEDRICH, J
VANDERKOOI, JM
FIDY, J
机构
[1] UNIV MAINZ,INST PHYS CHEM,W-6500 MAINZ,GERMANY
[2] UNIV PENN,DEPT BIOCHEM & BIOPHYS,PHILADELPHIA,PA 19104
基金
美国国家科学基金会;
关键词
D O I
10.1016/S0006-3495(91)82224-X
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
For the first time, conformational relaxation processes have been measured in a small protein, mesoporphyrin-horseradish peroxidase via their influence on spectral diffusion broadening of holes burnt in the fluorescence excitation spectrum of free base mesoporphyrin. Holes were burnt in three 0 <-- 0 bands of different tautomeric forms of the chromophore at 1.5 and 4K, and the spectral diffusion broadening was measured in temperature cycling experiments between 4 and 30 K. The inhomogeneous linewidth for the tautomeric 0 <-- 0 bands was estimated to be 60-70 cm-1; the hole width was found narrow, being in the order of 350 MHz (10(-2) cm-1) at 1.5 K what allowed for an extremely sensitive detection of the conformational changes. Though proteins have many features in common with glasses, the spectral diffusion broadening of photochemical holes under temperature cycling conditions in mesoporphyrin horseradish peroxidase has a very different pattern as a function of temperature. Up to 12 K, the linewidth did not significantly change, then around 14 K, a steplike broadening was observed for all three tautomers, although to a different extent. The total magnitude of line broadening up to 30 K was large and also different for the tautomers. We argue that the difference between the behavior of this protein and that of glassy matrices originate from finite size effects; the protein may be characterized by a small number of TLS, and their distribution may bear discrete features.
引用
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页码:305 / 312
页数:8
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